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Comment by Dr. Krishna Kumari Challa on February 23, 2022 at 9:36am

Tick saliva may offer a path to new therapies for inflammatory diseases

A recent study  has found that proteins found naturally in tick saliva, called evasins, can be modified to block the activity of important proteins in human inflammatory diseases such as arthritis, asthma and multiple sclerosis.

The study showed it was possible to modify evasins so that they bind to the exact group of disease-promoting human proteins (chemokines), helping to suppress inflammation.

This new discovery opens the door to the development of much needed new therapies for inflammatory diseases. 

Inflammatory diseases, such as atherosclerosis, arthritis, psoriasis, asthma and multiple sclerosis, all involve the same underlying phenomenon in which the body's white blood cells attack certain tissues. The white blood cells are attracted to these tissues by a class of proteins (chemokines) that are produced in the affected tissues (e.g. blood vessel wall in atherosclerosis, joints in arthritis). By targeting chemokines, evasins block the movement of white blood cells  and the resulting tissue damage.

Typically, each tick species secretes a cocktail of evasins, thereby accomplishing broad-spectrum suppression of the host inflammatory response, presumably enabling the tick to feed for extended periods while not alerting the host to the tick's presence.

However, some chemokines are involved in inflammatory diseases while others are needed for the body's normal immune function. Therefore, for therapeutic applications, it is essential to modify the evasins so they only target the disease-causing chemokines.

 Structure-guided engineering of tick evasins for targeting chemokines in inflammatory diseases, Proceedings of the National Academy of Sciences (2022). DOI: 10.1073/pnas.2122105119.

https://medicalxpress.com/news/2022-02-saliva-path-therapies-inflam...

Comment by Dr. Krishna Kumari Challa on February 22, 2022 at 12:06pm

Altruism in birds? Magpies have outwitted scientists by helping each other remove tracking devices

But these poor birds didn't know that scientists are only trying to help them!

When scientists attached tiny, backpack-like tracking devices to five Australian magpies for a pilot study, they didn’t expect to discover an entirely new social behaviour rarely seen in birds.

Scientists' goal was to learn more about the movement and social dynamics of these highly intelligent birds, and to test these new, durable and reusable devices. Instead, the birds outsmarted them!

the magpies began showing evidence of cooperative “rescue” behaviour to help each other remove the tracker.

While we’re familiar with magpies being intelligent and social creatures, this was the first instance we knew of that showed this type of seemingly altruistic behaviour: helping another member of the group without getting an immediate, tangible reward.

During a pilot study, scientists found out how quickly magpies team up to solve a group problem. Within ten minutes of fitting the final tracker, they witnessed an adult female without a tracker working with her bill to try and remove the harness off of a younger bird.

Within hours, most of the other trackers had been removed. By day 3, even the dominant male of the group had its tracker successfully dismantled. We don’t know if it was the same individual helping each other or if they shared duties, but we had never read about any other bird cooperating in this way to remove tracking devices.

The only other similar example of this type of behaviour we could find in the literature was that of Seychelles warblers helping release others in their social group from sticky Pisonia seed clusters. This is a very rare behaviour termed “rescuing”.

Tracking magpies is crucial for conservation efforts, as these birds are vulnerable to the increasing frequency and intensity of heatwaves under climate change.

Now scientists are scratching their heads to figure out how to save these birds without using trackers! 

https://www.birdlife.org.au/afo/index.php/afo/article/view/2247

https://www.birdlife.org.au/afo/index.php/afo

https://theconversation.com/altruism-in-birds-magpies-have-outwitte...

Comment by Dr. Krishna Kumari Challa on February 22, 2022 at 11:57am

IKEA and the fate of a European forest Accidents of geography and history have left Romania with one of the largest old-growth forests remaining in the world. Since around the time the country joined the European Union, however, between one-half and two-thirds of its virgin forest has been logged — most of it illegally. Along with the environmental loss has come violence: forest rangers have been murdered and conservationists working in the area are putting their lives at risk. One multinational company that denies any connection to poor forestry practices is the furniture behemoth IKEA. It is the world’s largest wood buyer and Romania’s largest private landowner (with much of the land purchased from the Harvard University endowment). A New Republic investigation shows how the complexities of land ownership, subcontracted manufacturing and weak oversight make the destruction of Romania’s forests so difficult to stop.

