Title : Stimulation of polyphosphoinositide turnover upon activation of protein kinases in human erythrocytes.

Pub. Date : 1988 Mar 11

PMID : 2830906






2 Functional Relationships(s)
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1 Activation of protein kinase C in erythrocytes by 4-beta-phorbol 12-myristate 13-acetate (PMA) resulted in a parallel stimulation (time course and dose response) of the phosphorylation of both membrane proteins (heterodimers of 107 kDa and 97 kDa, protein 4.1 and 4.9, respectively) and of phosphatidylinositol 4-phosphate (PIP) and, to a lesser extent, of phosphatidylinositol 4,5-bisphosphate (PIP2). Tetradecanoylphorbol Acetate erythrocyte membrane protein band 4.1 Homo sapiens
2 Activation of protein kinase C in erythrocytes by 4-beta-phorbol 12-myristate 13-acetate (PMA) resulted in a parallel stimulation (time course and dose response) of the phosphorylation of both membrane proteins (heterodimers of 107 kDa and 97 kDa, protein 4.1 and 4.9, respectively) and of phosphatidylinositol 4-phosphate (PIP) and, to a lesser extent, of phosphatidylinositol 4,5-bisphosphate (PIP2). Tetradecanoylphorbol Acetate erythrocyte membrane protein band 4.1 Homo sapiens