Abstract
Protein kinase C (PKC) is a key enzyme involved in regulation of growth and differentiated function (Nishizuka, 1986). In vitro, the enzymatic activity requires both calcium and phospholipids. The neutral lipid, diacylglycerol, also interacts with PKC and decreases the Kact for calcium to concentrations compatible with those found in the cytoplasm. DAG is considered to be the key regulator of PKC activation state in vivo. This is due to the fact that cellular levels of DAG are tightly coupled to hormonal activation of phospholipase C. Tumor promoting phorbol esters mimic diacylglycerol with respect to binding to and activating PKC. Infact, PKC is the major cellular receptor for phorbol esters (Castagna, et al., 1982; Niedel, et al., 1983). It is for this reason that phorbol esters are so often used as specific tools for exploring the role of PKC in biological processes.
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© 1990 Plenum Press, New York
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Jaken, S., Kiley, S.C., Klauck, T., Dong, L., Hyatt, S. (1990). Immunocytochemical Localization of Protein Kinase C. In: Vanderhoek, J.Y. (eds) Biology of Cellular Transducing Signals. GWUMC Department of Biochemistry Annual Spring Symposia. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0559-0_25
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DOI: https://doi.org/10.1007/978-1-4613-0559-0_25
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