BioQuakes

AP Biology class blog for discussing current research in Biology

Category: Student Post (Page 1 of 57)

The Potential End To COVID-19: How An Antiviral Pill Could Decrease Death Rates

When will the world return back to normal? In recent years, people have questioned the longevity of the COVID-19 outbreak. While concentrating on vaccine delivery and vaccination capabilities, a pill has been developed in the hopes of preventing future COVID variations. Hopefully, the pill will eventually be administered to patients; this would make it the first oral treatment for the virus.

A current study on molnupiravir, an antiviral pill, has published data demonstrating that the medicine has the ability to lower hospitalization and fatality rates as a result of COVID-19. The study dealt with two groups of people. One group of 377 people were given a placebo, and the other group of 385 people were given molnupiravir to examine how the antiviral affected patients with COVID-19. The findings were substantial. Within 29 days of starting the trial, 14.1 percent of the group given the placebo were hospitalized. Fortunately, of the individuals who were given molnupiravir, only 7.3 percent of them were hospitalized.

Molnupiravir is a prodrug of N4-hydroxycytidine (NHC), a nucleoside analog (meaning that it contains a sugar and a nitrogenous base). Molnupiravir metabolism

Molnupiravir is similar to the genetic coding of the coronavirus’s RNA, as is remdesivir (a FDA-approved medication). By interfering with the polymerase enzyme, the “fake” basic elements impair the coronavirus’s RNA synthesis, preventing the virus from replicating. Despite the fact that the two medications serve the same goal, they serve different actions. Remdesivir penetrates a growing RNA strand, slowing and ultimately blocking the polymerase enzyme. Unlike the COVID-19 vaccine, the structure of molnupiravir gives it the ability to target the polymerase enzyme instead of the virus’s spike protein. Molnupiravir enters the cell and is transformed into RNA-like building components. The active medication binds to the genome of RNA viruses, setting off a chain of mutations; this process is known as viral error catastrophe. In simpler terms, it disrupts how the virus replicates RNA.

Molnupiravir could theoretically be administered as soon as a patient receives a positive COVID-19 test, thereby preventing floods of COVID-19 patients from overburdening medical systems while the highly infectious delta variant continues to spread. Although the side effects of the drug remain unknown, it has been reported that the side effects of COVID-19 are much worse than those of molnupiravir. The antiviral drug has the potential to save lives, but the primary concern is about the long-term repercussions. When contemplating molnupiravir, the fear of birth abnormalities or cancer comes into play because it is a mutagenic medication. In response, the drug’s creator, Merck, stated that there is no indication of the possibility for mutagenicity. Although the manufacturer is confident in the treatment and believes that the long-term consequences are insignificant, it is logical that parents might have concerns about molnupiravir.

Ultimately, if patients receive the vaccination that targets the spike protein and are also able to take molnupiravir, hospitalization and mortality rates may dramatically reduce.

Smelling Saves Lives!

Using a Novel technique, researchers at Karolinska Institutet in Sweden have been studying the brain and how our central nervous system judges a smell to represent danger. Our brain can distinguish between millions of different smells because of the olfactory organ. The olfactory organ is located in the walls of the upper part of our nasal cavity. Most of these smells are associated with a threat to our body’s health. After inhaling an odor it takes between 100 and 150 milliseconds to reach the brain. The detection and reaction of a smell has always been an important factor in all mammals’ survival. The researchers at Karolinska Institutet’s study has proven that negative smells are associated with unrest and are processed earlier in the brain than positive smells.Anatomy and physiology of animals Olfactory organ the sense of smell

Unpleasant smells trigger a physical avoidance response. The avoidance response has always been seen as a conscious cognitive process but recent research has proven that it is actually an unconscious and rapid process.

For a long time it has been a mystery as to which mechanisms in the brain are involved in the process of associating an unpleasant smell with danger and causing avoidance behavior in humans.The researchers at Karolinska Institutet have come up with a process in which you can measure signals from the olfactory bulb. The Olfactory bulb transmits signals to the part of the brain that controls avoidance behavior. Avoidance behavior can be described by a number of patterns, one of those patterns being a pattern of protective reflexes.

Three experiments were conducted where participants were asked to give their opinions on six different smells. The associate professor at the Department of Clinical Neuroscience shares that “the results suggest that our sense of smell is important to our ability to detect dangers in our vicinity, and much of this ability is more unconscious than our response to danger mediated by our senses of vision and hearing.” 

In AP Biology class, we learned about protein receptors. Smelling relies on protein receptors recognizing specific ligands. Humans are able to distinguish thousands of different compounds by smell. The shape of a molecule is most responsible for its smell rather than its physical properties. Thus, the smell relies on the interaction with a binding surface, usually, a protein receptor. 

It is so interesting how our bodies can distinguish the smallest differences in molecules. These differences can change the smell of something completely. These smells also help to determine our emotions. Smelling something bad can make us uneasy or feel unsafe while smelling something good can bring us joy. Can you think of a scenario where a smell made you feel unsafe?

Is the Solution to Climate Change in your House? Ask Aloe Vera!

With temperatures rising each year, the future of our environment is in danger.JMP 4280 XR (48940003233) As the scientific issue of climate change has turned political and economic, limited action has occurred in a time where an immediate change is needed to reverse the effects of global warming. However, researchers from the Natural History Museum in Denmark and the University of Copenhagen’s Department of Plant and Environmental Sciences are looking toward aloe vera as plants that may help fight this battle.

 

Such household succulents are renowned for their ability to go long durations of time without water; in other words, they survive periods of drought. TAloe vera 101hus, scientists recognize aloe vera as a teacher to ways plants may survive in a warming world. In aloe vera’s structure, hydrenchyma tissues in the aloe’s leaves, in conjunction with the plant’s overwhelming composition from carbohydrates, help aloe manage water in their system. Carbohydrates – comprised of carbon, hydrogen, and oxygen – are organic compounds found in sugars and starches. In their complex (or polymer) form, polysaccharides may perform a structural function. Specifically, cellulose is a carbohydrate that comprises a plant’s cell walls.

 

The study relays how aloe vera plants adjust their cell walls when there is a lack of water (a drought) to help them survive. In extremely hot temperatures, the plants respond by folding their cell walls closer together. Here, the plant maximizes its resources for survival. Thus, the aloe may shrivel, ceasing its growth, and reallocate its energy/resources to root growth (from water in the soil). Conversely, when there is plentiful water and they become rehydrated, normal activity resumes as the aloe vera reverts to its original state.

 

Within the context of employing the aloe vera’s techniques in a real-world situation, the scientists’ experiment further aims to find a link between the composition of carbohydrates in these succulents and the folding of their cell walls. If a connection is discovered, theyEberndorf Gablern Maisfelder und Saualm im Hintergrund 18082015 6749 hope to utilize similar strategies in crops so they can survive periods where their environment may be hot and dry. I am hopeful that other plants can mimic the aloe’s techniques because crops and succulents share many similar qualities to aloe in their composition. Nonetheless, I also recognize this may take time and generations of crops to find a concrete solution. Though the implications of this study are not yet comprehensible, they hint that we may soon be a step closer to combatting climate change.

 

What do you think? Are the teachings of aloe vera a hopeless grasp at a solution to climate change or the pathway to our future?

A New Way to “Tangle” with Diseases? British Scientists Think They’ve Stumbled Upon the Future

A team of scientist from the Universities of Bath and Birmingham have made a discovery that is making noise in the world of Biology. Ironically, they had the realization while studying silent mutations in DNA. What they found is a new method of evolution. Well not a new method per say as the scientists predict this method is being used in all forms of life; however, new in the sense that it was only recently realized. What they have discovered is a trend of tangles in DNA strands. This tangling occurs in DNA strands that are not in a double helix as DNA typically is. However The DNA strands are separated during copying. This task is done by DNA polymerase enzymes. During the copying process, the enzymes are often disrupted by the tangles in the strand. The resulting skipping of genes causes specific mutations to the DNA.

