An article in Science Daily describes that proteins do not last forever; they deteriorate and are degraded in the cell back into amino acids and then recycled into new proteins. Proteasome, the cell’s protein recycler, gets rid of the unwanted toxic protein. This new discovery can help with treating muscle waste, neurodegeneration and cancer. New evidence shows that the proteasome is regulated, getting ready for activity when the cell has a large protein turnover. Researchers have found an enzyme tankyrase that regulates the proteasome’s activity. Researchers also found a molecule, XAV939 that inhibits tankyrase and blocks the activity of proteasome.
Tankyrase was identified for its role in elongating telomeres, the ends of a chromosome. Researchers discovered, through a series of experiments in fly and human cells, that tankyrase completes a process called ADP-ribosylation to modify PI31. This process regulates the activity and assembly of proteasome subunits into the active complex, 26S.
Proteasome is currently being developed for cancer therapies. The FDA has approved Valcade, a proteasome inhibitor being used for the treatment of multiple myeloma and mantle cell lymphoma. But you can be resistant to Valcade, or have symptoms of peripheral neuropathy. For multiple myeloma proteasome activity needs to increase.
The researchers also have also linked proteasome regulation and metabolism, which suggest that the proteasome digests too much protein. This can lead to muscle loss.
Stefan Maas, at the National Institute of Health’s National Institute of General Medical Sciences, explains that “this discovery reveals fundamental insights into protein degradation… the findings also enlighten ongoing research on cancer therapies, exemplifying the impact of basic research on drug development.”
And article on Science Daily referencing a journal published in sciencemag explains how the protein causing isolated congenital asplenia (ICA) causes this disorder. This condition is very rare and has be officially documented in less than 100 cases in medical literature. These scientists sequenced 23 exomes (the part of the genome formed by exons that get transformed into proteins). After proper testing and filtering, researchers narrowed down to 4,200 possible genes. Next, researchers hypothesized which exomes would be more likely to house these gene therefore, deciding to focus on ICA exomes. The gene RPSA responsible for coding for a protein found in the cell’s protein-synthesizing ribosome was found to be the culprit. Every individual with a coding mutation in this gene is developed with out a spleen. These results are puzzling because this ribosome is present in every organ in the body but only seems to effect the spleen.
This discovery may make it possible to develop new diagnostic test for ICA and lead to more research on this specific protein-making machinery.
Down syndrome: karyotype and affected child
In the article, Protein
Linked to Development Problems, it explains that mice with Alzheimer’s
disease and Down syndrome are both missing a protein called SNX27. Mice with
Down syndrome produce an extra copy of chromosome 21. Chromosome 21 does not
directly control the production of SNX27, but it does produce miR-155. miR-155
is a regulator that prevents the production of SNX27. The lack of SNX27
prevents the neurons from working properly in the brain. This discovery
partially explains the effects of Down syndrome. Discoveries like this can also
help to discover ways for treating people with Down syndrome. When scientists
tried inserting SNX27 into mice that lacked the protein, they found that their
brain function improved. In an article in Science Daily, it is said that:
“Everything goes back to normal after SNX27 treatment.
It’s amazing — first we see the glutamate receptors come back, then memory
deficit is repaired in our Down syndrome mice,” said Xin Wang, a graduate
student in Xu’s lab and first author of the study
Finding a way to help people with Down syndrome improve
their brain function will change the lives of many people. Hopefully it may
soon be possible to reverse the effects of Down syndrome through genetic
Approximately 20 years ago, the herpes virus genome was sequenced. This was thought to be able to predict all the proteins that the virus could produce. However, some scientists from the Max Planck Institute of Biochemistry and from the University of California in San Francisco have discovered several hundred novel proteins. In order to do this, the scientists infected cells with the herpes virus and observed which proteins were produced over a 72 hour period. Upon observation, the scientists noticed that the intermediate products of the virus had many short, novel RNA products. However, one of the most surprising results was that they found the organization of information required for protein production to be much more complex than previously believed.
Overall, I found this information to be quite interesting and hope that it may someday help scientists better identify a way to treat those infected with the herpes virus. The scientists in this study say that much more research needs to be done to take this identification of the virus’ genome and determine what the actual products are that the genome is producing.
Viruses, such as the herpesvirus, have relatively small genomes. The production of proteins relies on the information encoded by the genome. Surprisingly, the genome of the herpesvirus contains a significantly large amount of information.
Hundreds of small novel proteins have been newly discovered in the herpesvirus. Scientists were able to identify the different proteins that were produced by cells that were infected with the herpesvirus for the duration of 72 hours. Genetic material must first be copied (RNA) in order to initiate the production of proteins. Observing the RNA resulted in the discovery of a significant amount of short novel RNA molecules. The results of the herpesvirus’ genome regarding material required for protein production showed a complexity in relation to the organization of the required material’s information.
The information provided by this article allows readers to see the new discoveries that being made in relation to harmful viruses. Each new discovery opens a door to new possibilities for cures.
According to ScienceDaily, two proteins have been linked to the progression of breast cancer. The two proteins that were linked are JMJD2C and HIF-1. Breast cancer cells have the ability to use partnered proteins to unlock cancerous genes. The JMJD2C protein has the ability to release harmful genes that result in the growth of tumors. The HIF-1 protein has the ability to turn on genes, but can also be controlled by a cancer influencing variable which can result in an increased malignancy in breast tumors. On a positive note, the majority of genes that can be activated by HIF-1 are enclosed within mature cells, and cannot be unlocked without the JMJD2C partner. When HIF-1 and its partner JMJD2C are readily available to one another the HIF-1 protein turns on the JMJD2C gene and initiates protein production, which in turn activates the target genes. If the JMJD2C protein is unavailable when breast cancer cells are present then the tumor cells will be less likely to evolve.
