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 language | English (US) |
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Pages (from-to) | 30855-30858 |
Number of pages | 4 |
Journal | Journal of Biological Chemistry |
Volume | 273 |
Issue number | 47 |
DOIs | |
State | Published - Nov 20 1998 |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Cell Biology