Comment by Dr. Krishna Kumari Challa on February 22, 2022 at 11:50am

Bacteria upcycle carbon waste into valuable chemicals

Bacteria are known for breaking down lactose to make yogurt and sugar to make beer. Now researchers have harnessed bacteria to break down waste carbon dioxide (CO₂) to make valuable industrial chemicals.

In a new pilot study, the researchers selected, engineered and optimized a bacteria strain and then successfully demonstrated its ability to convert CO₂ into acetone and isopropanol (IPA).

Not only does this new gas fermentation process remove greenhouse gases from the atmosphere, it also avoids using fossil fuels, which are typically needed to generate acetone and IPA. After performing life-cycle analysis, the team found the carbon-negative platform could reduce greenhouse gas emissions  by 160% as compared to conventional processes, if widely adopted.

 Michael Jewett, Carbon-negative production of acetone and isopropanol by gas fermentation at industrial pilot scale, Nature Biotechnology (2022). DOI: 10.1038/s41587-021-01195-w. www.nature.com/articles/s41587-021-01195-w

https://phys.org/news/2022-02-bacteria-upcycle-carbon-valuable-chem...

Comment by Dr. Krishna Kumari Challa on February 22, 2022 at 11:47am

Tough and stretchable ionogels

Silent speech device developed

Comment by Dr. Krishna Kumari Challa on February 21, 2022 at 10:01am

Researchers conducted experiments using human cells and a mouse model mimicking the cytokine storm seen in some patients with severe COVID-19 infection. They applied CRISPR genome-wide screening to analyze how cell function, in particular cell death, changes when one gene is knocked out (inactivated).

Receptor-interacting protein kinase (RIPK1) plays a critical role in regulating inflammation and cell death. Many sites on this protein are modified when a phosphate is added (a process known as phosphorylation) to suppress RIPK1's cell death-promoting enzyme activity. How the phosphate is removed from RIPK1 sites (dephosphorylation) to restore cell death is poorly understood. This new work discovered that PPP1R3G recruits phosphatase 1 gamma (PP1γ) to directly remove the inhibitory RIPK1 phosphorylations blocking RIPK1's enzyme activity and cell death, thereby promoting apoptosis and necroptosis.

An  analogy of a car brake help explain what's happening with the balance of cell survival and death in this study: RIPK1 is the engine that drives the cell death machine (the car). Phosphorylation applies the brake (stops the car) to prevent cells from dying. The car (cell death machinery) can only move forward if RIPK1 dephosphorylation is turned on by the PPP1R3G protein complex, which releases the brake.

In this case, phosphorylation inhibits the cell death function of protein RIPK1, so more cells survive. Dephosphorylation takes away the inhibition, allowing RIPK1 to activate its cell death function.

The researchers showed that a specific protein-protein interaction—that is, PPP1R3G binding to PP1γ—activates RIPK1 and cell death. Furthermore, using a mouse model for "cytokine storm" in humans, they discovered knockout mice deficient in Ppp1r3g were protected against tumor necrosis factor-induced systemic inflammatory response syndrome. These knockout mice had significantly less tissue damage and a much better survival rate than wildtype mice with the same TNF-induced inflammatory syndrome and all their genes intact.

Overall, the study suggests that inhibitors blocking the PPP1R3G/PP1γ pathway can help prevent or reduce deaths and severe damage from inflammation-associated diseases, including heart disease, autoimmune disorders and COVID-19. They are working to screen and identify peptide compounds that most efficiently inhibit the PPP1R3G protein complex. They hope to pinpoint promising drug candidates that may stop the massive destruction of cardiac muscle cells caused by heart attacks.

