BioQuakes – Page 5 – AP Biology class blog for discussing current research in Biology

Scientists have achieved a fascinating breakthrough by transplanting chloroplasts from algae into hamster cells, allowing them to photosynthesize and produce energy for up to two days. This experiment, recently published in Proceedings of the Japan Academy, Series B, could open new doors in biotechnology and cellular engineering.

Researchers from the University of Tokyo sought to replicate the mechanism in mammalian cells after being inspired by sacoglossan sea slugs, which naturally use chloroplasts from their algae diet to produce energy. The scientists used robust chloroplasts from red algae, which flourish in harsh conditions, to successfully transplant chloroplasts into fungal cells, although earlier attempts to do so quickly destroyed the cells.

After carefully separating the chloroplasts, the researchers changed the growth media to allow the hamster ovary cells to naturally absorb the organelles rather than putting them in using force. After entering, the chloroplasts remained structurally sound and carried out electron transport, which is an essential part of photosynthesis, for 48 hours before breaking down.

There are still difficulties in spite of this progress. Animal cells lack the genes necessary to support chloroplasts long term, and thus depend on protein assistance to function. By inserting genes linked to photosynthesis into animal cells, researchers hope to fix this issue and possibly extend the survival and utility of the cells.

Looking ahead, these findings could lead to groundbreaking applications such as photosynthetic materials that capture carbon dioxide or boost oxygen production in lab-grown tissues. However, as it would require an unfeasible quantity of surface area covered in chloroplasts, the idea of solar-powered humans is still unattainable.

In our AP Biology class, we have learned about the endosymbiotic theory, which explains how organelles like mitochondria and chloroplasts originated from symbiotic relationships between primitive cells. According to this theory, a larger host cell engulfed smaller prokaryotic cells capable of energy production, and instead of digesting them, they formed a mutually beneficial relationship. Over time, these engulfed cells evolved into organelles, such as mitochondria for ATP production and chloroplasts for photosynthesis in plant cells. This theory is supported by evidence such as the presence of their own DNA and double membranes.

The recent experiment connects to the endosymbiotic theory by demonstrating how animal cells can temporarily host chloroplasts and perform photosynthesis. It provides a modern-day parallel to the evolutionary process that occurred billions of years ago, suggesting that under the right conditions, symbiotic relationships could potentially be engineered in the lab. This research could deepen our understanding of cellular evolution and pave the way for innovative applications in synthetic biology.

Personally, I find this research incredibly exciting because it highlights how science can push the boundaries of what’s possible. Could we one day engineer cells to create their own energy from sunlight? What other possibilities might arise from blending plant and animal biology? I’d love to hear your thoughts—leave a comment!

Cholesterol Fighting Microbes: The true superheros

By almoeba

Did you know that your gut microbiome correlates to many different aspects of your health? Your oral health, mental health, and cardiovascular health, all correlate with the microbes in your gut.

Sneha Khedkar explains how certain microbes in the gut help protect against heart disease and lower cholesterol.

An increase in diversity of gut microbes has shown to decrease the chance of cardiovascular disease. The reason why: these microbes are able to break down cholesterol, a main component to heart disease. Researchers found that the enzyme IsmA was responsible for this.

After exploring a variety of microbiomes, researchers found that people with the IsmA enzyme have less cholesterol in their blood than those who didn’t or lacked the enzyme. Additionally, their was an abundance of Oscillibacter bacteria in the stool samples of people with lower triglyceride and cholesterol levels. After growing the bacteria in the lab and exposing it to cholesterol, the researchers found that like the IsmA enzyme it broke the cholesterol down.

The researchers then used a machine-learning algorithm, a type of artificial intelligence, to find that genes producing proteins similar to IsmA are likely responsible for helping Oscillibacter break down cholesterol. Through this, they realized that there are still many gut microbes with functions that are unknown.

Khedkar’s articles represents that ones gut microbiome may be more important to their health then one may think. With more research, altering ones gut microbiome may be the key to managing cardiovascular diseases!

In our AP Biology class, we recently learned the functions of enzymes. This gives us a better understanding of how enzymes like IsmA work. Enzymes are globular proteins that break down substrates. The substrates bind to the enzyme’s active site, ultimately altering the enzyme shape. This creates an induced fit to better enable the enzyme to break or build a bond. If the substrate is broken down, like the cholesterol with the IsmA enzyme, then hydrolysis is used creating a catabolic reaction. To build a bond, the enzyme uses dehydration synthesis, creating an anabolic reaction.

Enzymes are very interesting to learn about and a main component to our gut microbiome and overall health. Now we can only wonder, what other aspects does our gut microbiome influence. What aspects of our lifestyles impact our gut microbiome, and how does that impact our overall health? Could health issues like cardiovascular disease be healed through altering our guts? With more research, I hope we can find out!

Doritos? Dyes? Transparent Skin? The Surprising Future of Medical Imaging!

By eiszymes

Next time you reach for a bag of Doritos, remember—it’s not just the crunch that’s surprising. These chips can actually make your skin temporarily invisible, and scientists are using this to explore the human body in a whole new way!

This unexpected revelation about the food coloring, tartrazine (E102), has caught the attention of researchers who have found that it can make your skin transparent for a brief period of time. This process works by altering the refractive index of skin tissue, allowing light to pass through in a way that makes the skin appear see-through. This discovery is not only a fascinating science trick but also a potentially groundbreaking technique for medical research, allowing scientists to take a look into the body without typical invasive procedures. By using this method, they can observe internal organs and blood vessels more clearly, which could have applications in diagnostics, surgical planning, and even disease detection.

This is explored in an article in The Sun, where this innovation has caught the attention of many medical professionals for its potential. Researchers have been studying how tartrazine interacts with skin cells at a cellular level, and it’s believed that this could revolutionize how we visualize internal body structures. Just imagine: using such a simple substance as a food dye can allow doctors to see into your body without invasive procedures such as surgery.

The discovery of tartrazine’s ability to temporarily make skin transparent can be tied to the function of cell membranes, a concept we explored in our class. The process of light passing through the skin and revealing underlying structures is influenced by the interaction of tartrazine with the cellular membranes of skin cells. Membranes, which are composed of a phospholipid bilayer and embedded proteins, regulate what enters and exits cells, including substances like dyes or chemicals. When tartrazine interacts with these membranes, it can alter the way light refracts through the tissue. This demonstrates how membrane permeability and the properties of membrane-bound proteins play a key role in cellular interactions.