DNA replication split horizontal

The scientists then tested their hypothesis by way of experiment. They did so by studying the evolution of soil bacteria called Pseudomonas fluorescens (SBW25 and Pf0-1). They began by removing the gene that give the bacteria the ability to swim. They then observed the re-evolution of the strains to regain the ability swim. Both strains evolved quickly; however, there was a clear differences in predictability. One strain (SBW25) mutated the same part of a particular gene in every trial. The other strain (Pf0-1) varied in which gene and where the mutation occurred in each trial. Upon further observation, this contrast coincided with a hair-pin shaped tangle in the SBW25 strain. As the DNA polymerase enzymes would pass this tangle they would be effected in a predictable manner that would disrupt copying of DNA and result in a mutation that allows for the bacteria to swim. The scientists tested the theory by removing the tangle. They did so using 6 silent mutations so that the DNA sequence would not have a relevant change. The trials after the change showed that both strains showed inconsistent areas being mutated.

 

DNA are the dictators of protein synthesis in the body. The DNA sequences code for the types of proteins that are created. Proteins perform many of the bodies function. This means that even the slightest change in the sequencing of DNA can have major effects on the functioning of a human body or any organism. The process of evolution was thought to be caused by random errors in DNA sequencing that coincidentally gave an organism a survival advantage. These mutations would then be tested in the concept of survival of the fittest. While this is still thought to be the most prevalent form of evolution, especially with eukaryotic organisms, the tangling of DNA strands proposes a form of evolution that would be easier to study and predict.

 

The predictability of such a phenomenon is where the intrigue in viruses arises. “If we knew where the potential mutational hotspots in bacteria or viruses were, it might help us to predict how these microbes could mutate under selective pressure.” says Dr. Tiffany Taylor, from the Milner Centre for Evolution. Mutational hotspots have already been found in cancer, and the new information on their significance is getting scientists excited about the opportunities present. The new ways to understand and predict evolution of bacteria and viruses may allow scientists to be a step ahead on vaccines and be able to anticipate and understand new variants. It’s hard not to think this information would’ve been nice before the rise of SARS-CoV-2.

Synthesizing More Durable Bulletproof Vests Using Animal Muscle Fibers!

Wait, why? Are Animals harmed? These two may be the first two questions that arise after reading the title. Rest assured that no animals will be harmed since the organism producing these muscle fibers will be engineered microbes. A group of researchers at Washington University’s Engineering school conducted this research that leads to the production of stronger clothing that is more durable which makes it more sustainable because we are no longer using traditional materials like cotton, silk, and nylon.

First, what are Microbes? The National Center for Biotechnological Information states that Microbes are tiny living things that are found all around us and are too small to be seen by the naked eye. “They live in water, soil, and in the air. The human body is home to millions of these microbes too, also called microorganisms. … the most common types are bacteria, viruses, and fungi.” There are many different types of microbes, and there are some that are prokaryotic cells and others that are Eukaryotic cells. The difference between the two is that prokaryotes don’t have a nucleoid region while Eukaryotic cells contain a nucleus that stores DNA. Interestingly in prokaryotes, their DNA is circular-shaped while eukaryotes have linear DNA. In this particular study, they used bacteria, a prokaryotic single-celled organism.

E coli at 10000x, original

Picture of Microbes

Challenge 

 Through synthetic biology, this team modified bacteria so that the microbes were able to synthesize protein to produce muscle fibers. Synthetic biology is where “engineering principles are mixed with biology.” Well, to produce the proteins for muscle fibers, microbes must have ribosomes that synthesize amino acids and combine them to form protein chains. In this particular case, the protein they are synthesizing is titin. “It’s the largest known protein in nature,” said Cameron Sargent, a researcher on the team. It normally consists of 34,350 amino acids.

One of the problems the researchers overcame was controlling how the microbes were able to produce proteins “50 times” the average protein size. They utilized synthetic chemistry on the microbe they engineered to polymerize proteins and form many peptides and other bonds in the process. Peptide bonds, specifically, are covalent chemical bonds linking two consecutive amino acids.

201405 skeletal muscle

Muscle Fibers

My Take

I think this research is very advanced with regard to synthetic biology. If we further develop this field of science, in the future we might be able to synthesize more complex protein structures with simple microbes. I don’t see any bad implications that this research might have on society. I can’t wait to see what Professor Zhang and his team will produce in the future. Sargent  even said, “we can take proteins from different natural contexts, then put them into this platform for polymerization and create larger, longer proteins for various material applications with a greater sustainability.” With applications that are only limited by our imagination, I want to commend Professor Zhang and his team’s effort.

Points to Ponder and Comment:

If clothing were designed out of muscle fibers ethically, would you wear it? Why or why not? What uses do you have envisioned for this field of science if it continues to advance?

Smoking Can Harm More Than Just Your Lungs

When you think of the damage smoking does to your body, you think of your lungs, right? Well, did you know that smoking can actually harm your eyes?

Tobacco has previously been proven to be linked to many leading causes of blindness and vision impairments such as cataracts, glaucoma, and macular degeneration, but all of these effects occur in the inner part of the eye. A new study shows that smoking can actually harm and kill cells on the surface of your eyes.

Research from a recent study conducted by Wataru Otus, a biomedical researcher at the Gifu Pharmaceutical University in Japan, and his colleagues, published by Scientific Reports, found that the compounds found in the smoke of cigarettes and smoking devices cause an iron buildup in the corneal epithelium (the outer layer of corneal tissue on the eye), which can harm and kill cells.

In the study, the researchers exposed human epithelium cells to smoke extract of a cigarette as well as that of heated tobacco devices, and recorded their observations. The researchers found that after 24 hours, more cells that were exposed to cigarette and heated tobacco smoke were killed than those not exposed. They also found that smoking tobacco or using heated tobacco devices caused damage to the cells of the outer eye regardless of nicotine or tar being involved.

The cells that were exposed to tobacco products had damaged cell membranes, lumps of iron, and a lot of damaged ferritin, which strongly indicated ferroptosis, a form of programmed cell death.

Ferroptosis human prostate cancer modelFerroptosis occurred when the compounds in the tobacco made contact with the cells on the outer layer of the eye. The compounds caused the ferritin proteins inside the cells – which store and release iron – to break down and release the iron they were storing. Some of the iron that was released bunched up and produced hydroxyl radicals. Hydroxyl radicals are known to be a very reactive species that attacks organic molecules by removing or deteriorating them. In this case, the hydroxyl radicals attacked the lipids in the film on the surface of that eye, an event called lipid peroxidation. When these lipids are attacked and/or destroyed, your eye is much more likely to dry out, because lipids help prevent the eye from drying out due to their role as lubricators. This is why smokers tend to suffer from dry eye syndromeWhen too many radicals accumulate and are damaging the lipids in the cell membranes, cells can die. The death of eye cells (aka photoreceptors) can lead to the loss of or impaired vision.

As a solution in the study, the researchers found that by adding chemicals that are known to block ferroptosis to the human epithelium cells, more cells exposed to tobacco were able to live, suggesting that ferroptosis treatment could help smokers suffering from eye problems.

Moreover, ophthalmologist Dilek Altinörs of the Başkent University in Turkey, who has studied the results of this study, also suggested that smokers experiencing eye problems should use tear drops with ferroptosis blocking compounds. Although, further study needs to be done on the effects and successfulness of this treatment method. 

