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New technique reveals cross-talk between 2 essential cellular processes
Date:7/19/2012

its caspase cleavage sites would always tend to block that cleavage. The new evidence suggested otherwise. "We could see that these apoptosis-specific phosphorylations sometimes persisted on caspase-cleaved fragments," said Dix.

Dix and Simon showed that these phosphorylations in some cases had enabled the caspase cleavage events; in others, cleavage events had enabled the phosphorylations. Similarly, they confirmed that some of the kinase enzymes that phosphorylate proteins during apoptosis can't do their jobs until they are cleavage-activated by caspases. "We've tended to study proteolysis and phosphorylation separately, but it's clear that they're intimately associated and need to be looked at as such," Dix said.

Potential Applications in Cancer Treatment

The Cravatt laboratory is now applying the techniques developed in this study to other analyses, starting with studies of apoptosis in a variety of cell types. The cells they used in the just-published study, Jurkat T-cells, are often used to investigate apoptosis because they can be easily induced to undergo the process. "But each cell type has its own set of working proteins, which will give it a distinct signature when it undergoes apoptosis," Cravatt said.

Techniques to detect apoptosis in specific cell types would be useful in cancer diagnostics and therapy. Tumor cells typically have evolved resistance to apoptosis, whereas chemotherapies often kill tumor cells by overcoming that resistance. Dix, Cravatt, and their colleagues are now trying to determine whether certain phosphorylated protein fragments can be used as highly specific "biomarkers" of apoptosis in cancer cells, detectable in a simple blood test. "Such a test would tell you whether or not your cancer drug is working," Cravatt said.

The wealth of data from these apoptosis studies may also help researchers devise new apoptosis-inducing cancer drugs, he notesand apoptosis is merely one cellular p
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Contact: Mika Ono
mikaono@scripps.edu
Scripps Research Institute
Source:Eurekalert  

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