While researchers are still working to refine the technique, its potential is undeniable. As highlighted in Scientific American, advancements in the use of transparent skin are already being applied to the field of medical imaging. For example, studies have demonstrated that temporary transparency could aid in visualizing internal organs and blood vessels, offering doctors a new method to detect and diagnose diseases without the need for invasive procedures. It’s clear that this innovative approach could transform the future of non-invasive surgeries, improving accuracy and outcomes for patients.

The University of Texas at Dallas also highlights how this method is being tested on animals, like mice, to study diseases such as cancer. By making the skin transparent, scientists can observe the real-time effects of treatments on tumor growth, which could lead to more personalized, effective therapies.

The ability to make skin temporarily transparent using tartrazine is a game-changer for medical imaging. This breakthrough could improve diagnostics and treatment monitoring, offering a non-invasive method to study tissue in the body. As Technology Networks explains, this technique opens new doors for observing internal organs in real-time, potentially transforming how doctors detect and treat diseases. With further development, this approach could lead to safer and more efficient healthcare practices in the near future.

Now the next time you share a bag of Doritos with a friend you can tell them about how their favorite snack could contain the future of medicine!

What do you think? Could this actually be a regular medicinal practice one day? Let me know!

The Cleanup Crew: PLD3 and PLD4

By schwarzcells

Scientists at Scripps Research have made significant strides in their understanding of PLD3 and PLD4, two essential enzymes that break down nucleic acids such as DNA and RNA in cells. These enzymes aid in the prevention of nucleic acid accumulation. Nucleic acid accumulation can activate the immune system and result in autoimmune and immune disorders including lupus, Alzheimer’s disease and rheumatoid arthritis if left unchecked. Rheumatoid arthritis is a chronic inflammatory disease that can damage more than just one’s joints. This disease can affect a variety of body systems, including the skin, eyes, lungs, heart and blood vessels. PLD3 and PLD4 aid in the prevention of the diseases above by cleaning up the cellular environment and setting the threshold for what is considered an infection or not. Wow – I didn’t know these enzymes were so important to your health! Did you know about these enzymes?

The scientists were able to observe how the enzymes interact with their substrates during the degradation process by using X-ray crystallography to generate extremely precise, nearly atomic level models of these enzymes in different stages. X-ray crystallography first generates a photo that shows the pattern of diffracted x-rays, which scientists then use to develop a map of the enzyme’s molecular structure. Observing these models in various stages, the researchers found that both PLD3 and PLD4 use a two-step process to break down the nucleic acid. The enzyme first cleaves and links the DNA strand and separates a single nucleotide from the rest of the strand. Then, the enzyme releases this nucleotide.

Due to the fact that the enzymatic reaction described above occurs so quickly, the scientists used an alternative substrate to observe the enzyme’s structure during catalysis. The scientists incubated the enzymes together with a molecule that acted similarly to the substrate that the enzyme normally degrades (nucleic acid). However, the enzyme degrades this molecule much more slowly. After analyzing this slowed-down version of the enzymatic reaction between PLD3/PLD4 and nucleic acid, the scientists surprisingly discovered the function of phosphatase activity in both of the enzymes. How interesting!

The study also examined PLD3 and PLD4 mutations associated with diseases, specifically those connected to spinocerebellar ataxia and Alzheimer’s disease. While certain mutations led to reduced enzyme activity, making it more difficult to eliminate nucleic acids, others, including those associated with late-onset Alzheimer’s, enhanced enzyme activity. What a surprise! However, this increased enzyme activity seemed to lead to the instability and aggregation of the enzyme which are frequently linked to neurodegenerative diseases. After reaching these findings, the researchers are beginning to think about potential treatment plans. Some possible treatments include inhibiting the enzymes in cases where they are overactive. Other treatment ideas include replacing the enzymes in individuals who have non-functional versions of the enzymes. Can you think of any other possible treatment ideas that could work?

This article connects to AP Biology because it demonstrates the significance of enzymes. Enzymes are significant because they are vital to nearly every biological process due to the fact that they speed up chemical reactions that are necessary for life. More specifically, they are proteins that catalyze reactions, helping to break down molecules, build new ones, and maintain cellular processes.

However, as discussed in AP Biology, enzymes are susceptible to environmental influences such as temperature, pH, and substrate concentration. If these environmental factors are not within a specific range, the enzymes may not function to their fullest potential. For example, as temperature increases, enzyme function will increase until the enzyme ultimately denatures at a temperature that is too hot. When the temperature becomes too hot, the shape of the enzyme will change because the quaternary, tertiary, and secondary protein structures of the enzymes will be destroyed, leaving simply the primary structure (covalent bonds). Similarly with pH, specific enzymes have their own optimal pHs in which they can function best. If the pH deviates from this optimal pH, the increase of OH-/H+ will disrupt the quaternary, tertiary, and secondary protein levels of the enzyme and cause the protein to denature. In both of these cases, the quaternary, tertiary, and secondary protein levels were destroyed because their bonds such as hydrogen bonds, van der Waals interactions, disulfide bonds, ionic bonds, hydrophobic interactions are not strong enough to withstand extreme conditions. Lastly, substrate concentration can also affect the function of the enzymes. As the amount of substrate increases, the enzyme function increases until the enzyme function plateaus because the enzyme can only bind to so many substrates.

In the context of the study, when PLD3 and PLD4 activity is disrupted either by environmental factors or genetic mutations that alter their structure, nucleic acid accumulates which may lead to conditions like autoimmune diseases or neurodegenerative disorders. The study highlighted how mutations in these enzymes could reduce their activity or make them overactive, both of which could have harmful effects. Overall, the findings in the study emphasize the significance of understanding how enzyme function is influenced by environmental factors and other influences, as imbalances can contribute to dangerous responses such as disease.

Personally, this article made me even more grateful for my health. I realized that even little changes in my body could potentially cause major health issues. I am also grateful for the individuals who are researching about human health and improving society each day!