The findings of the study help one understand how and why it is that cigarette and tobacco devices affect the eyes of smokers, and show treatments for ferroptosis as a possible treatment for smokers’ having eye troubles. But the obviously best way to prevent smoking from harming your eyes is to not smoke at all. Having smokers learn and understand this new information will hopefully show them yet another reason why smoking is harmful, and why it is in their best interest to quit. 

Progress Towards Solving a 50-year-old Problem in Biology

Protein structures revealed at record pace

One of the hardest problems in biology is predicting the structure of a protein. Proteins are complicated. There are many interactions  between both the side chains and backbones of the proteins, making it very difficult to predict how a protein will fold into its 3D structure solely based on the amino acid sequence (primary structure). In our AP Biology class, we talked extensively about how this 3D (tertiary) structure of the protein is extremely important as it determines the function of the protein. For example, the success of the delta variant of SARS-CoV-2 is largely due to the change in the tertiary structure of it’s spike proteins. Thus, if the 3D structure of a protein is known, it is much easier to predict the function of that protein, and how well it performs the function. However, the methods of determining the tertiary structure of proteins is extremely costly. To determine the structure of a single protein, it can take up to $120,000 and one year.

AlphaFold 2.0 is a breakthrough in this long thought impossible problem. AlphaFold, created by Deepmind, uses deep learning to predict protein’s tertiary structures. In particular, it uses an architecture of transformers, a relatively new and increasingly popular deep learning technique. Using this method AlphaFold is able to achieve remarkably accurate and detailed results, even on an atomic level.

Because of its ability to predict the structure of unknown proteins, AlphaFold can be used to determine how a single nucleotide mutation can affect the structure of a protein. Interestingly, many diseases result from an improperly folded protein, these include: Cystic Fibrosis, Alzheimer’s, and Parkinson’s. While the protein structures themselves do not often lead to the creation of new treatments, they do offer a better understanding of how the protein works. This deeper understanding can then be used to develop new therapies. Thus, AlphaFold has the potential to accelerate new treatments for many untreatable diseases at a much lower cost.

In addition to diseases resulting from misfolded proteins, AlphaFold can be used to predict the effect mutations will have on the folding of the SARS-CoV-2 spike proteins. This can help to quickly determine how a mutation will change the shape (and thus function) of the spike proteins. This makes it much easier to predict how these mutations will affect the spread and severity of the new variants and, using this info, classify the new variants.

However, AlphaFold is not perfect. While most predictions are quite good, a small percentage of the protein structures generated are clearly  inaccurate, putting hydrophobic amino acids on the outside of the protein. Knowing this, it is still necessary to analyze any prediction made by the computational model before using it for biological analysis.  Nonetheless, AlphaFold is a powerful tool for prediction of protein structure and will revolutionize the field of computational protein structure prediction.

If you want to experiment yourself with AlphaFold, a working notebook can be found here. Any PDB sequence can be queried, and the AlphaFold model will predict the structure to the best of its ability.

 

 

Did You Inherit Stress From Your Mother?

Have you ever wondered why you are so stressed? Maybe because of school, sports, or homework, but have you ever thought you could have inherited from your mother? I bet not. Biologists at the University of Iowa found that roundworm mothers subjected to heat stress passed the stress exposure to their offspring and their offspring’s children. 

C elegans maleStress2a

In a study last year researchers looked at how mother roundworms react when she senses danger, such as a change in temperature. Their results were that the mother ringworms release serotonin when she senses dangers by traveling from her nervous system to warn her unfertilized eggs.  The warning is there “stored”, and then passed to offspring. Genes have “memories” of past environmental conditions that affect their expression even after these conditions have changed. It is still unclear how this “memory” is established, how it persists past fertilization and after the embryo develops into adults because most organisms typically reset any changes that have been made to genes’ past activity. 

The research team turned to the roundworm, a creature regularly studied by scientists, for clues. They exposed mother roundworms to unexpected stresses and found the stress memory was ingrained in the mother’s eggs through the actions of a protein called the heat shock transcription factor, or HSF1. The HSF1 protein is present in all plants and animals and is activated by changes in temperature, salinity, and other stressors. Although protein can be found in both Prokaryotic and Eukaryotic cells, this particular protein is only found in Eukaryotic cells which means that it interacts with numerous things found in these types of cells. HSF1 interacts with mRNA processing, chromatin modification, transcriptional coactivators and corepressors, and DNA and RNA metabolism which are all an array of proteins with diverse cellular functions. As we learned in biology, proteins nearly have every task of cellular life, including receiving signals from outside of the cell and mobilizing intracellular response which explains why the HSF1 protein has many functions.

The team found that HSF1 recruits another protein, an enzyme called a histone 3 lysine 9 (H3K9) methyltransferase. This normally acts during embryogenesis to silence genes and erase the memory of their prior activity. However, the research team observed something else entirely. They found that HSF1 collaborates with the mechanisms that normally act to ‘reset’ the memory of gene expression during embryogenesis to, instead, establish this stress memory. One of these newly silenced genes encodes the insulin receptor, which is central to metabolic changes with diabetes in humans, and which, when silenced, alters an animal’s physiology, metabolism, and stress resilience. Because these silencing marks were found in offspring, their stress-response strategy was switched from one that depended on the ability to be highly responsive to stress, to relying instead on mechanisms that decreased stress responsiveness but provided long-term protection from stressful environments.

What the team concluded was that if the mother was exposed to stress for a short period of time, only its offspring would be subjected to stress in utero, but the offspring’s children would not. If the mothers were exposed to stress for a longer period of time, then the offsprings children would retain this “memory” of  stress.

 

Have There Ever Been Oceans on Earth’s Sister Planet?

Venus, commonly referred to as the volcanic planet, also known as Earth’s sister planet, is the second closest planet to the sun. The planet’s surface is currently known to be the hottest in the solar system due to its dense atmosphere which traps in an immense amount of heat. This characteristic of Venus is actually very similar to how Earth’s greenhouse effect traps in warm air, keeping our planet warm; however, Earth also has oceans that cool the atmosphere, thus allowing for life to flourish.  Recently, research has been conducted to get to the bottom of whether or not Venus has actually ever had oceans.

Venus dome 3D

From a distance, Earth and Venus are strikingly similar: both around the same size, with a rocky surface and an atmosphere. As mentioned previously, Venus’ atmosphere traps in far more heat than Earth’s. In addition to having a very thick CO2 atmosphere, Venus also has sulphuric acid clouds which Earth does not. Life simply cannot exist on Venus due to the intense atmospheric pressure and the extreme temperatures created by the trapped heat. An article by Charles Q. Choi and Chelsea Gohd entitled “Venus: The hot, hellish & volcanic planet” gives more information about the nature of Venus’s surface. Choi and Gohd stated that Venus has the heaviest atmosphere out of all the planets in the solar system which causes its pressure to be about 90 times that on Earth. They mentioned a similar study also exploring the possibility of oceans on Venus. It concludes that the ultraviolet radiation, from the sun, as it grew closer, caused the water vapor molecules in the atmosphere to split apart, thus allowing for the hydrogen molecules to escape into space. This was the cause of the build-up of CO2 in the atmosphere that then lead to the current-day conditions of the planet. Unlike Earth, Venus has very strong winds and is primarily a dry desert land with many active volcanoes. Contrastingly, Earth’s surface is 70% water and is covered with dirt and plants. We can understand the similarities between Earth and Venus when we dig underneath all that dirt and ocean. Earth happens to have the same rocky surface that Venus has that came from cooled lava billions of years ago. To learn more about Earth’s surface, click here.

