| Literature DB >> 2203192 |
Abstract
Under physiological conditions, protein kinase C is active when bound to membranes. Like most membrane-bound enzymes, its activity is dependent on the nature of its lipid environment. In this article, Richard Epand and David Lester describe the relationship between the ability of specific membrane-active agents to alter the biophysical properties of the lipid environment and their potential to modulate protein kinase C activity. They argue that this can lead to a greater understanding of the mechanism of inhibition and activation of protein kinase C through modulation of the bulk biophysical properties of the membrane, and may provide a new approach to the development of a more specific set of inhibitors.Entities:
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Year: 1990 PMID: 2203192 DOI: 10.1016/0165-6147(90)90234-y
Source DB: PubMed Journal: Trends Pharmacol Sci ISSN: 0165-6147 Impact factor: 14.819