Penicillin Strikes Back

By prestandna

Penicillin has been a cornerstone in the fight against bacterial infections for over 80 years, but as bacteria evolve, many have become resistant to this once-unstoppable antibiotic. However, a recent breakthrough in research could help restore penicillin’s power against these resistant strains. This new discovery involves combining penicillin with an enzyme inhibitor to prevent the breakdown of the antibiotic by bacterial enzymes, offering a promising new strategy in the battle against antibiotic resistance.

The research focuses on a specific group of bacteria that produce an enzyme called beta-lactamase. This enzyme breaks down penicillin and other beta-lactam antibiotics, rendering them ineffective. However, scientists have discovered that when penicillin is combined with an inhibitor that blocks beta-lactamase, it can remain effective against these resistant bacteria. This finding is exciting because it doesn’t require creating entirely new antibiotics; instead, it enhances the effectiveness of an existing antibiotic by pairing it with a simple compound.

Beta-lactamase resistance has been one of the biggest challenges in treating infections with penicillin, but by inhibiting this enzyme, penicillin can work properly again. The compound used to inhibit beta-lactamase prevents the enzyme from breaking down penicillin, allowing the antibiotic to continue targeting bacterial infections. This discovery could dramatically improve treatment outcomes for patients battling antibiotic-resistant infections.

This approach is groundbreaking because it doesn’t involve developing new antibiotics from scratch, which can take years and cost millions of dollars. Instead, scientists are exploring how existing antibiotics can be paired with other compounds to boost their effectiveness. This could significantly extend the life of penicillin and other antibiotics, helping us stay ahead of evolving bacterial strains.

In AP Biology, we learned that penicillin functions as a co-factor for certain enzymes. A co-factor is a non-protein molecule that helps enzymes carry out their reactions more efficiently. This new discovery ties into that concept because it shows how penicillin not only inhibits bacterial cell wall synthesis but also interacts with enzymes like beta-lactamase to regulate their activity. Understanding penicillin’s role as a co-factor helps explain why it can be so effective at targeting bacteria, and why pairing it with enzyme inhibitors could restore its power against resistant strains.

The idea of co-factors—whether organic molecules like penicillin or metal ions—was something that I found particularly interesting in class. Penicillin’s role as a co-factor isn’t just about its antibacterial action; it also highlights how it interacts with bacterial enzymes to influence their behavior. Seeing how these biochemical principles are applied in real-world solutions is exciting, especially when it comes to addressing major health challenges like antibiotic resistance.

This topic is especially interesting to me because I’m allergic to penicillin. Learning about how it works as a co-factor in enzyme reactions and how recent research is finding new ways to combat resistance has made me realize how much more there is to learn about this antibiotic, even after so many years of use. It’s fascinating to think that penicillin still has the potential to evolve in response to antibiotic resistance, and this new research proves just how important it is to keep exploring its properties.

As antibiotic resistance becomes an increasingly global issue, this research offers hope for the future—not only in overcoming resistance but in finding smarter ways to use the antibiotics we already have.

What do you think about the recent discoveries regarding penicillin’s effectiveness against resistant bacteria? Do you think this research will help manage the growing issue of antibiotic resistance? I’d love to hear your thoughts in the comments!

Bacteriophages: The Surprising Fuel for Mammalian Cells

By emzyme

The human body is home to numerous microorganisms, forming a diverse ecosystem full of possibilities. These include bacteriophages, which are viruses that specifically target and kill bacteria. Despite the enormous number of these viruses in the body, nothing is known about how they interact with human cells until now. A groundbreaking study led by microbiologist Jeremy Barr reveals that mammalian cancer cells can use these bacteria-killing viruses as food sources. This surprising finding challenges long-held beliefs about how phages interact with human cells.

Jeremy Barr and his colleagues used human and and dog cancer cells in an experiment at Monash University in Melbourne, Australia. The bacteriophage T4 virus, which is known to infect and destroy E.coli bacteria, was abundant in the environment where the scientists cultivated these cells. Surprisingly, the phages caused changes in the cell that boosted growth instead of triggering the expected immune response. The cancer cells seemed to “eat” the phages, using them as a source of energy. According to Barr’s research, the viruses may be used as fuel by mammalian cells.

This research differs from typical biology. For years, researchers have been told that phages do not interact with mammalian cells. Barr’s research, however, indicates that this view is not correct, at all. The consequences could be significant, as they may imply that all mammalian cells, including both cancerous and noncancerous, could use phages as fuel. Even though the study used lab-grown cancer cells, Barr is eager to investigate whether this happens in noncancerous cells within living animals. In order to comprehend their broader influence on human health, he is also researching phages from other environments, such as the human gut!

In AP Biology, we have studied the processes of cell growth and energy production. For instance, during cellular respiration, cells break down molecules like glucose to produce ATP, which is the cell’s energy source. This new finding about cells consuming bacteriophages as a food source can be related to our knowledge of how cells obtain energy from different sources. The research tells us that cells are dynamic and continuously adapt to their surroundings in ways that we are still learning about.

In addition, the procedure also demonstrates important biological processes that enable cells to take in foreign materials, like phagocytosis and endocytosis.

Barr plans on exploring the bacteriophage’s function in the body in greater detail, with a focus on phage therapy. As antibiotic resistance increases, phage therapy, using bacteria to treat bacterial infections instead of antibiotics, is becoming more and more popular as a substitute. Barr’s research may potentially offer new insights into how phages may be used not only to fight bacterial infections but also in treating or understanding other complex diseases, such as cancer.

What do you think about using viruses as a food source for cells?

Can this change the way we think about diseases and the immune system?

How will this finding impact the future of medicine and the treatment of diseases like cancer?

Elderberry Juice: The Secret Ingredient for a Healthier Gut and Metabolism?

By aerna

According to a recent study led by Washington State University, elderberry juice, derived from the small, dark purple berries of the elder tree native to Europe, may play a significant role in weight management and metabolic health. This research, published in the journal Nutrients, highlights the potential health benefits of consuming 12 ounces of elderberry juice daily.

Personally, I wonder if the effects would be significantly reduced if elderberry juice was not consumed daily, as drinking it every day might be challenging for some people to commit to unless the benefits are truly life-changing.

