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Papers In Press, published online ahead of print May 13, 2003
Department of Surgery, New Jersey Medical School, Newark, NJ 07103
Corresponding Author: hausercj{at}UMDNJ.edu
Store-operated calcium entry (SOCE) is a fundamental mechanism of calcium signaling. The mechanisms linking store depletion to SOCE remain controversial, hypothetically involving both diffusible messengers and conformational coupling of stores to channels. Sphingosine 1-Phosphate (S1P) is a bioactive sphingolipid that can signal via cell surface G-protein-coupled receptors, but S1P can also act as a second messenger, mobilizing calcium directly via unknown mechanisms. We show here that S1P opens calcium entry channels in human neutrophils (PMN) and HL60 cells without prior store depletion, independent of G-proteins and of Phospholipase C. S1P mediated entry has the typical divalent cation permeability profile and inhibitor profile of SOCE in PMN, is fully inhibited by 1mM Gd3+, and is independent of [Ca2+]i. Depletion of PMN calcium stores by thapsigargin induces S1P synthesis. Inhibition of S1P synthesis by dimethylsphingosine blocks thapsigargin-, ionomycin- and PAF-mediated SOCE despite normal store depletion. We propose that S1P is a "Calcium Influx Factor", linking calcium store depletion to downstream SOCE.
J. Biol. Chem, 10.1074/jbc.M301763200
Submitted on February 19, 2003
Revised on May 6, 2003
Accepted on May 13, 2003
Sphingosine 1-phosphate: A diffusible calcium influx factor mediating store-operated calcium entry
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