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Researchers Discover The Secrets Of Protein Kinase C

Scientists at the San Diego School of Medicine have published a new study in Cell Reports which reveals a more accurate structure of the protein Kinase C (PKC), a family of enzymes that is known to control the activity of other proteins in the cells. As a result of this work, the researchers have been able to provide new drug targets for neurodegenerative diseases and cancer.

What is PKC?
Protein Kinase C is family of enzymes that are able to control other protein activity in a cell by attaching chemical tags to them. This action determines whether a cell lives or dies. When the process is interrupted or changed, it may result in a number of diseases. The work carried out by the researchers at the University of California offers new targets for fine-tuning the activity of these enzymes in order to improve the function of the cells.


Professor of pharmacology, Alexandra Newton, explains that PKC has the ability to clamp itself closed and so, once they understand how these enzymes do this, they can look for ways to keep it open and doing its job. By doing so, it opens up possibilities for the development of more targeted therapies for cancer, as keeping the enzyme in its open position will encourage the death of the tumour cells. Conversely, it would be possible to do the opposite when dealing with degenerative diseases, where the aim would be to develop a treatment that would keep the tumours alive.


Researchers used a sophisticated cellular imaging technique


In the past, scientists have a used a technique called X-ray crystallography to uncover the structure of proteins, however they soon found that the identified structure didn’t equate with the biology of how the enzymes actually work. With this in mind, the researchers at UC San Diego School of Medicine began to look at different ways to test the structure using a sophisticated cellular imaging technique. This allowed them to find the processes that came into play during chemical tagging, and understand how the enzymes became locked open or shut. The team were also able to mutate specific parts of the protein, thus allowing them to replicate the unlocking and relocking PKC structures, giving hope that this will be able to used to develop new treatments in the future.

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