In a randomized, placebo-controlled trial, 18 overweight adults consumed either elderberry juice or a placebo with similar taste and color for one week, while maintaining a standardized diet. Participants who drank elderberry juice showed remarkable improvements in their gut microbiome. Beneficial bacteria such as firmicutes and actinobacteria increased, while harmful bacteria like bacteroidetes decreased. Actinobacteria are especially important because they help maintain a healthy gut by breaking down nutrients and producing compounds that support the immune system. This positive shift supports better nutrient absorption and overall physical and mental health.

Would these results be as dramatic for someone who already had a healthy gut microbiome, or for someone who maintained a healthy weight?

Beyond microbiome changes, elderberry juice also had notable effects on metabolism. In our most recent Biology unit studying energy and enzymes, we learned that metabolism is the total of all reactions carried out by an organism. Participants experienced a 24% reduction in blood glucose levels and a 9% decrease in insulin levels, signaling improving glucose tolerance and insulin sensitivity. These improvements relate to what we learned in AP Biology about the impact of dietary choices on blood sugar and insulin demand, where the body’s need for insulin increases with higher sugar intake to help store excess glucose. The decrease in insulin levels suggests that the participants’ bodies became more efficient at processing glucose, meaning less insulin was required to regulate their blood sugar levels. This improved efficiency can help reduce the strain on the pancreas and lower the risk of developing insulin resistance over time. Additionally, the juice enhanced the body’s ability to burn fat, increasing fat oxidation both during exercise and after consuming high-carbohydrate meals. Have you ever considered how specific foods might impact your metabolism?

The researchers attribute these benefits to elderberry’s high levels of anthocyanins, plant-based compounds with known anti-inflammatory, anti-diabetic, and antimicrobial properties. According to the Cleveland Clinic, anthocyanins can also lower blood pressure, reduce risk of heart disease, prevent neurological diseases, and slow cancer growth. While other berries also contain anthocyanins, elderberries have a significantly higher concentration, delivering more powerful effects in smaller servings.

According to Patrick Solverson, an assistant professor at WSU, this study supports the idea that “food is medicine,” highlighting elderberry’s long history as a folk remedy and its growing potential in modern nutritional science. Although elderberry products are more common in Europe, their popularity surged in the U.S. during COVID-19, and is continuing to grow.

Although I don’t usually drink elderberry juice, I care a lot about maintaining my health and being mindful of the foods I eat. Knowing that it can improve gut health and support metabolism makes me excited to try it. After learning about its benefits, I’m will definitely add elderberry juice to my routine as a simple way to support my overall well-being.

Have you tried elderberry juice? If not, would you consider trying it after learning about its benefits? What other natural remedies or foods do you use to support your health?

CRISPR: Rewriting the Script in Cancer Treatment

By jchainjoe

Cancer continues to impact millions of people each year around the world; however, new breakthroughs in cancer treatment using CRISPR technology are set to transform how we can combat this complex disease. By leveraging CRISPR’s gene-editing capabilities, researchers are unlocking new possibilities to enhance immune responses, optimize therapies, and develop more precise and effective treatments.

A groundbreaking study from Harvard Medical School, led by LaFleur et al. and Milling et al., explored how CRISPR can reprogram T cells to more effectively fight cancer. Cancer cells typically evade the immune system by downregulating antigen presentation or suppressing the immune system. The researchers addressed these challenges by targeting specific genes in T cells to enhance target recognition(improved the T cells’ ability to recognize tumor antigens), increase the length of the immune response, and strengthen activation(amplifying the response on the detection of cancer). These genetically modified T cells show significant improvements in combating cancer in laboratory and preclinical models than the typical T cell. This showcases their potential to develop more effective immunotherapies, especially for cancers resistant to traditional treatments.

CAR T-Cell immunotherapy diagram by (OHC CAR-T team)

Another innovative study by Lei et al. explored CRISPR’s role in enhancing CAR(Chimeric Antigen Receptor) T-cell therapy, a promising approach that modifies a patient’s T cells to target cancer cells. While CAR T-cell therapy has shown success, it faces challenges like limited efficacy against solid tumors, safety concerns, and high costs. CRISPR offers potential solutions by improving efficacy(Enhances T-cell function and persistence through precise gene edits), enhancing safety(disables genes responsible for adverse effects like cytokine release syndrome), and reducing costs(streamlining the manufacturing process to make the therapy more accessible)

This study emphasizes how CRISPR can address existing barriers, making CAR T-cell therapy safer, more effective, and available to more patients.

The potential of CRISPR extends beyond these studies. CRISPR has opened up a new frontier in cancer research by directly editing the genes within cancer cells, disrupting oncogenes, and reshaping immune responses. For example, recent findings revealed that CRISPR can target oncogenes in leukemia cells, reducing their ability to proliferate and making them more vulnerable to existing treatments (Carlo et al.).

These advancements directly connect to what we’ve studied in AP Biology. The role of CRISPR in gene editing demonstrates the power of manipulating transcription and translation, concepts which are directly related to nucleic acids. Additionally, the focus on T-cell activation and immune responses ties into our understanding of cell communication and the immune system’s intricate pathways.

I chose to write about this topic because it represents a deeply personal and hopeful turning point in cancer treatment. My mom battled breast cancer, and seeing her fight the disease made me acutely aware of the challenges cancer patients and their families face.

What do you think about CRISPR’s role in transforming cancer treatment? Could we one day eliminate certain types of cancer altogether? Share your thoughts and let’s discuss!

The Bubble Wrap of the Human Body

By daphnatomy

What if the secret to faster healing and groundbreaking regenerative medicine was found in something that may be the skeletal equivalent of bubble wrap? Lipocartilage is a newly discovered type of skeletal tissue that is soft, springy, and super stable. These qualities could revolutionize how we repair and regenerate the human body. According to researchers at the University of California-Irvine and an international team of scientists, this exciting discovery offers new hope for addressing injuries, degenerative skeletal conditions, and everything in between.

Lipocartilage is a hybrid skeletal tissue uniquely packed with fat-filled cells called lipochondrocytes. These cells give the tissue its distinctive characteristics. Imagine the softness and elasticity of bubble wrap combined with remarkable stability. This combination makes it perfect for absorbing shocks and adapting to stress, all while maintaining its structure.

The texture of lipocartilage isn’t the only thing that makes it special. It plays a crucial role in the body, especially in areas where flexibility and support are equally important, such as the hips and shoulders. Researchers believe this tissue forms in areas under high mechanical stress, making it an important part of injury prevention and recovery.