This article was interesting because of the detailed information that it provided on cancer and how proteins can be a significant influence towards cancerous genes. The information provided in this article provides hope for a potential target in relation to cancer drug development.
As widespread as Alzheimer’s has become in the elderly community, there is very little known about how it develops. What is known is that its has to with a plaque build up of a small protein called A-beta. The question is whether A-beta actually causes the disease or the disease causes A-beta residue from its activity, but the trend in research is pointing toward the first theory.
A-beta has been targeted in several studies and the findings show that if it is limited, so is the effects of the disease. There are two ways that A-beta is being dealt with, directly and at its origins. A-beta is part of a larger protein called Amyloidbeta (APP) that is cleave by two different enzymes called beta-secretase & gamma-secretase. The first of two medications in trial stages, blocks the gamma-secretase so it doesn’t cut the APP and cause the A-beta debry to build up. The second medication builds up immunity against the A-beta by slowly injecting it into the body and having the immune system get use to it as a foreigner & attacking it.
I find this article extremely relevant to today’s society. There are so many seniors with Alzheimer’s or some form of dimensia that creates barriers between themselves and their family, when they are in a lonely stage of life to begin with. Just as keeping an active lifestyle improves physical health, I believe that staying mentally active is the best way to prevent the on coming of this disease. Hopefully modern science will eventually find a safe way to prevent the disease as well.
It is a widespread misconception that all proteins need to fold into their rigid 4° structure before they are active. They are required to be shaped specifically for target molecules with precise active sites and catalytic sites. However it is beginning to emerge that there are many proteins that don’t take on a structure at all. And they are extremely active.
The lack of folding was always considered pathology, that lead to disease and limited function, but to be fluid is now believed to be crucial for some proteins functions. In fact, about 1/3 of the body’s proteins are thought to be “intrinsically Disordered” having at least some unfolded or disordered parts. This fluidity allows proteins to adapt to different target molecules and perform more than the traditionally thought one task. There is also evidence that these types of proteins may have been the first to evolve, performing several tasks in life’s early evolution.
I think there is a lot of sense behind this discovery. Our body’s functions and different metabolic pathways are so complex and efficient, that modern science can’t duplicate them. Science has come along way in the past couple hundred years, but do to the technological evolution that we live in, there will be a lot more advances, and insights to come. This is still the beginning.
According to the New York Times, signs of Alzheimer’s disease can be found years before the individual develops the first symptoms of the disease. the studies, published in the journal Lancet Neurology, show how scientists used an extended family that had 5,000 individuals who had a genetic ancestor with Alzheimer’s. it showed how the researchers could find changes in the brain that were connected to the disease almost 20 years before the person showed any actual mental deterioration. in this family, the changes in the brain were shown as early as 18 to 26 years of age. the actual signs of mental deterioration didn’t appear until the individuals were about 45 years old and reached the dementia stage at 53 years old.
The changes in the brain occur earlier than the formation of the plaques that cause the disease. the protein called beta amyloid is the milestone for the disease. it is known that this protein is found at a higher than normal level in the body and it is found in the spinal cord of a young adult. the researchers believe that the memory encoding proteins in the brain are being overworked at this young age. this shows that the individual will eventually have Alzheimer’s because by the time these proteins are suppose to be working harder, they won’t be able to.
They also noticed that the areas in the brain that will be modified by the disease will be smaller than individuals who will not be affected by the disease. this family was a perfect tool for research because about a third of this family is attacked by Alzheimer’s by the time they are in the midlife. they also have a rare type of this disease which is caused by a genetic mutation. with such a large sample size, the researchers were able to identify who would have the disease and who wouldn’t.
Being able to identify whether a person will have Alzheimer’s is a great tool to have. this is help individuals find a way to prevent or slow down the effects of the disease. it was fascinating to know that the researchers were able to pin point who in the family would get the disease. they were able to find several mutations that would affect an individual and would help the disease progress. they used many different techniques to find their results including brain imaging and research about mutations and proteins.
Researchers at MedUni Vienna’s Institute of Medical Genetics discovered two genes (TSC/Tuberin and PRAS40) are extremely important regulators in the development of stem cells. If these genes are switched off, the stem cells will not develop and instead die a programmed cell death. The leader Markus Hengstschager, Director of Institute of Medical Genetics published a journal in Human Molecular Genetics that these stem cells need both proteins to develop and be involved in regeneration and differentiation processes in cell death. The human body maintains a stable equilibrium between cell death and the breakdown of tissue and the regeneration of tissues in stem cells. Stems cells are also rebuilding tissues in your skin, muscle, or nerve cells. A human cell can live up to two days. Skin cells live up to four weeks. A lung cell dies around 80 days, and red blood cells die within 120 days. These two poteins are highly essential to make these tissues for the cells, and cannot regenrate without it.
This is fasinating and scary. This shows how every protein, cell, or whatever is needed to make the body function to produce the tissues needed in your body. It is crazy that if something is taken away from the ingredients to produce a tissue nothing will be made, and what is even crazier instead of regenrating it will degenrate it and will cause death within the cell! Researchers need to create some sort of pill to help regenrate the absent of proteins. what if your body is just uncapable of producing those proteins?