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J. Biol. Chem., Vol. 277, Issue 17, 15021-15027, April 26, 2002
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From the Activation of protein kinase C (PKC)
Nitric Oxide (NO) Induces Nitration of Protein Kinase
C
(PKC), Facilitating PKC Translocation via Enhanced
PKC-RACK2 Interactions
A NOVEL MECHANISM OF NO-TRIGGERED ACTIVATION OF PKC
*
§,§,§,,§,,§¶
Department of Physiology and Biophysics,
University of Louisville, Louisville, Kentucky 40202 and the
§ Department of Medicine, Division of Cardiology,
Louisville, Kentucky 40202
by
nitric oxide (NO) has been implicated in the development of
cardioprotection. However, the cellular mechanisms underlying
the activation of PKC by NO remain largely unknown. Nitration of
protein tyrosine residues has been shown to alter functions of a
variety of proteins, and NO-derived peroxynitrite is known as a strong
nitrating agent. In this investigation, we demonstrate that NO
donors promote translocation and activation of PKC in an NO- and
peroxynitrite-dependent fashion. NO induces
peroxynitrite-mediated tyrosine nitration of PKC in rabbit
cardiomyocytes in vitro, and nitrotyrosine residues were also detected on PKC in vivo in the rabbit myocardium
preconditioned with NO donors. Furthermore, coimmunoprecipitation of
PKC and its receptor for activated
C kinase, RACK2, illustrated a
peroxynitrite-dependent increase in PKC-RACK2
interactions in NO donor-treated cardiomyocytes. Moreover, using an
enzyme-linked immunosorbent assay-based protein-protein interaction
assay, PKC proteins treated with the peroxynitrite donor SIN-1
exhibited enhanced binding to RACK2 in an acellular environment. Our
data demonstrate that post-translational modification of PKC by NO
donors, namely nitration of PKC, facilitates its interaction with
RACK2 and promotes translocation and activation of PKC. These
findings offer a plausible novel mechanism by which NO activates the
PKC signaling pathway.
*
This work was supported in part by NHLBI, National
Institutes of Health Grants HL-63901 and HL-65431 (to P. P.) and
HL-43151, HL-55757, and HL-68088 (to R. B.), American Heart
Association National Center Grant-in-aid 9750721N (to P. P.), by the
Commonwealth of Kentucky Research Challenge Trust Fund, and by the
Jewish Hospital Research Foundation, Louisville, Kentucky.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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