The discovery of lipocartilage could dramatically advance regenerative medicine. Because of its unique properties, this tissue offers a natural blueprint for developing bioengineered materials that mimic its structure and function. What if we could create soft, springy materials that seamlessly integrate with the body to repair skeletal or joint damage? This breakthrough could pave the way for new treatments for arthritis, joint injuries, and even degenerative conditions that currently have limited options.

The researchers describe lipocartilage’s texture as being similar to bubble wrap. Not only is it soft and pliable, but it’s also incredibly resilient. It can handle stress and strain without breaking down, which is exactly what you want in a tissue designed to support movement and flexibility. This bubble wrap analogy isn’t just a fun way to think about the tissue; it also highlights its potential in engineering. Imagine developing implants that replicate these properties, giving patients a way to heal more naturally and effectively.

One of the most promising aspects of lipocartilage is its potential to speed up and improve healing in areas like joints, where current treatments often fall short. Whether you’re dealing with a torn meniscus, worn-down cartilage, or even major skeletal trauma, lipocartilage inspired therapies could offer better outcomes with less invasive procedures. For athletes, such as myself, this could mean returning to the field faster after injuries. For people with chronic conditions, it could mean regaining mobility and comfort. And for everyone else, it could mean faster healing for any everyday injuries you might face!

Of course, there’s still awhile before lipocartilage becomes a staple in regenerative medicine. Scientists need to study how this tissue forms, how it interacts with other skeletal components, and how to replicate its properties in the lab but, the potential is undeniable. If researchers can figure out how to harness lipocartilage effectively, it could revolutionize everything from orthopedic surgery to joint replacement therapies.

This discovery isn’t just exciting for doctors and scientists, it’s also a big deal for all of us. As life expectancy increases, so does the need for better ways to maintain and repair our bodies. Lipocartilage could be an important solution in ensuring that we don’t just live longer but live better, with less pain and more mobility.

The discovery of lipocartilage also ties into the study of enzymes, a key concept in AP Biology. Enzymes are crucial in the formation, maintenance, and repair of connective tissues like lipocartilage. For instance, enzymes such as collagenases and proteases are responsible for remodeling the extracellular matrix, a critical component that gives lipocartilage its unique properties. Additionally, enzymes like lysyl oxidase help cross-link collagen fibers, contributing to the tissue’s stability and elasticity. In regenerative medicine, researchers may harness or mimic these processes to replicate or enhance lipocartilage for therapeutic applications. This connection highlights how enzymes regulate complex biological systems, from tissue formation to repair. It also connects to the concept of cell communication. The formation and maintenance of lipocartilage rely on complex signaling pathways between cells in the skeletal system. For example, chondrocytes (cartilage cells) and osteoblasts (bone-forming cells) communicate through signaling molecules like cytokines and growth factors, such as transforming growth factor-beta.

These signals coordinate the differentiation of cells, the remodeling of the extracellular matrix, and the tissue’s adaptation to mechanical stress. Additionally, lipocartilage’s role in repairing and regenerating skeletal tissue involves cell signaling to detect damage, activate repair processes, and regulate inflammation.

How do you think a tissue like lipocartilage could change the future of medicine and even improve the quality of life for humans?

Is Severe COVID-19 the Secret to Reducing Cancer Tumors?

By emzyme

When we think of COVID-19, cancer treatment isn’t the first thing that comes to mind. But according to the ground-breaking study that was published in the Journal of Clinical Investigation in November 2024, severe COVID-19 infections might have an unanticipated ability to make tumors smaller. Based on how the virus modifies immune cells, this discovery may result in new therapies for advanced and treatment-resistant cancers.

Under the guidance of Northwestern Medicine’s Dr. Ankit Bharat, the study concentrates on the monocytes, which is a subset of white blood cells. Monocytes at tumor locations typically undergo a transformation into cancer-friendly cells, creating a barrier of defense that promotes cancer growth. Severe COVID-19 cases, however, change the rules.

Based on the study, the virus causes the immune system to produce specialized monocytes that have a receptor that firmly attaches to a particular COVID-19 RNA sequence. These altered monocytes move straight to tumors, stimulate natural killer cells, and resist transformation into cancer-friendly cells. When activated, natural killer cells attack the cancer, and cause the tumors to get stronger.

In mice with stage 4 cancers (such as melanoma, lung, breast, and colon), scientists administered a medication to stimulate the immunological reaction brought on by severe COVID-19. Across all the cancers that were tested, tumors shrank significantly, demonstrating the potential of these monocytes to fight cancer.

The technique bypasses the body’s dependence on T-cells, which is an important drawback of existing immunotherapies that only benefit 20-40% of patients. Because T-cell production frequently fails in patients with compromised immune systems, this finding offers an exciting alternative.

Although encouraging, this finding needs to be used with caution. While the study was successful in mice, clinical trials in humans are still needed to confirm the same results.

Furthermore, the absence of the required RNA sequence in the COVID-19 vaccines prevent them from eliciting this response. However, researchers hope to create future medications or vaccinations that mimic this tumor-shrinking without carrying the danger of serious illnesses.

In AP Bio, our class talks about the immune system and the function of specialized cells. For example, we have studied how natural killer cells target pathogens and infected cells, which is what happens when the transformed monocytes activate NK cells near tumors. Connecting to the processes of transcription and translation, the viral RNA programs immune cells to behave differently — an intriguing real-world application of molecular biology that we have studied.

This study is particularly fascinating to me, as I hope to pursue medicine in my future. I am interested in studying various types of cancers, and it is very important for me to know how diseases affect them.

The idea of turning a lethal virus into a weapon to fight one of the most deadly diseases in the world is both thrilling and terrifying. Imagine a future where doctors will be able to treat cancer by using the immune system instead of invasive surgeries or toxic chemotherapy. Could this discovery be the key to unlocking a universal cancer treatment?

Self-Regenerating Hearts?

