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

C J Favre¹, C A Ufret-Vincenty, M R Stone

¹Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland 21201, USA.

The Journal of Biological Chemistry

|November 13, 1998

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S-nitrosylation activates store-operated calcium (Ca2+) entry channels, a key mechanism in cellular Ca2+ signaling. This process involves thiol modification and is enhanced by Ca2+ pool depletion.

Area of Science:

Cellular Physiology
Molecular Biology
Ion Channel Regulation

Background:

Calcium (Ca2+) signaling is crucial for numerous cellular processes.
Store-operated Ca2+ entry is a major pathway for replenishing intracellular Ca2+ stores.
The precise activation mechanism of store-operated Ca2+ entry channels remains elusive.

Purpose of the Study:

To investigate the role of S-nitrosylation in regulating Ca2+ entry.
To determine if S-nitrosylation contributes to the activation of store-operated Ca2+ channels.

Main Methods:

Utilized novel lipophilic nitric oxide (NO) donors to assess Ca2+ entry.
Employed cell-permeant alkylators to investigate thiol modification in Ca2+ entry.
Examined the effect of Ca2+ pool depletion on Ca2+ entry rates and sensitivity to modifiers.

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Main Results:

Lipophilic NO donors induced Ca2+ entry independently of guanylate cyclase.
Cell-permeant alkylators mimicked NO donor effects, indicating activation via thiol modification.
Ca2+ pool depletion significantly enhanced Ca2+ entry induced by both NO donors and alkylators.

Conclusions:

S-nitrosylation is identified as a key mechanism for activating store-operated Ca2+ entry.
Thiol modification of channel proteins underlies this NO-mediated Ca2+ entry pathway.
Ca2+ pool depletion potentiates S-nitrosylation-dependent Ca2+ entry.