Activation of Protein Kinase C by Triton X-100 Mixed Micelles Containing Diacylglycerol and Phosphatidylserine*
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TLDR
A mixed micellar assay for protein kinase C was developed to investigate the specificity and stoichiometry of activation by phospholipids and diacylglycerols and establishes that a phospholIPid bilayer is not required for protein Kinase C activation and that activation of monomeric protein kinases C occurs.About:
This article is published in Journal of Biological Chemistry.The article was published on 1985-08-25 and is currently open access. It has received 438 citations till now. The article focuses on the topics: Protein kinase C & Micelle.read more
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Journal ArticleDOI
Studies and perspectives of protein kinase C
TL;DR: A novel role of this protein kinase system seems to give a logical basis for clarifying the biochemical mechanism of signal transduction, and to add a new dimension essential to the understanding of cell-to-cell communication.
Journal ArticleDOI
Functions of sphingolipids and sphingolipid breakdown products in cellular regulation
Yusuf A. Hannun,Robert M. Bell +1 more
TL;DR: The discovery that breakdown products of cellular sphingolipids are biologically active and inhibit protein kinase C, a pivotal enzyme in cell regulation and signal transduction has generated interest in the role of these molecules in cell physiology and pathology.
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Protein kinase C isoenzymes: divergence in signal transduction?
TL;DR: In this article, the authors describe a system of rather different cellular components assembled to guarantee a specific and successful process of signal transduction between the signal and the gene, which are evolutionarily conserved and ubiquitously distributed amongst living organisms.
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Sphingosine inhibition of protein kinase C activity and of phorbol dibutyrate binding in vitro and in human platelets
TL;DR: It is suggested that sphingosine will be a useful inhibitor for investigating the function of protein kinase C in vitro and in living cells.
Book
Protein Kinase C
TL;DR: The evidence now suggests that the type of protein kinase C in a cell may govern the nature and mechanisms of functional responses.
References
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The role of protein kinase C in cell surface signal transduction and tumour promotion
TL;DR: Protein kinase C probably serves as a receptor for the tumour promoters and further exploration of the roles of this enzyme may provide clues for understanding the mechanism of cell growth and differentiation.
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Direct activation of calcium-activated, phospholipid-dependent protein kinase by tumor-promoting phorbol esters
TL;DR: Kinetic analysis indicates that TPA can substitute for diacylglycerol and greatly increases the affinity of the enzyme for Ca2+ as well as for phospholipid, and various phorbol derivatives which have been shown to be active in tumor promotion are also capable of activating this protein kinase in in vitro systems.
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Inositol trisphosphate and diacylglycerol as second messengers.
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Turnover of inositol phospholipids and signal transduction
TL;DR: Various extracellular informational signals such as those from a group of hormones and some neurotransmitters appear to be passed from the cell surface into the cell interior by two routes, protein kinase C activation and Ca2+ mobilization.
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Activation of calcium and phospholipid-dependent protein kinase by diacylglycerol, its possible relation to phosphatidylinositol turnover.
TL;DR: A possible coupling is proposed between the protein kinase activation and phosphatidylinositol turnover which can be provoked by various extracellular messengers.