By keomeostasis

On January 12, 2025

In an interesting article from the University of Arizona’s Department of Health Sciences, a substantial feat was discovered, being that some artificial heart patients could regenerate heart muscle. A research team led by Dr. Hesam Sadek at the University of Arizona’s Sarver Heart Center uncovered that some patients with left ventricular assist devices could regenerate heart muscle. The study used tissue samples from patients with artificial hearts. A group of experts used carbon dating techniques and in the end found that heart muscle cells in patients with artificial hearts could regenerate over 6 times faster than healthy hearts. As many of the experts hypothesized, it was generally concluded that the artificial heart’s ability to take some load off the heart (by pumping blood for the heart) is what encouraged the regeneration to occur. The goal for these experts is to try and make regeneration possible for all people, which could potentially cure problems like heart failure.

This article connects to our most recent Unit in AP Bio, that being cellular respiration. Heart cells, like all cells require energy to maintain their cellular functions, including repair and regeneration. The regeneration of these heart cells naturally require extreme energy in the form of ATP, a compound produced through Cellular Respiration. There are 3 distinct parts of cellular respiration, that being Glycolysis, Oxidation of Pyruvate & the Krebs cycle, and Oxidative Phosphorylation. In Glycolysis, ATP is used to break down glucose. Then, the glucose molecules are rearranged and phosphates are removed. In the end the removal of phosphates help form 4 ATP. However, as 2 ATP are used to break down the glucose, it is a net gain of 2 ATP. During the Krebs Cycle, a reduced NAD+ (Now NADH) is put into the cycle, and in the end, the products are 6CO2, 2 ATP, 8 NADH, and 2 FADH2. Lastly, during oxidative phosphorylation, NADH and FADH2 are oxidized and the electrons are passed down an electron chain consisting of cytochromes. Then as the H+ gradient fills up, H+ will flow through the ATP synthase complex, generating 28 ATP. Lastly, O2 will act as the “final electron acceptor” and join with electrons from the chain and H+ to reset the cycle and make a waste product of H20. In the end, cellular respiration converts glucose and oxygen into carbon dioxide, water, and the most important product, energy in the form of ATP. The finding helps support the idea that the heart’s inability to regenerate is due to the constant need to pump blood. Since the ATP given to heart muscle cells is used to keep the heart pumping, there is not enough ATP left for heart muscle cells to use to regenerate. However, people with artificial hearts do not have this problem as the artificial heart helps the heart pump blood. Therefore there is sufficent ATP for the heart to regenerate.

There are many future implications to this article. But most importantly, if scientists can find why the heart muscles regenerate, and how to apply it to all people could lead to potential treatments for many heart problems like heart failure. As someone who knows how common severe heart problems are, I am excited to see that this study could lead to a potential cure to many of these problems. What problem do you think scientists will be able to solve with this groundbreaking discovery?

Long Covid: a Hazy Mind, and a Hazier Definition.

By alleliola

On January 12, 2025

The term “long COVID ” has been thrown around frequently without a clear definition. In fact, it has no straight definition and is just as foggy as its symptoms suggest. New research on long COVID has revealed just why this syndrome is so nebulous and how to effectively avoid it.

The definition of long Covid varies between different public health bodies. Still, overall, it shares the idea that it is a condition characterized by unexplainable symptoms well after an initial COVID-19 infection. Such symptoms can commonly include memory issues (“brain fog”), cough, headaches, problems with taste and/or smell, and chronic fatigue. While the pathological mechanisms for long COVID aren’t entirely understood, research has pointed to the virus’s ability to disregulate the immune response. A dysregulation in the immune response would allow the virus to remain inside the body’s tissues long after the initial infection and prevent it from being adequately dealt with.

In AP Biology, we learned about the exact biochemical and cellular pathways essential to the immune response. Helper-T cells carry the information of an infection into the lymph and signal B-cells and other T-cells to divide. Cytotoxic-T cells destroy infected cells, and cytokines are biochemical transmitters that allow cells to communicate with each other. Long COVID attacks these basic functions by exhausting the Helper-T cells and preventing them from effectively signaling other cells. The virus also elevates the number of cytokines and cytotoxic-T cells, overwhelming the immune system with unneeded information and expending more energy on unnecessary cytotoxic-T cells that may start attacking uninfected cells. These attacks therefore weaken the immune system and allow for the effects of long COVID.

Currently, there is no specific treatment for long Covid, but there is a way to prevent it altogether. Avoiding infection by COVID-19 means that the effects of long COVID can never set in, so the best way to prevent these terrible symptoms is to stay as vigilant as possible and keep ourselves healthy. Do you know anyone with long COVID? If so, what have they done to cope with their symptoms? Let me know!

From Predator to Pollinator: How Ethiopian Wolves Supplement Their Diet

By alleliola

On January 12, 2025

Ethiopian Wolves, also known as Red Jackals, are among the most endangered canid species in the world. They inhabit the mountains of Southern Ethiopia, primarily feeding on rodents like Giant Mole Rats and a few other small mammals. However, a recent paper reveals that these predators also supplement their diet with something unexpected: nectar.

The specific plant that these canids enjoy is called the Ethiopian Red Hot Poker, named for its vibrant color and spear-like shape. The flowers of this plant produce an abundance of sugar-rich nectar to attract pollinators such as insects, birds, and small mammals. While various plants employ similar strategies, what sets the Ethiopian Red Hot Poker apart is the role of Ethiopian Wolves in the pollination cycle. This discovery makes Ethiopian Wolves one of the few large carnivores known to consume nectar and significantly contribute to pollination. Observations have shown that large amounts of pollen accumulate on the muzzles of these canids, which aids in the pollination of Red Hot Pokers when the wolves feed from different flowers.

In our AP Biology class, we have been working on a pollination project throughout the school year. In this project, we collect pollen from flowers and manually transfer it to other flowers to facilitate fertilization. This practice is a form of artificial selection, as humans determine which plants reproduce based on specific characteristics. Nonetheless, it mirrors natural instances such as those involving Ethiopian Wolves. Have any of you observed pollination assisted by mammals before? I would love to hear your thoughts!

Long COVID: Unveiling the Immune System’s Lingering Struggles

By dihybridross

On January 10, 2025

As we approach 2025 it’s hard to believe that 5 years have passed since the COVID 19 pandemic swept through the world. However, in the realm of science, progress often moves more slowly than the rapid pace at which we experience change. Only recently have key developments emerged enhancing our understanding of how our body reacts to the virus and what makes COVID-19 so frightening..