Venus Earth Comparison Horizontal

Theories have formed that Venus was once a far more inviting planet with potential for life. The National Centre of Competence in Research (NCCR) PlanetS and the University of Geneva (UNIGE), leading a team of astrophysicists, thoroughly explored whether Venus could have actually experienced milder days. Unfortunately, according to the results of the study posted in the journal Nature, this was not the case. Martin Turbet and his team of astrophysicists used the tools available on Earth to come to a conclusion.  They created a three-dimensional simulation of both Earth and Venus in their early stages when their surfaces were still molten and any present-day water would have been vaporized. They used the simulation to then evaluate how the evolution of the plants would play out. By examining how the atmospheres evolved, they can determine whether or not it was possible for oceans to have formed in the process. Marcus Turbet concluded that “Thanks to our simulations, we were able to show that the climatic conditions did not allow water vapour to condense in the atmosphere of Venus.” Due to the level of heat in the planet’s atmosphere, the water vapor was never able to cool to the point where it would form water droplets and fall to the surface; therefore; it remained in the gaseous state and never formed oceans.

As we learned in AP Biology this year, water (H2O) plays a huge role in life on Earth and it makes sense that other planets, such as Venus, that lack liquid water, would not be able to support life. We discussed that one of water’s main properties moderating temperature. Due to water’s unusually high specific heat,  its temperature changes less when it loses or absorbs a certain amount of heat. Life can exist on Earth because Earth’s oceans are able to moderate and control any temperature fluctuations that happen on land to keep the atmosphere in ideal condition for life. Water also has a high heat of vaporization which, again, aids life on Earth. Oceans absorb heat, and as some water evaporates, it condenses and then falls back to Earth in the form of rain, thus cooling the surface. On a much smaller scale, this can be related to how humans sweat (sweat representing the oceans and humans representing a planet). I run a lot, which means that I also sweat a lot, especially in the summertime when the temperature starts to rise. The sweat being 99% water means that it offers the same cooling effects that pure water does. The liquid on the surface of my skin allows my body temperature to be lowered so I can still feel cool enough to continue on my run. Hopefully, this aids our understanding of how oceans could never have existed on Venus because the water vapor was unable to become cool enough to transform into its liquid state and moderate the temperature of the planet. Venus’s surface is left to be rocky and full of volcanoes while Earth’s surface is able to support an immense amount of life.

The Common Misconception Around Antibiotics & New Findings

Gfp-medicine-container-and-medicine-tabletAntibiotics as a treatment are never fun – not only are you most likely dealing with a bacterial infection, but you need to take them on a strict cycle and can be quite aggressive on your stomach. I once had to go on antibiotics for treating a sinus infection, and it didn’t quite make me feel better after taking it. So after, I went on the same antibiotic, Cefuroxime, and took a higher dose, but I was not consistent in taking it and started feeling ill. This reaction was due to the antibiotics impact on the protective bacteria in my stomach’s microbiome. I soon learned more about the effects the antibiotics had on my stomach’s microbiome, and realized the common misconception around antibiotics – that they only benefit one’s health – and how some of the symbiotic relationships with bacteria in there are essential to digestion and immune protection. 

Biological overview

Antibiotics have been around since 1928 and help save millions of lives each year. Once antibiotics were introduced to treat infections that were to previously kill patients, the average human life expectancy jumped by eight years. Antibiotics are used to treat against a wide variety of bacterial infections, and are considered a wonder of modern medicine. However, they can harm the helpful bacteria that live in our gut.

The word antibiotic means “against life”, and they work just like that – antibiotics keep bacterial cells from copying themselves and reproducing. They are designed to target bacterial infections within (or on) the body. They do this through inhibiting the various essential processes we learned in Unit 1 about a bacterial cell: RNA/DNA synthesis, cell wall synthesis, and protein synthesis. Some antibiotics are highly specialized to be effective against certain bacteria, while others, known as broad-spectrum antibiotics, can attack a wide range of bacteria, including ones that are beneficial to us. Conversely, narrow spectrum antibiotics only impact specific microbes.

Antibiotic resistance mechanisms

The Human stomach is home to a diverse and intricate community of different microbial species- these include many viruses, bacteria, and even fungi. They are collectively referred to as the gut microbiome, and they affect our body from birth and throughout life by controlling the digestion of food, immune system, central nervous system, and other bodily processes. There are trillions of bacterial cells made of up about 1,000 different species of bacteria, each playing a different role in our bodies. It would be very difficult to live without this microbiome – they break down fiber to help produce short-chain fatty acids, which are good for gut health – they also help in controlling how our bodies respond to infection. Many antibiotics are known to inhibit the growth of a wide range of pathogenic bacteria. So, when the gut microbiome is interfered with using similar antibiotics, there is a high chance that the healthy and supportive microbes in our stomachs are targeted as well. Common side effects of collateral damage caused by antibiotics can be gastrointestinal problems or long-term health problems (such as metabolic, allergic, or immunological diseases). There is a lot of new research on the gut microbiome, some even suggesting that it impacts brain health by influencing the central nervous system. It is essential that we know more about how we can optimize its overall well-being.

New Research

Tackling the Collateral Damage to Our Health From Antibiotics

Researchers from the Maier lab EMBL Heidelberg at the University of Tübingen have substantially improved our understanding of antibiotics’ effects on gut microbiomes. They have analyzed the effects of 144 antibiotics on our most common gut microbes. The researchers determined how a given antibiotic would affect 27 different bacterial strains; they performed studies on more than 800 antibiotics.

The studies revealed that tetracyclines and macrolides – two commonly used antibiotic families – led to bacterial cell death, rather than just inhibiting reproduction. These antibiotic classes were considered to have bactericidal effects – meaning that it kills bacteria rather than just inhibiting their reproduction. The assumption that most antibiotics had only bacteriostatic effects was proven not to be true; about half of the gut microbes were killed upon being treated with several antibiotics, whereas the rest were just inhibited in their reproduction. 

These results expanded existing datasets on antibiotic spectra in gut bacterial species by 75%. When certain bacteria in the gut are dead, and others are not, there can exist an reduction of microflora diversity in the microbiota composition; this concept is referred to as dysbiosis. This can result in diarrhea, or even long term consequences such as food allergies or asthma. Luckily, the Researchers at EMBL Heidelberg have suggested a new approach to mitigating the adverse effects of antibiotics on the gut microbiome. They found that it would be possible to add a particular non-antibiotic drug to mask the negative effects the antibiotics had. The Researchers used a combination of antibiotic and non-antibiotic drug on a mouse and found that it mitigated the loss of particular gut microflora in the mouse gut. When in combination with several non-antibiotic drugs, the gut microbes could be saved. Additionally, they found that the combination used to rescue the microbes did not compromise the efficacy of the antibiotic.

It has been known for a while that antibiotics were impactful on gut microbiome, but its true extent had not been studied much until recently.  More time is needed to identify the optimal dosing and combinations, but the research coming from the Maier lab is very substantial as it fills in “major gaps in our understanding of which type of antibiotic affects which types of bacteria, and in what way,” said Nassos Typas, Senior Scientist at EMBL Heidelberg.

Yoga is Scientifically Good for You! Who Would have Known?

Yoga. A mindfulness practice first instilled by the Indus-Sarasvati civilization in Northern India over 5,000 years ago. To this day, yoga is practiced as a regular fitness activity by many but the real question lies in, is it actually good for you? Why? How? 

