The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Phospholipids inhibit proteolysis of protein kinase C alpha by mM calcium-requiring calpain.

The alpha isoform of protein kinase C (PKC alpha) is rapidly hydrolyzed by mM Ca(2+)-requiring calpain (calcium-activated neutral proteinase) under cell-free conditions (Shea et al, 1994, FEBS Lett. 350:223). In the present study, we demonstrate that this hydrolysis is inhibited by phosphatidyl serine, diacylglycerol, phosphatidyl choline, phosphatidyl inositol, and phosphatidic acid. With the exception of phosphatidic acid, these phospholipids did not directly inhibit calpain activity as evidenced by degradation of [14C]azocasein, suggesting that the nature of inhibition of calpain-mediated PKC alpha degradation is due to an effect of phospholipids on PKC alpha conformation. These findings suggest that m calpain-mediated PKC alpha hydrolysis may be specifically minimized at the plasma membrane, and leave open the possibility that such a mechanism exists in situ. In addition, the unique inhibition of calpain activity by phosphatidic acid suggests the existence of a specific mechanism by which this phospholipid regulates PKC alpha activity.[1]

References

  1. Phospholipids inhibit proteolysis of protein kinase C alpha by mM calcium-requiring calpain. Lang, D., Beermann, M.L., Hauser, G., Cressman, C.M., Shea, T.B. Neurochem. Res. (1995) [Pubmed]
 
WikiGenes - Universities