A recent study conducted by the Medical University of Vienna concluded that the COVID-19 infection can cause changes to the immune system which can explain the phenomenon known as “long covid.” The definition of Long Covid is currently not set in stone with Mayo Clinic claiming that there is no universal definition; however, the CDC currently describes long covid as “a chronic condition that occurs after SARS-CoV-2 infection and is present for at least 3 months. Long COVID includes a wide range of symptoms or conditions that may improve, worsen, or be ongoing.” Jumping back to the study, the researchers first assessed the immune cells, cytokines, and growth factors in the blood of 106 COVID-19 survivors, comparing the results to 98 people who had been unexposed. The team also measured the level of antibodies against the virus’s spike protein. The study showed that 10 weeks after those who were infected with the virus recovered there was still increased activity of T and B cells, this is in contrast to the healthy subjects. Moreover they found plenty of cytokines and remnants of acute inflammation. However, this data was to be expected, what was shocking was the researchers findings when they took data 10 months following recovery.

After 10 months survivors did not have a robust immune response with an increase of specific immune cells like effector memory cells and effector memory cells, transitional B cells, and immature B cells called plasmablasts, rather they exhibited a significant reduction in immune cells including B and T cells. Moreover survivors had significantly unregulated serum interleukin 4 levels Even a student of Biology may immediately realize how detrimental an unregulated interleukin level is, however an unregulated interleukin 4 level can cause excessive inflammation which if left unchecked can damage tissue and impair normal immune system function. To make matters worse, more than 90% of the patients lacked neutralizing antibody activity, suggesting a large proportion of study subjects lost protection from reinfection.

The lead researchers have stated that the results of their study suggest that survivors’ immune systems aren’t adequately responding to some pathogens and can explain why many get “Long Covid” symptoms. These results are of course very concerning, especially to a student of AP biology. As I just wrapped up learning about the immune system, I learned all about how memory cells and neutralizing antibodies are key in providing long term protection against pathogens by mobilizing your body quickly to defeat them, so the patients lacking these key components was very troubling to hear.

However there is hope. One critical detail stood out to me in the study: none of the participants were vaccinated. In AP Bio we learned how vaccines train the immune system by exposing it to harmless pathogens which creates memory cells. This knowledge assures me that ongoing vaccine development can help to mitigate the detrimental effect COVID-19 has.

What do you think? Could vaccination be the key to addressing the long-term effects of COVID-19, or should we focus more on post-infection treatments? I’d love to hear your thoughts in the comment section!

Uncovering the Deep Enzyme Pockets Behind Parkinson’s and Cancer

By metamorgosis

There are approximately 75,000 different enzymes in the human body. These abundant proteins serve such a variety of roles in our bodies’ systems, we would truly not function the same without them. Nevertheless, enzymes can also become involved in the development of diseases such as Parkinson’s and even some cancer types.

One specific family of enzymes named the GTPases are often involved in these diseases. Science Direct classify GTPases as enzymes that facilitate the “conversion of guanosine triphosphate (GTP) to guanosine diphosphate (GDP).” Specifically, the reason this enzyme family has been historically deemed “undruggable” is related to the slippery exterior of the enzyme that made it difficult for modern drugs to target the disease-causing enzymes.

In September of 2024, researchers at the University of California San Francisco (UCSF) discovered a method for targeting the infamous K-Ras protein, a member of the GTPase family responsible for “up to 30% of all cancer cases.”

Structure of K-Ras Protein.

This enzyme and others like it work to regulate molecular movement and cell functions, so when an issue arises in these networks, diseases can easily develop. At UCSF, the team manipulated a K-Ras mutation to find new drug-binding sites that were previously unable to be seen by other drug discovery tools. Essentially, the mutation nudged open a pocket in the GTPases where the drug could bind, “freeze” the enzyme, and successfully inhibit a GTPase.

As we have learned in AP Biology, enzymes are globular proteins that are organic catalysts in living things. Enzymes work by lowering the amount of activation energy needed for a reaction to occur, and they do this by weakening the bonds between molecules and bringing them closer together to react with one another. Moreover, enzymes catalyze reactions by binding to one or more reactant molecules called substrates in the enzyme’s active site. This enzyme-substrate complex binds in a way that either a chemical bond-breaking or bond-forming process takes place, ending with the products of the reaction leaving the active site.

Meanwhile, enzyme inhibitors — such as the drugs studied by the UCSF researchers — can bind to the active site or another area of the enzyme and prevent the substrate(s) from binding and inhibit the reaction from happening.

According to the National Cancer Institute, an enzyme inhibitor is “a substance that blocks the action of an enzyme.” Relating to the significance of the researchers’ findings, this source explains that “In cancer treatment, enzyme inhibitors may be used to block certain enzymes that cancer cells need to grow.”

Illustrative comparison between enzyme catalysis and enzyme inhibition.

Groundbreaking research like this is becoming increasingly important for our understanding of the widespread diseases we face. Learning about the current innovative work of researchers is incredibly fascinating, as their work has significant implications for future enzyme research. It is truly exciting to see what researchers will investigate next in the field chemical genetics. What do you think will be the next step in enzyme research?

Leaky Blood Vessels and Long COVID

By cathoxylgroup

Earlier this year, researchers in Dublin, Ireland, found that brain fog from long COVID is associated with blood-brain barrier disruption. COVID-19 is an infectious disease that causes symptoms lasting for two to six weeks, depending on the severity of the case. Long COVID, on the other hand, is a lingering illness that can cause one’s COVID symptoms to last for months. This lingering illness consists of prolonged COVID symptoms after initial infection, with patients reporting fatigue, dizziness, impaired taste and smell, and brain fog. Cognitive impairment, or brain fog, is a particularly devastating symptom of long COVID, as it causes the affected individual to experience mental exhaustion and forgetfulness. The team of researchers in the aforementioned article set out to find the root cause of brain fog in people with long COVID. They used dynamic contrast-enhanced MRI (DCE-MRI), which specifically measures tissue vascularity and permeability, to study patients’ brains. The researchers found that a significant percentage of long COVID patients who self-reported symptoms of brain fog also had increased blood-brain barrier permeability. The blood-brain barrier (BBB) is a protective layer that lines the brain’s blood vessels. In an earlier AP Bio unit, we learned that cell membranes are semi-permeable and filter out harmful substances. The function of the BBB is practically identical to that of a cell membrane: it is a semi-permeable bilayer that filters out harmful substances. Both the cell membrane and the BBB are structured with phospholipids, and both have transport mechanisms, include pumps, to filter substance in and out.

