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Calcium mobilization in permeabilized fibroblasts effects of inositol trisphosphate o vanadate mitogens phorbol ester and gtp

, : Calcium mobilization in permeabilized fibroblasts effects of inositol trisphosphate o vanadate mitogens phorbol ester and gtp. Journal of Cellular Physiology 130(1): 29-36

Utilizing a digitonin-permeabilized cell system, we have studied the release of calcium from a non-mitochondria intracelular compartment in cultured human fibroblasts (HSWP cells). Addition of 1 mM MgATP to a monolayer of permeabilized cells in a cytosolic media buffered to 150 nM Ca with EGTA rapidly stimulates 45Ca uptake, and the subsequent addition of the putative intracellular messenger inositol triphosphate (InsP3) induces rapid release of 85% (.+-. 6% n = 6) of the 45Ca taken up in response to ATP. Mitogenic peptides (bradykinin, vasopressin, epidermal growth factor [EGF], and insulin) and orthovanadate, which are effective in mobilizing intracellular Ca in intact cells, have little or no effect when added alone to permeabilized cells. However, in the presence of GTP these agents stimulate accumulation of inositol phosphates and release Ca from the InsP3-sensitive pool. These data suggest that a GTP bindng protein is involved in receptor mediated activation of phosholipase C, which leads to release of inositol phosphates. The GTP-dependent release of InsP3 and the mobilization of 45Ca from the intracellular compartment are inhibited by pretreatment of cells, prior to permeabilization, with the protein kinase C activator 12-O-tetradecanoyl-phorbol-13-acetate (TPA). TPA preteatment does not affect the InsP3 stimulated Ca release. These results suggest that protein kinase C is involved in down-regulation or inhibition of phospholipase C, or the GTP binding protein responsible for relaying the mitogenic signal from the cell surface receptor to the phospholipase C activity.


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