Kailash Integral Yoga

As a yogi myself, I am passionate, and maybe even slightly biased, to the enormous amounts of positives that come with the practice of yoga. On the surface, yoga is said to improve flexibility, muscle tone, and core strength. But, there are many benefits to yoga that lie beneath the surface of our bodies. Let’s start off with mental health. The concept of parasympathetic nervous system activation, is the activation of our ‘rest and digest’ state in our bodies. This activation is due to yoga’s practice of breathing and “single-pointed focus”. It puts our bodies into this rest and digest state and pulls us out of our agitated ‘fight or flight’ state, also known as the sympathetic state. Anxiety, a stress inducing mental health disorder, increases the secretion of stress hormones, like cortisol and adrenaline, in the body. This elevated secretion causes an unbalanced nervous system. Yoga’s inherent goal, as stated in Is Yoga Good For You?, is to bring our bodies out of chronic sympathetic activation, this reverses the negative effects of anxiety in the body, reduces the secretion of stress hormones, and rebalances the body’s nervous system. As we learned in AP Biology this year, steroid hormones are a type of lipid. Cortisol, a stress hormone Cortisolthat increases production when anxiety levels rise, is a type of steroid hormone. We know that lipids work as insulators, store energy, and form the plasma membrane. Anxiety, as I mentioned, increases the secretion of our stress hormones. Anxiety causes the cortisol levels to remain elevated in a stressful situation, this can lead to several health problems linked to high blood pressure, heart disease, etc. Considering all of this, yoga’s breathing tactics to calm the body actually lessen our symptoms of anxiety, depression, and stress and can be a very beneficial practice for someone who has anxiety. 

If the effects on mental health haven’t urged you to buy a yoga mat on Amazon just yet, keep reading. If they have, I recommend the link below 🙂 

Yoga is not only a beneficial tool for someone looking to improve their mental health, but it is a capable practice for all ages. Myths surrounding yoga say that it is only for the young, but studies have shown that yoga does improve the physical function and mental wellbeing of adults over sixty yeaYoga Barnstarrs old! It is a great tool for the elderly due to its ability to lower blood pressure levels and aid in our cardiovascular health. For young kids, though, yoga can be beneficial to calm down the overactive ones and/or ones with behavioral issues. Yoga is actually being implemented into many schools in the form of mandatory classes due to all of its positive benefits on young kids’ minds. As kids, the frontal cortexes of their brains are not fully developed yet so they are literally able to take in ideas, essentially more open minded and creative. This allows kids who take up yoga to appreciate it in a much different way, their innate curiosity can even lead them to creating coping mechanisms and life skills that would have otherwise not been developed says Pearce. 

So, is yoga beneficial for you? Though yoga can improve mental health, stress, and even help the elerdly, you don’t have to fall into any of these categories to participate in the practice. Yoga acts as a mood booster, stress reliever, strengthens flexibility, and provides you with an outlet of relaxation that you may not get in this busy world. Yoga is for everyone and the inclusivity of the yoga community will embrace you as you are; you don’t have to be “good” at yoga to participate either! Now, here is a link to buy a yoga mat… Come join me for hot yoga classes at Bikram Yoga in Roslyn, Namaste! 

If I wasn’t able to convince you to buy a yoga mat by now, please comment below and tell me why not!

 

Have We Discovered The Itchy Stitch?

A Brand New Poison Ivy Vaccine is in the Works; here is What We Know So Far.

Vaccine: The word spoken and heard by most Americans at least ten times daily this past year, yet not usually preceded by “Poison Ivy.” Working at Duke University, biochemist Sven- Eric Jordt heads a team of researchers investigating pain and itch mechanisms, studying the unpleasant sensations of Toxicodendron radicans, better known as poison ivy. Jordt reveals that contact dermatitis (the red rash received from poison ivy) is usually treated by local doctors and rarely shown attention or mass funding. Author of ‘A Vaccine Against Poison Ivy Misery Is In The Works,’ Claudia Wells states, “given the toll in suffering and dollars, you would think serious attention would be paid to this worsening public health issue, you’d be wrong.” When pharmaceutical companies recognized more money was to be made on drugs for chronic skin conditions like eczema, they felt no need to research effective treatments on a temporary rash.  

Toxicodendron radicans (poison ivy) 2 (49046043216)

Having never personally contracted poison ivy, I cannot describe the exact feelings of pain or irritation, but to quote a good friend, “it would be less painful for my skin to be set on fire.” Now I must state that this friend did have an extreme reaction to poison ivy, they pitched their tent in a field of the poisonous plant, yet severe reactions are more common than most might assume. Every year 10 – 50 million Americans contract poison ivy and suffer for an average of 2-3 weeks. Research obtained in a six-year study at Duke University found that an increase of carbon dioxide, i.e., climate change, causes the poison ivy plant to produce a more potent allergenic form of Urushiol, the resin responsible for the rash. With increased concerns regarding climate change, it appears odd that Jordt is one of few who take this rash seriously.

 Currently, the main treatment methods of antihistamines and cortisone cream do the rash very little justice. This is because our body’s reaction to Urushiol has no relationship to histamines, rendering antihistamines useless. In explaining this information to my dad, he agreed that all of the efforts recommended to him when he got poison ivy, a little less than two years ago, proved ineffective. To solve this, Sven Jordt and his colleagues began to analyze receptors that matched with proteins that showed inflammation from Urushiol.

In biology, receptors are proteins that receive signals by bonding with molecules known as ligands to send a specific message onward. A cell’s response depends on the types of receptors present, and each cell has its own number and type of receptor that allows them to act differently to various stimuli. Regarding poison ivy, Jordt and his team discovered that interleukin 33, an immune chemical in the body, is the main culprit behind the symptom of itchy skin. Jordt and his team of researchers are currently testing antibodies against IL-33, such as ST2, in primary sensory neurons. If ST2 could effectively block IL-33’s receptors, the necessity to scratch would virtually disappear. “This is all very new information,” Dermatologist Brain Kim, co-director of the Center for the Study of Itch & Sensory Disorders at Washington University in St. Louis, states. In the past, scientists believed that both the rash and itch from poison ivy were triggered by the immune system’s T cells. Further studies, however, have shown that the inflamed rash and itch sensation come from two different places entirely; It is believed “T cells do cause the inflamed rash of poison ivy but that these other pathways provoke the itch.” (Brian Kim)

 While human research has been challenging to complete due to a lack of study funding, a compound called PDC-APB, a small synthetic molecule derived from active urushiol components, is being developed into a vaccine to prevent painful contact dermatitis.

 As stated earlier, I have thankfully never had poison ivy myself, and I would like to keep it that way. As someone who goes on Sunday hikes through the woods with my family, contracting poison ivy is a constant fear of mine and leaves me wearing pants while walking in the July heat. I think a vaccine would be a fantastic option for someone who spends much of their time in places of possible poison ivy. The only question would be, is this the solution to our itchy problem?

 

WP20Symbols vaccine

This Parasite Can Change Agriculture for the Better

When parasites take control of a host, it may seem like all is lost for the unfortunate animal. However, a newly discovered parasite uses a mechanism that actually slows down plant aging, and may offer new ways to protect crops that were once threatened by diseases. 

Prior to this discovery, very little was known on how this parasite functioned on both a molecular and mechanistic basis. The Hogenhout group at the John Innes Centre and collaborators published in Cell have identified a manipulation molecule produced by Phytoplasma bacteria, which hijacks the development of plants. This protein breaks down key growth regulators, which as a result causes abnormal growth.

According to an article published by FronteirsIn, phytoplasmas and their associated diseases cause severe yield loss globally. For example, Aster Yellows cause major yield losses in crops such as lettuce, carrots, and cereals. As stated in the article, “Phytoplasma diseases of vegetable crops are characterized by symptoms such as little leaves, phydolly, flower virescence, big buds, and witches’ brooms.” These effects ultimately cause the host plants to die over time. 

