Inhibition of Protein Kinase C Phosphorylation by Mono- and Divalent Cations
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1989/07/14
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Personal Author:
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Description:The effect of a matrix of concentrations of Ca2+ (0.01, 0.1, 0.5, 5 mM), Mg2+ (0.2, 0.5, 1, 2, 5, 10 mM), and Na+ (50, 100, 150 mM) on the phosphorylation of histone H-1 by protein kinase C was measured in the presence of 5 mol % diacylglycerol and Mg-ATP in both phosphatidylserine micelles and liposomes formed from a 1:4 mixture of phosphatidylserine and phosphatidylcholine. Monovalent cations (150 mM) reduced activity by 60 and 84% in the micelle and liposome assay systems, respectively. Inhibition was also observed with 5 mM Ca2+ and 10 mM Mg2+. The phosphorylating activity was compared with computer calculations of the negative electrostatic potentials (Psi o) of the phospholipid membranes in the presence of the cations. [Description provided by NIOSH]
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ISSN:0006-291X
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Pages in Document:45-50
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Volume:162
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Issue:1
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NIOSHTIC Number:nn:20060022
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Citation:Biochem Biophys Res Commun 1989 Jul; 162(1):45-50
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Federal Fiscal Year:1989
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Performing Organization:Stanford University, Stanford, California
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Peer Reviewed:True
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Start Date:19800901
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Source Full Name:Biochemical and Biophysical Research Communications
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End Date:19901130
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Main Document Checksum:urn:sha-512:eddb95be6c9a66867e51e0436e5fc0c6c28d9b6667e333acbdca918b51829a457751f4c06e36bcc5d3e0ba51c240c8101c49b58b31095e03b0c3eee27bb49d80
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