Dephosphorylation of activated protein kinase C contributes to downregulation by bryostatin

Dephosphorylation of activated protein kinase C contributes to downregulation by bryostatin

Dephosphorylation predisposes protein kinase C to proteolysis. Greater production of the 76-kDa form of protein kinase C explains the more efficient downregulation of the kinase by bryostatin versus phorbol 12-myristate 13-acetate.

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Veröffentlicht in:American Journal of Physiology: Cell Physiology 1996-07, Vol.40 (1), p.C304-C311
Hauptverfasser: LEE, H.-W, SMITH, L, PETTIT, G. R, BINGHAM SMITH, J
Format: Artikel
Sprache:eng
Schlagworte:
Antineoplastic agents
Biological and medical sciences
Cells
Cellular biology
General aspects
Medical sciences
Pharmacology. Drug treatments
Proteins
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Zusammenfassung:Dephosphorylation predisposes protein kinase C to proteolysis. Greater production of the 76-kDa form of protein kinase C explains the more efficient downregulation of the kinase by bryostatin versus phorbol 12-myristate 13-acetate.
ISSN:0363-6143
1522-1563