Phytoplasma Growing on a Plant

Professor Saskia Hogenhuot said that “Our findings cast new light on a molecular mechanism behind this extended phenotype in a way that could help solve a major problem for food production.” One of these findings includes the bacteria protein entitled SAP05, which manipulates the plant’s molecular structure. This manipulation targets the process of the proteasome, which breaks down obsolete proteins inside plant cells. SAP05 causes the plant proteins that are used for regulating growth and development to be thrown out. With the absence of the proteins, the plant’s development favors the bacteria, which in turn triggers vegetative growth and pauses the plant’s aging process.

Specifically, SAP05 directly binds to the plant developmental proteins and the proteasome. Proteasomes hold a very important role in the cell regarding the degradation of proteins, with Professor Gonzalez writing, “proteasomes perform crucial roles in many cellular pathways by degrading proteins to enforce quality control and regulate many cellular processes such as cell cycle progression, signal transduction, cell death, immune responses, metabolism, protein-quality control, and development.” Conversely, SAP05’s direct binding is a newly discovered method of degrading proteins, unlike the usual fashion of proteins degraded by proteasomes that are tagged with ubiquitin beforehand. 

To further study SAP05, the research team wanted to see if SAP05 affects the insects that carry the bacteria plant to plant. Turns out, SAP05 does not affect the insects due to the structure of the host proteins in animals differing enough from plants. This research also enabled the team to identify the two amino acids in the proteasome that interact with SAP05. If these two amino acids in the plant proteins were switched to the amino acids found in the insect protein, they would prevent abnormal growth. 

In a polypeptide chain, every amino acid is important to how the chain functions. Specifically, an amino acid’s unique side-chain gives it different characteristics, which plays a role in how the protein is structured and its function in the cell. In this case, these two amino acids from plant to insect proteins ultimately change the way SAP05 interacts with the polypeptide chain, which as a result changes the effect. 

Personally, I feel that this discovery is groundbreaking since it enables countless possibilities regarding the prevention of mass yield loss. How do you think this research will be utilized in the future? Let me know in the comments!

Is Junk DNA Really Junk?

DNA is the base code of all living creatures. It is in every plant, animal, and single-cell organism, yet  50% of human DNA is seen to be irrelevant to bodily function. While some DNA is responsible for synthesizing materials within cells, much of it is in essence, spare genes, or ancient viruses that have become part of the human genome over time. Moreover, it has been debated whether the 50% of DNA that is not seen to be relevant is truly essential for survival. That is, can humans live without unused genetic code, or is it vital to the survival of the species?

Ácido desoxirribonucleico (DNA)

One specific element of junk DNA is transposons. Transposons are sequences of DNA that have the ability to mutate a cell or change its function as a whole. A study was conducted at the University of California, Berkley, and Washington University on transposons, as written in the So-called Junk DNA – Genetic “Dark Matter” – Is Actually Critical to Survival in Mammals, by the University of California, Berkley. The studies looked at a specific transposon in mice called MT2B2, one that controlled the growth rate of cells in a fertilized embryo, and when the embryo would implant in the uterus of the mother by initiating the short gene Cdk2ap1. When the researchers disabled the MT2B2 transposon using CRISPR-EZ, the mice created a longer version of the gene Cdk2ap2. This new version of the gene decreased cell growth and increased the period of implantation. The teams found that half of the baby mice died before birth without this transposon in their DNA. When the transposon was disabled, the mice sort randomly instead of uniformly in the uterus, and some may cause the death of a developed fetus and or the mother.

The team at Washington University researched the transposons turned on before embryos are impacted into the uterus in humans, rhesus monkeys, marmosets, mice, goats, cows, pigs, and opossums. The team used scRNA-seq, which records messenger RNA levels to indicate which genes are being used. With this technique,  the team saw that in every animal, a group of species-specific transposons was turned on. While the transposons were different for each species, the result of their use was nearly the same for all eight cases. Moreover, the gene Cdk2ap1 was expressed by all eight animals, but the amount of short and long versions of the gene expressed was unique for each one. While an animal that needs fast implantation uses more of the short version of the gene, like the mouse, animals with little to none of the shorter version of Cdk2ap1 took two weeks to longer for implantation to occur, like the cow.

Baby Mouse Rehabber

For these transposons to be promoting the expression of the Cdk2ap1 gene, at a certain point in history, a virus entered the organism and eventually part in a mutually beneficial symbiotic relationship with the organism until it evolved into the current iteration of the transposon. When viruses blend into the DNA of a species, they can be used to regulate and perform tasks that the cell could not previously perform. This can create a wide range of evolutionary options in species. Additionally, the main difference between the different genomes of species is the regulation of genes. By studying transposons, scientists can better understand differences in the genome of one species to another. With the understanding of this transposon, scientists could now begin searching further into junk DNA, as the removal of the transposon studies by the two universities proved lethal 50% of the time. Moreover, undiagnosed patients could have junk DNA mutations that lead to health problems, but those cases are currently a mystery to the medical world. Transposons are just the beginning of scientists dive into junk DNA, and who knows what wonders they will find next?

For Cancer Cells, it’s Halloween All Year Long– New Research Finds That They Masquerade as Normal Cells by Covering Themselves in “Sugary Costumes”

Dr. Rachel Willand-Charnley and her team of biochemist researchers at South Dakota State Univerity have achieved a “sweet victory” in cancer research. Their recent findings determine how cancer cells utilize sugar to deceit our immune systems. Their research suggests that cancerous cells mimic normal cells’ glycans due to genetic mutations, and because of this similarity, the immune system then confuses the cancer cell for a normal, healthy cell. This is because glycans on cell membranes of the cell are inspected by T-cells belonging to the immune system

Macs killing cancer cell

This is revolutionary to understanding the behavior and function of cancer cells which could help create more effective cancer treatments. Potential new treatment methods include stripping or altering the sugary layer of the cancer cell, allowing the immune system to recognize it as a threat and take care of it itself.

Milestones in cancer research are significant because as of right now, there is no cure for it. As we have learned in AP Biology, normal cells comply with signals that direct themselves into apoptosis, or programmed cell death. This process involves the expulsion of lysosomal enzymes into the cytosol which kills off the cell. This occurs when the cell is deemed inefficient or unable to function. If cancerous cells are detected by the immune system, those cells could avoid destruction by evading apoptosis signals and continue to progress within the human body which often leads to death. 

How could a cancer cell bypass something like this? Well, it seems that their newly adapted sugary coating could play a role in avoiding those signals. This is because T-cells from the immune system inspect glycans in the extracellular matrix for deviations. When deviations are present, an immune response is triggered, which could also trigger apoptosis of the deviated cell. So, the modified glycans on the cancer cell’s extracellular matrix help cancer evade a process like apoptosis.

Isn’t it astonishing that a single genetic modification could actually make cancers resistant to immunotherapy and chemotherapeutics? What do you think about this discovery?

 

“I Wanna Live Forever Young”

Aging: the inevitable… or so we thought. Don’t get too excited, aging is apart of every living organisms’ life, and it always will be. Besides growing old as a downside itself, the real worry of aging is all of the diseases that you grow prone too. But what if there was a way to change that? What if there was a way to grow old healthily? In this blog post, I am going to be explaining how cellular modifications can potentially change the future of aging forever.

