Elsevier

Methods in Enzymology

Volume 201, 1991, Pages 340-347
Methods in Enzymology

[28] Use and specificity of staurosporine, UCN-O1, and calphostin C as protein kinase inhibitors

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Publisher Summary

This chapter discusses the use and specificity of staurosporine, UCN-01, and calphostin C as protein kinase inhibitors. Protein kinases are classified into protein-serine/threonine kinases and protein-tyrosine kinases. Many protein kinases have been identified as protein-serine/threonine kinases; for example, cAMP-dependent, cGMP-dependent, Ca2+/phospholipid-dependent protein kinases, and oncogenic protein kinases, such as the mos and raf proteins. The Ca2+/phospholipid-dependent protein kinase (protein kinase C) is a protein-serine/threonine kinase involved in the regulation of many cellular processes, including cellular growth, differentiation, and tumor promotion. The primary structure of protein kinase C has two functional domains—the catalytic domain and the regulatory domain. The carboxyl terminal region of protein kinase C is the catalytic domain, and the aminoterminal region has cysteine-rich repeats and is presumed to be the regulatory domain, which has phospholipid and diacylglycerol/phorbol ester binding regions.

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