Jingchun Du, Yougui Xiang, Hua Liu, Shuzhen Liu, Ashwani Kumar, Chao Xing, Zhigao Wang. RIPK1 dephosphorylation and kinase activation by PPP1R3G/PP1γ promote apoptosis and necroptosis. Nature Communications, 2021; 12 (1) DOI: 10.1038/s41467-021-27367-5

https://researchnews.cc/news/11713/Researchers-identify-protein-com...

Part 2

Comment by Dr. Krishna Kumari Challa on February 21, 2022 at 10:00am

Researchers identify protein complex critical in helping control cell death

 Cell death plays an important role in normal human development and health but requires tightly orchestrated balance to avert disease. Too much can trigger a massive inflammatory immune response that damages tissues and organs. Not enough can interfere with the body's ability to fight infection or lead to cancer.

Researchers are studying the complex molecular processes underlying necroptosis, which combines characteristics of apoptosis (regulated or programmed cell death) and necrosis (unregulated cell death).

During necroptosis dying cells rupture and release their contents. This sends out alarm signals to the immune system, triggering immune cells to fight infection or limit injury. Excessive necroptosis can be a problem in some diseases like stroke or heart attack, when cells die from inadequate blood supply, or in severe COVID-19, when an extreme response to infection causes organ damage or even death.

A new preclinical study  identifies a protein complex critical for regulating apoptosis and necroptosis—known as protein phosphatase 1 regulatory subunit 3G/protein phosphatase 1 gamma (PPP1R3G/PP1γ, or PPP1R3G complex). The researchers' findings suggest that an inhibitor targeting this protein complex may help reduce or prevent excessive necroptosis.

Cell death is very complicated process, which requires layers upon layers of brakes to prevent too many cells from dying. If you want to protect cells from excessive death, then the protein complex  identified in this study is one of many steps you must control.

Part 1

Comment by Dr. Krishna Kumari Challa on February 20, 2022 at 12:18pm

Comment by Dr. Krishna Kumari Challa on February 20, 2022 at 11:41am

In the computer simulations, PE particles were found to prefer the center of the lipid membrane as their location. In the PAMPA experiments, PE plastic partially permeated the membrane, but membrane permeability slowed down significantly over time, probably due to the accumulation of plastic in the membrane. In the simulations, the preferred location of PET particles was, to a certain degree, the surface part of the membrane, and in the experiments, they permeated the membrane fairly well. According to this study, the properties of the membrane structures were not significantly affected by individual plastics.

Joni Järvenpää et al, PE and PET oligomers' interplay with membrane bilayers, Scientific Reports (2022). DOI: 10.1038/s41598-022-06217-4

https://phys.org/news/2022-02-nano-sized-plastics-permeate-cell-mem...

Part 2

Comment by Dr. Krishna Kumari Challa on February 20, 2022 at 11:39am

Nano-sized plastics may enter and permeate cell membranes

The occurrence of microplastics in nature has been studied extensively. However, little is known about the health effects of microplastics, and understanding of their transport into the human body is also lacking. Any adverse health effects possibly associated with plastics may be caused by the plastic compound itself, or by the environmental toxins it carries. Many known fat-soluble environmental toxins and heavy metals are known to be able to attach to the surface of small plastic particles. This is why it is important to investigate the transport mechanisms of microplastics into the human body.

With the help of molecular modeling, researchers at the University of Eastern Finland's School of Pharmacy analyzed the behavior and transport of nano-sized microplastics in bilayer membranes which mimic cell membranes. The researchers performed simple molecular dynamics simulations using well-known and widely used polyethylene (PE) and polyethylene terephthalate (PET) particles.

The cell membrane permeability of pulverized PE and PET plastics was also examined using the Parallel Artificial Membrane Permeability Assay method, PAMPA. The method is usually used to investigate passive absorption of medicines, but it hasn't been used to study microplastics before. The PAMPA method was used to investigate the amount of matter permeating the membrane. The amount of plastic permeating the artificial membrane was measured by NMR spectroscopy at certain intervals.

In both experiments, the movement of molecules was controlled only by concentration differences on different sides of the membrane, and by occasional movement induced by heat. In other words, the methods provided information on the passive permeation of molecules through the membranes.

Part 1

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