In order to understand how to prevent aging, we must understand how aging occurs in the first place. One of the main causes of aging roots from the mitochondria. The mitochondria is the source of energy for the cell and is responsible for cellular respiration. It also is independent from the cell, so it has its own DNA known as mtDNA. As time goes on, exposure to toxic products within the cell begins to cause the mitochondria’s DNA (mtDNA) to mutate. The build up of this mutation in mtDNA eventually causes the cell to function improperly, causing respiratory chain disfunction and many cell degenerative diseases. Common diseases due to mtDNA mutations are Parkinson’s disease, Alzheimers, and Huntington’s disease. Mitochondrial dysfunction can also lead to the damaging of nerve function- another side effect of old age. In our AP Biology class, we learned about the significant role the mitochondria has on cell function and how it came to be apart of the cell through the Endosymbiont Theory. This theory mentions the mitochondria’s own DNA, which we are diving into today to understand the effects of genetic mutation in the mitochondria and how we might combat it.

Mitochondrion (standalone version)-en

 

Professor and disease research specialist Ming Guo dives into how we can achieve healthier aging by combating mtDNA mutation. The only way to do this would be to rid the cell of mutant mtDNA and restore mitochondrial function. In order to understand how to do this, Guo conducts an experiment with Professor Bruce Hay involving fruit flies. Fruit flies share 80% of their disease genetics with humans, making them a viable option to begin testing on. Guo observed that by forcing the cell into autophagy, the cell will remove damaged cell parts and therefore restore proper cell function. By starving the cell, the cell is forced to eat damaged parts of itself, including mutated mitochondrial DNA, in order to survive. The term “autophagy” can be broken in to two terms: “auto” and “phagy”. “Auto” refers to “self” and “phagy” means “eat”. In essence, autophagy means, “self eating”, as seen through the cells digestion of its own damaged parts. This gets inevitably prevents mutations of the cell that damage cognitive function and mobility that usually come with old age. In our AP Bio class, we also discussed autophagy, or the removal of waste from a cell through the use of lysosomes.

The findings of this study shed light on how to counter mtDNA mutation through triggering cellular processes, such as autophagy, at a more efficient level than the cell previously had.  On average, triggering autophagy in a cell gets rid of 95% of its mutated mitochondrial DNA. Guo and Hay’s findings are only just the beginning. Now that it is understood how to prevent mitochondrial DNA mutation, scientists must discover specific drugs on how to activate the cellular processes in a way that is safe, easy to administer, and available to the public. The answer to healthy aging, and longer lasting cognitive function that goes with it, is just around the corner!

I chose this topic because aging is inevitable for everybody, therefore it is relevant to every single person. Also, being that my family has a history with age related diseases, this topic particularly interests me. Ever since I was a kid, I would hear things like “You’ll be able to live to 200 the way technology is advancing” all of the time. This discovery is a huge step on making that statement a reality. Hopefully aging will soon become a less dreadful concept and people will live to be happier and healthier.

 

 

 

 

Your Inner Chimpanzee

 

Chimpanzees

What is the closest living relative we have (evolutionary speaking)? That’s right, chimpanzees!! Our evolutionary paths separated us about five to six million years ago leading to the chimpanzee of today, and us humans of the 21st century, but we still have much in common. Like humans, Chimpanzees use body language to communicate. They often kiss, hug, pat each other on the back, hold hands and shake their fists. They even laugh when they get tickled. At the same time, a lot has also changed. Not only do we stand on two legs and are relatively hairless, but we also have brains that function differently. 

 

Recent research from Lund University has found the answer to what in our DNA makes our brains different. Created by Shinya Yamanaka, the study used a revolutionary stem cell technique. Yamanaka discovered that if reprogrammed specialized cells can be developed into all types of body tissue. It was even recognized by the 2012 Nobel Prize in Physiology or Medicine. 

 

The researchers used stem cells grown in a lab. Their partners in Germany, the US, and Japan reprogrammed the skin cells. Then Johan Jakobsson, professor of neuroscience at Lund University, and his partners examined the stem cells that they had developed into brain cells. Using the stem cells, the researchers specifically grew brain cells from humans and chimpanzees and compared the two cell types. The researchers then found that humans and chimpanzees use a part of their DNA in different ways. This appears to play a significant role in the development of our brains.

 

What the researchers learned was different in part of our DNA they and I found so unexpected. Unlike previous research in the part of the DNA where the protein-producing genes are — about roughly two percent of our entire DNA, the difference that was found indicated that the differences between chimpanzees and humans appear to lie outside the protein-coding genes. The research found that it is actually located a so-called structural variant of DNA in what has been labeled as “junk DNA,” a long repetitive DNA string that has long been deemed to have no function. This was thought to have no function. 

 

This data suggests that the basis for the human brain’s evolution is a lot more complex than previously throughout genetic mechanisms, as it was supposed that the answer was in that 2 percent of the genetic DNA. These results indicate that the overlooked 98 percent is what has been significant for the brain’s development is instead perhaps hidden in, which appears to be important. 

 

Researchers hope to answer that question one day. But there is a long way to go before they reach that point. The question that now remains is instead of carrying out further research on the two percent of coded DNA should they delve deeper into all 100 percent. Even though exploring the missed ninety-eight percent is a considerably more complicated task for research. 

 

One question that also definitely still remains is why did the researchers want to investigate the difference between humans and chimpanzees in the first place?  

 

Well, Johan Jakobsson believes that in the future the new findings will prove his belief that the brain is the key to understanding what it is that makes humans human. How did it come about that humans can use their brains in such a way that they can build societies, educate their children and develop advanced technology? It is fascinating!” (Lund University). He hopes that this research will contribute to answers about things like genetically-based questions about psychiatric disorders, such as schizophrenia. As for me, I wonder if this continued research will tell us anything about how Chimpanzees will evolve. 

 

 

The Dark Truth of Athletic Industry: The Effects of Anabolic-Androgenic Steroids on the Brain

Decades ago, the use of performancing-enhancing drugs, or PEDs, had been reserved for use by only the most elite of athletes, including bodybuilders and competitive sports players. In this day in age, however, PEDs have become ubiquitous amongst not only competitive athletes, but also regular gym-goers. As they play such a drastic role in the betterment of athletic performance, the benefits of PEDS are not without a trade-off: they have innumerable dangerous health consequences that must be understood. 

But what are PEDs in the first place? The most common form of PEDs comes in the form of anabolic-androgenic steroids, or AAS, which are derivatives of the male sex hormone testosterone. In a performancing-enhancing context, AAS such as pure testosterone are used to increase systemic androgenic activity in the body, manifesting in the hyper-development of male sexual characteristics such as hair growth, acne development, low voice, muscularity, and libido. By taking AAS, athletes are also able to reap the competitive benefit of erythropoiesis, or the production of red blood cells, increasing athleticism and endurance. In addition to overall increase in testosterone, many forms of testosterone derivatives other than pure testosterone, have anabolic, tissue-selective properties, directly leading to an increase in muscle mass. By taking AAS, athletes are able to give themselves a competitive edge in beating their counterparts. 

However, the effects of AAS on the body also have overwhelming negatives. It is widely known that taking AAS in the form of exogenous testosterone can shut down endogenous androgenic activity, leading to symptoms such as shrunken testicles, breast tissue development, and low energy. In addition, a new study conducted by Oslo University Hospital suggests that AAS can also lead to premature aging of the brain

Due to their chemical structure, after being injected using a needle into the blood, AAS enter the brain very easily. As steroids, AAS are hydrophobic, non-polar molecules, meaning they are able to passively diffuse through the phospholipid bilayer of cells through passive transport, depending upon concentration. At Oslo University Hospital, Dr. Bjørnebekk and his colleagues lead a study to investigate the effects of AAS on brain aging by scanning the brains of patients with past AAS use and those without it using MRIs. In the study, Dr. Bjørnebekk tested the brain age gap, or the difference between a patient’s chronological age and their predicted brain age, with a high brain age gap marking a higher risk for cognitive disease. Across the board, the AAS group showed significantly higher brain aging, or higher brain age gap, than standard participants, illustrating the underlying risks involved with AAS use. 

