Ca2+ pool emptying stimulates Ca2+ entry activated by S- nitrosylation

Cécile J. Favre, Carmen A. Ufret-Vincenty, Michele R. Stone, Hong Tao Ma, Donald L. Gill

Research output: Contribution to journalArticlepeer-review

38 Scopus citations

Abstract

The entry of Ca2+ following Ca2+ pool release is a major component of Ca2+ signals; yet despite intense study, how 'store-operated' entry channels are activated is unresolved. Because S-nitrosylation has become recognized as an important regulatory modification of several key channel proteins, its role in Ca2+ entry was investigated. A novel class of lipophilic NO donors activated Ca2+ entry independent of the well defined NO target, guanylate cyclase. Strikingly similar entry of Ca2+ induced by cell permeant alkylators indicated that this Ca2+ entry process was activated through thiol modification. Significantly, Ca2+ entry activated by either NO donors or alkylators was highly stimulated by Ca2+ pool depletion, which increased both the rate of Ca2+ release and the sensitivity to thiol modifiers. The results indicate that S-nitrosylation underlies activation of an important store-operated Ca2+ entry mechanism.

Original languageEnglish (US)
Pages (from-to)30855-30858
Number of pages4
JournalJournal of Biological Chemistry
Volume273
Issue number47
DOIs
StatePublished - Nov 20 1998

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Ca<sup>2+</sup> pool emptying stimulates Ca<sup>2+</sup> entry activated by S- nitrosylation'. Together they form a unique fingerprint.

Cite this