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Evidence for the regulation of the activity of protein kinase C through changes in membrane properties

EPAND, R. M ; EPAND, R. F ; LEON, B. T.-C ; MENGER, F. M ; KUO, J. F

Bioscience reports, 1991-02, Vol.11 (1), p.59-64 [Periódico revisado por pares]

Colchester: Portland Press

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Título:
Evidence for the regulation of the activity of protein kinase C through changes in membrane properties
Autor: EPAND, R. M ; EPAND, R. F ; LEON, B. T.-C ; MENGER, F. M ; KUO, J. F
Assuntos: Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Calcium - metabolism ; Calorimetry, Differential Scanning ; Cattle ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Hexachlorophene - metabolism ; Lipid Bilayers - metabolism ; Membrane Lipids - metabolism ; Phosphatidylcholines - metabolism ; Phosphatidylserines - metabolism ; Protein Kinase C - antagonists & inhibitors ; Protein Kinase C - metabolism ; Temperature ; Transferases
É parte de: Bioscience reports, 1991-02, Vol.11 (1), p.59-64
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: We measured the effects of two branched-chain analogs of distearoyl-phosphatidylcholine, containing either a methyl or an n-butyl group at the 8 position, on the bilayer to hexagonal phase transition temperature of dielaidoylphosphatidylethanolamine. The former compound raised the bilayer to hexagonal phase transition temperature while the latter compound lowered it. The opposite effects of these amphiphiles on protein kinase C activity (inhibition and activation, respectively) correlated with their effects on lipid polymorphism. Because of the similarity of the structures of these two compounds, it seems likely that their opposite effects on the activity of protein kinase C is a result of their alteration of the lipid environment of the membrane rather than to binding to a specific site on the protein. We also compared the effects of hexachlorophene on lipid polymorphism and protein kinase C activity at high and at low calcium concentrations. We also found that the effect of hexachlorophene forming a complex with Ca2+ is to increase both the hexagonal phase forming propensity of the membrane as well as to increase the activity of protein kinase C, again demonstrating the correlation between lipid phase propensity and effects on protein kinase C activity.
Editor: Colchester: Portland Press
Idioma: Inglês

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Evidence for the regulation of the activity of protein kinase C through changes in membrane properties

EPAND, R. M ; EPAND, R. F ; LEON, B. T.-C ; MENGER, F. M ; KUO, J. F

Colchester: Portland Press

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