While the detrimental effects of exogenous AAS abuse are widespread across the body, unfortunately, technology to aid in the success of PED-using athletes has been flourishing in recent years. As exogenous AAS use often leads to crashed endogenous testosterone production in men, PCT, or Post-Cycle Therapy, drugs have been created to help men regain normal endogenous testosterone production after exogenous steroid abuse. Since AAS users usually experience low testosterone and high estrogen levels, estrogen blockers, such as Clomid or Nolvadex, are used in PCT to regain natural hormonal balance. While this may address the acute hormonal consequences of AAS use, technology, as of now, has not yet been created to ameliorate the long-term effects of AAS use on the brain. Manifested in the higher incidence of brain age gap in AAS users in the study, the neurodegenerative effects of AAS cause neurons to gradually lose function and die, which is often permanent. In conclusion, while PEDs in the form of AAS do exhibit strong competitive benefits for athletes, their long-term negative consequences and role in the acceleration of neurodegeneration make using AAS an unwise choice. 

Depo-testosterone 200 mg ml crop

Muscle Regeneration: More Than Just “Tearing Muscle Fibers”

Have you ever felt sore after a workout? Maybe your muscles ache and you wonder why this is so? This soreness you are feeling is the result of the tearing of muscles fibers in your body. But the muscle repairing process isn’t as simple as “rebuilding muscles fibers.” It is a part of a chain of reactions and processes that our body triggers in perhaps the most fantastic biological response.

After an intense workout, your muscles are covered in microscopic tears. The easiest and most simple explanation for muscle growth is when you tear these fibers, they grow back stronger leading to stronger muscles. However, a newer study found the presence of scars surrounding the torn muscle fibers. I was totally shocked to learn that after we workout, we get mini scars on our muscles and not just fiber tears. As it turns out, bunches of nuclei go to the scars and begin to heal them. They trigger the release of mRNA which reads the DNA to make new proteins. Who knew that nuclei had something to do with the regeneration of muscles. However, the process of re building a torn muscle fiber is much more extensive than nuclei creating new proteins.

When we dive deeper we can see that there are many different levels to this process. The primary area of rupture after a workout are to the skeletal muscles. Skeletal muscles are laid out in sheets and are connected to bones by tendons. This type of muscle is responsible for a process called protein synthesis. When your body is undergoing an exercise, your muscles are constantly fed protein in order for the cells within your muscles to continue functioning properly and at a proper pace. When your workout concludes, it is vital to consume protein since protein stimulates and accelerates muscle repair and growth. For example, I consume a protein filled meal generally very soon after I workout, making sure I am getting the proper nutrients I need to help my muscles strengthen and prosper. The process of protein synthesis is imperative to muscle recovery and stamina, but if we look even closer into the recovery process we can see a couple of cellular organelles performing some impressive things.

According to the new study, two of the most important organelles in animal cells that is necessary for muscle regeneration is the mitochondria and the nuclei. The mitochondria’s function within a cell is to perform cellular respiration. Cellular respiration is the process where sugars are broken up into useful energy that can be used by the cell and eventually by the body. As we learned in biology class, the mitochondria ultimately converts the sugar glucose into ATP (Adenosine Triphosphate). ATP is essential for muscle regeneration post workout and during a workout because it is responsible for muscle contraction and movement. Just recently, we have learned that the nuclei also comes to the rescue for torn muscle fibers. Nuclei will arrive at the tear and then increase production for more myofilaments, the basis of myofibers. Traditionally, myofibers are the building blocks for muscle growth and rejuvenation. These myofilaments are consisted of small proteins that stimulate muscle movements. All in all, the addition of nuclei to the muscle rejuvenation process highlights the amount of energy needed by the body to perform these functions, which comes from the mitochondria and ATP.

Within the skeletal muscles are areas of high activity that consist of two main organelles doing most of the work: nuclei and mitochondria. The traditional forms of muscle rejuvenation with the mitochondria go hand in hand with the newest discovery of nuclei. In order for the muscle to rebuild it needs proteins and ATP. With the help of these two organelles, this accelerated process can successfully go through. The next time you get sore after a workout, take a second and admire that your body is hard at work with a task that is nothing short of mesmerizing.

Muscle Tissue Skeletal Muscle Fibers (41241952644)

The Importance of Gut Health: How to Live Long and Be Happy

Gut health – why is it so important? I had always thought that the concept of good gut health was a myth and only lived on the side of a bottle of Kombucha. I could not have been more incorrect!Kombucha, Health-Ade,

It turns out that a happy gut is critical to live a long, happy, and healthy life! The gut, also known as the digestive tract or gastrointestinal track, includes the mouth, esophagus, stomach, small intestine, pancreas, liver, gallbladder, colon, and rectum. Therefore, it processes all of the nutrients you take in, fights diseases, serves as a center for communication, and produces hormones. These are all critical tasks that affect your everyday well-being!

202004 Gut microbiota

When thinking about gut health, scientists are usually referring to the gut microbiome. In short, the gut microbiome is all of the microbiomes in your intestines. Humans would have a very hard time surviving without the gut microbiome. It digests breast milk when babies are first born, controls the immune system, digests fiber, and even helps control brain health. In fact, a recent study done with mice suggests that gut health affects social interaction/behaviors, stress, anxiety, and autism spectrum disorder. Additionally, in 2011 another study was done with mice, which involved antibiotics killing “bad” gut bacteria, also known as, gut flora. These mice became scientifically less anxious after killing the gut flora and “showed [positive] changes in their brain chemistry that have been linked to depression”  according to Live Science.

Gut flora is not the same for everyone. Another study done with gut flora showed that obese individuals tend to have less diversity in their gut flora when compared to lean individuals. This difference is because of an increase in Firmicutes and decrease of Bacteroidetes in obese individuals. Gut flora also affects an individual’s metabolism because of its affects on the breakdown of a key organic compound we have learned about in biology, carbohydrates. As we know, carbohydrates provide energy for the body which is imperative for all individuals. Another subject we have discussed in our class, amino acids, can have an increase in production because of gut flora (Live Science).

Now, you may be wondering, “how can I keep my gut happy?” The key to a healthy gut comes from diet. After an extensive amount of research, here are some tips I have gathered and why they work:

  1. Eat a variety of foods – to keep your microbiome diverse (recommended to eat specifically a variety of fruits and vegetables for fiber, vitamins, and minerals)
    Fresh fruits and vegetables in 2020 06
  2. Eat fermented foods (ex. yogurt, kefir, kimchi, pickles, sauerkraut) – it “can reduce the amount of disease-causing species in the gut” (Healthline)Vegan yogurt, March 2012
  3. Eat nuts, seeds, and legumes for fiber and proteinNuts on Spice Bazaar in Istanbul 01
  4. Eat whole grains for dietary fiberHome made whole grain bread
  5. Eat prebiotic foods (ex. bananas, artichokes, apples, asparagus, oats, flax seeds, garlic, onions, broccoli) – to “help boost the population and diversity of good bacteria” (Orlando Health)29 Nov 2011 - Apples and BananasThree Onion in Peng Chau
  6. Limit antibiotics – they kill both good and bad bacteria in the gut, which decreases necessary varietyAntibiotic pills
  7. Take a probiotic supplement – it “can help restore the gut to a healthy state after dysbiosis” (Healthline)Red and blue pill

These are all relatively small changes for the huge benefits that they reap. Start incorporating them today to improve your gut health and live a longer, happier, and overall healthier life!

 

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