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J Biol Chem, Vol. 273, Issue 47, 30855-30858, November 20, 1998
From the Department of Biochemistry and Molecular Biology,
University of Maryland School of Medicine,
Baltimore, Maryland 21201
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.
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