Ca2+ entry activated by S-nitrosylation. Relationship to store- operated Ca2+ entry

Hong Tao Ma, Cécile J. Favre, Randen L. Patterson, Michele R. Stone, Donald L. Gill

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

The coupling between Ca2+ pools and store-operated Ca2+ entry channels (SOCs) remains an unresolved question. Recently, we revealed that Ca2+ entry could be activated in response to S-nitrosylation and that this process was stimulated by Ca2+ pool emptying (Favre, C. J., Ufret-Vincenty, C. A., Stone, M. R., Ma, H-T., and Gill, D. L. (1998) J. Biol. Chem. 273, 30855-30858). In DDT1MF-2 smooth muscle cells and DC-3F fibroblasts, Ca2+ entry activated by the lipophilic NO donor, GEA3162 (5-amino-3-(3,4- dichlorophenyl)-1,2,3,4-oxatriazolium), or the alkylator, N-ethylmaleimide, was observed to be strongly activated by transient external Ca2+ removal, closely resembling activation of SOC activity in the same cells. The nonadditivity of SOC and NO donor-activated Ca2+ entry suggested a single entry mechanism. Calyculin A-induced reorganization of the actin cytoskeleton prevented SOC but had no effect on GEA3162-induced Ca2+ entry. However, a single entry mechanism could account for both SOC and NO donor-activated entry if the latter reflected direct modification of the entry channel by S- nitrosylation, bypassing the normal coupling process between channels and pools. Small differences between SOC and GEA3162-activated Ba2+ entry and sensitivity to blockade by La3+ were observed, and in HEK293 cells SOC activity was observed without a response to thiol modification. It is concluded that in some cells, S-nitrosylation modifies an entry mechanism closely related to SOC and/or part of the regulatory machinery for SOC- mediated Ca2+ entry.

Original languageEnglish (US)
Pages (from-to)35318-35324
Number of pages7
JournalJournal of Biological Chemistry
Volume274
Issue number50
DOIs
StatePublished - Dec 10 1999
Externally publishedYes

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Ethylmaleimide
Alkylating Agents
Fibroblasts
Sulfhydryl Compounds
Machinery
Muscle
Actins
Chemical activation
Cells
HEK293 Cells
Actin Cytoskeleton
Smooth Muscle Myocytes
calyculin A

ASJC Scopus subject areas

  • Biochemistry

Cite this

Ma, H. T., Favre, C. J., Patterson, R. L., Stone, M. R., & Gill, D. L. (1999). Ca2+ entry activated by S-nitrosylation. Relationship to store- operated Ca2+ entry. Journal of Biological Chemistry, 274(50), 35318-35324. https://doi.org/10.1074/jbc.274.50.35318

Ca2+ entry activated by S-nitrosylation. Relationship to store- operated Ca2+ entry. / Ma, Hong Tao; Favre, Cécile J.; Patterson, Randen L.; Stone, Michele R.; Gill, Donald L.

In: Journal of Biological Chemistry, Vol. 274, No. 50, 10.12.1999, p. 35318-35324.

Research output: Contribution to journalArticle

Ma, Hong Tao ; Favre, Cécile J. ; Patterson, Randen L. ; Stone, Michele R. ; Gill, Donald L. / Ca2+ entry activated by S-nitrosylation. Relationship to store- operated Ca2+ entry. In: Journal of Biological Chemistry. 1999 ; Vol. 274, No. 50. pp. 35318-35324.
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AB - The coupling between Ca2+ pools and store-operated Ca2+ entry channels (SOCs) remains an unresolved question. Recently, we revealed that Ca2+ entry could be activated in response to S-nitrosylation and that this process was stimulated by Ca2+ pool emptying (Favre, C. J., Ufret-Vincenty, C. A., Stone, M. R., Ma, H-T., and Gill, D. L. (1998) J. Biol. Chem. 273, 30855-30858). In DDT1MF-2 smooth muscle cells and DC-3F fibroblasts, Ca2+ entry activated by the lipophilic NO donor, GEA3162 (5-amino-3-(3,4- dichlorophenyl)-1,2,3,4-oxatriazolium), or the alkylator, N-ethylmaleimide, was observed to be strongly activated by transient external Ca2+ removal, closely resembling activation of SOC activity in the same cells. The nonadditivity of SOC and NO donor-activated Ca2+ entry suggested a single entry mechanism. Calyculin A-induced reorganization of the actin cytoskeleton prevented SOC but had no effect on GEA3162-induced Ca2+ entry. However, a single entry mechanism could account for both SOC and NO donor-activated entry if the latter reflected direct modification of the entry channel by S- nitrosylation, bypassing the normal coupling process between channels and pools. Small differences between SOC and GEA3162-activated Ba2+ entry and sensitivity to blockade by La3+ were observed, and in HEK293 cells SOC activity was observed without a response to thiol modification. It is concluded that in some cells, S-nitrosylation modifies an entry mechanism closely related to SOC and/or part of the regulatory machinery for SOC- mediated Ca2+ entry.

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