This research study ultimately suggests that long COVID disrupts the BBB and causes systemic inflammation. Systematic inflammation causes the body to experience irregular temperatures, increased heart and breathing rates, and produce an abnormally high amount of cytokines. This response ultimately leads to structural changes in the brain that cause brain fog.

While I don’t know of anyone in my personal life who has or had long COVID, I do know how awful it is to have regular COVID, so I can’t imagine how horrible it would feel for those symptoms to linger for months on end. Have you or someone you love ever experienced long COVID? What was it like for you or them to live with those symptoms?

How We Prevent COVID-19 Beyond Vaccinations.

By bunsenbyrner

In 2023, Chinese researchers conducted a study to determine the genetic diversity of COVID-19 before and after nationwide policies were instituted to prevent the virus’s further spread. A specific focus was placed on measuring the development of the more recent Omicron variant in terms of genetic diversity. This study was carried out from September 2022 to January 2023 and researchers gathered genomic data and concluded that, after the implementation of international global health policies focused on prevention and control (promoting the coronavirus vaccine for example), there were no particularly genetically unique Omicron variants across all samples (over 21,000 genomic sequences with 1,897 of those being from outside of China) that provide any new harm to human health and safety.

The immense genetic diversity of Coronavirus is primarily due to it being an RNA-based virus. A typical DNA based virus functions in a similar way that steroids cause gene expression in cells because they enter the cell (through endocytosis rather than simple diffusion for steroids) and then head to the cell nucleus to add and virus genes into the cell and cause them to be expressed. However, RNA0based viruses virus types only contain RNA in their genome, releasing RNA directly into the cell (bypassing the transcription phase in gene expression) and immediately interacting with the cell’s ribosomes to create more viruses. Not having DNA means that fewer regulatory processes take place to regulate genomic adaptation, causing more variations to occur among virus particles. This makes it very difficult for modern medicine to keep up with SARS-CoV-2 as antibodies manufactured through vaccines become less effective to newer, more differentiated strands of the virus with different targetable spike proteins. This process is also very beneficial to the replicative abilities of the virus, as RNA viruses are known to replicate at an increased rate than their DNA-centered counterparts. This is due to the fact that eliminating the need for DNA transcription makes the creation of new virus particles much more rapid, making such species typically more volatile. However, Chinese health policies have counteracted the danger presented by viruses such as COVID-19 by enforcing strict policies regarding the spread of the virus and vaccination policies in order to reduce the number of infected hosts and therefore limit the opportunities that these viruses have to mutate beyond our control. This has proven successful as no significantly dangerous strands have appeared since policies to spread vaccination and limit the COVID epidemic in China were implemented.

This study has proven the value that can be derived from taking preventative measures against viruses and that limiting the mutability of pathogenic viruses can lead to long-term health. Vaccinations are an incredibly valuable tool in our fight against diseases and their future usefulness is dependant on our ability to limit the spread and mutation of the pathogen the vaccine targets for. In order to keep ourselves and our neighbors safe, it is our responsibility to take preventative measures against contracting diseases to make sure that vaccines continue to keep us all immune.

This does add to the notion of the potential ineffectiveness of vaccinations given certain circumstances occurring within the virus genome and may show that medicine is overly reliant on the development of vaccinations rather than enforcing more strict prevention measures. The COVID-19 pandemic has shown the extreme unpreparedness that humanity has for the elimination of viruses. The results of this study beg the question if we focus less on the development of new vaccine models and more on limiting virus mutation or would this ultimately be detrimental to human health with minimal benefit? Due to the negative mental impacts that quarantine has had on humans globally, would people even prefer this strategy of prevention?

The Lucky Few…

By daphnatomy

Have you ever wondered why some people almost seem immune to COVID-19, no matter how much they’re exposed to it? A recent study has uncovered a fascinating clue which might just be the answer: a gene called HLA-DQA2. This little-known gene could possibly explain why some people’s immune systems are able to fight off the virus before it even takes hold.

In a groundbreaking study, researchers from the Netherlands Cancer Institute conducted a trial by exposing orignally 36 healthy volunteers to SARS-CoV-2 in 2021. The goal was to understand how the virus infects people. 16 out of the 36 participants went under more extentisve testing. However, only six of the 16 volunteers who underwent extensive testing became sick. Miraculously, rest did not get sick despite being placed under the same conditions.

The researchers soon realized they had stumbled upon a unique opportunity to understand how some people could fend off COVID-19 more effectively. It turned out that their immune systems had a stronger response, thanks to elevated activity in a gene called HLA-DQA2. This gene is involved in alerting the immune system to the invasion of pathogens, and the participants who didn’t get sick showed higher activity of this gene in their immune cells even before exposure to the virus.

This elevated gene activity allowed their immune systems to respond rapidly once the virus entered their system. Within one day of exposure, these participants immune systems triggered a response, signaling their bodies to fight the virus. In contrast, people who got sick took, took five days to trigger the same immune response, allowing the virus time to spread and cause illness.

The study revealed that this gene activity could be a predictor of who might be more resistant to COVID-19. While scientists aren’t sure exactly how HLA-DQA2 works, previous research has linked it to milder COVID-19 outcomes.

Although the study was conducted during the early days of the pandemic, when few had immunity from vaccines or prior infections, its findings offer valuable insights into how the immune system works. As research continues, scientists hope this discovery could lead to better ways to prevent or treat COVID-19—and maybe even other diseases in the future.

This study connects to the AP Biology immune system unit by showing how genetics, specifically the HLA-DQA2 gene, can influence the immune response. The gene helps trigger a faster immune reaction, preventing illness in some individuals exposed to COVID-19. This ties into the concepts of innate immunity, where the body’s first defense responds quickly, and how genetic differences affect immune function. HLA-DQA2 helps amplify inate response by activation T cells that secrete cytokines which then activate more cells to carry out the immune response.

Have you ever caught covid? If not, do you think it could be due to this gene, or simply a lack of exposure to the disease.

Rogue Antibodies: Unraveling the Mystery of Long COVID’s Lingering Pain

By lucysome