PMID: 11934646Apr 6, 2002Paper

Calcium-sensing receptor-mediated activation of phospholipase C-gamma1 is downstream of phospholipase C-beta and protein kinase C in MC3T3-E1 osteoblasts

Bone
S L Godwin, S P Soltoff

Abstract

Elevated extracellular calcium (Ca(e)) stimulates both chemotaxis and mitogenesis of MC3T3-E1 osteoblasts via a calcium-sensing receptor (CasR). Ca(e)-mediated chemotaxis of these bone-forming cells is dependent on phospholipase C (PLC) and blocked by the Gi-protein inhibitor pertussis toxin. In this study, we examine the signaling mechanisms by which the CasR stimulates PLC activity in MC3T3-E1 osteoblasts. We found that elevated Ca(e) stimulated PLC-gamma1 tyrosine phosphorylation in a time-dependent and Ca(e)-concentration-dependent manner. The maximal increase in PLC-gamma1 tyrosine phosphorylation was observed 3-5 min after increasing Ca(e) by 3.2 mmol/L from 1.8 mmol/L. Elevated Ca(e) also promoted a rapid increase in both inositol 1,4,5-trisphosphate [Ins(1,4,5)P3], a second messenger formed by PLC-mediated hydrolysis of phosphatidylinositol 4,5-bisphosphate, and cytosolic free calcium ([Ca+2]i). The kinetics of the CasR-mediated increases in Ins(1,4,5)P3 and [Ca+2]i and the sensitivity of the Ca(e)-stimulated elevation in [Ca+2]i to U73122 (a PLC inhibitor) together suggest that the osteoblast CasR is coupled via Gq to PLC-beta. U73122 blocked the Ca(e)-promoted, but not PDGF-promoted, PLC-gamma1 tyrosine phosphorylatio...Continue Reading

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Jul 5, 2008·Journal of Bone and Mineral Metabolism·Toru Yamaguchi
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