Title : Role of protein kinase C in phosphorylation of vinculin in adriamycin-resistant HL-60 leukemia cells.

Pub. Date : 1988 Jun 15

PMID : 3130982






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 In response to phorbol esters such as 12-O-tetradecanoylphorbol-13-acetate (TPA), HL-60 cells differentiate to macrophage-like cells and exhibit the ability to phosphorylate vinculin in vitro. Tetradecanoylphorbol Acetate vinculin Homo sapiens
2 In response to phorbol esters such as 12-O-tetradecanoylphorbol-13-acetate (TPA), HL-60 cells differentiate to macrophage-like cells and exhibit the ability to phosphorylate vinculin in vitro. Tetradecanoylphorbol Acetate vinculin Homo sapiens
3 Coincident with these changes after TPA treatment was a reduction in Ca2+ and phospholipid-independent phosphorylation of vinculin in vitro in extracts from HL-60/ADR cells, whereas HL-60 cells exhibited an elevation of this phosphoprotein. Tetradecanoylphorbol Acetate vinculin Homo sapiens
4 The phosphorylation of vinculin in TPA-treated HL-60 cells or untreated HL-60/ADR cells was blocked by antibodies to protein kinase C. Tetradecanoylphorbol Acetate vinculin Homo sapiens