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J. Biol. Chem., Vol. 275, Issue 27, 20355-20360, July 7, 2000
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From the Expression of the brain natriuretic peptide (BNP)
gene in cultured neonatal rat ventricular myocytes is activated by
mechanical strain in vitro. We explored the role of
cell-matrix contacts in initiating the strain-dependent
increment in human BNP (hBNP) promoter activity. Coating the culture
surface with fibronectin effected a dose-dependent increase
in basal hBNP luciferase activity and amplification of the
response to strain. Preincubation of myocytes with an RGD peptide
(GRGDSP) or with soluble fibronectin, each of which would be predicted
to compete for cell-matrix interactions, resulted in a
dose-dependent reduction in strain-dependent
hBNP promoter activity. A functionally inert RGE peptide (GRGESP) was without effect. Using fluorescence-activated cell sorting, we demonstrated the presence of
Integrin Dependence of Brain Natriuretic Peptide Gene Promoter
Activation by Mechanical Strain*
,¶
Metabolic Research Unit, the
§ Lung Biology Center, and the ¶ Department of
Medicine, University of California,
San Francisco, California 94143
1, 3, and
v5 integrins in myocytes as well as
non-myocytes and 1 only in non-myocytes in our cultures. Inclusion
of antibodies directed against 1, 3, or
v5, but not 1,
2, or cadherin, was effective in blocking the BNP
promoter response to mechanical strain. These same antibodies
(anti-3, -1, and
-v5) had a similar inhibitory effect on
strain-stimulated ERK, p38 MAPK, and, to a lesser extent, JNK
activities in these cells. Cotransfection with chimeric integrin
receptors capable of acting as dominant-negative inhibitors of integrin
function demonstrated suppression of strain-dependent BNP
promoter activity when vectors encoding 1 or
3, but not 5, 5, or a
carboxyl-terminal deletion mutant of 3
(3B), were employed. These studies underscore the
importance of cell-matrix interactions in controlling cardiac gene
expression and suggest a potentially important role for these interactions in signaling responses to mechanical stimuli within the myocardium.
*
This work was supported by Grant HL 35753 from the National
Institutes of Health and Grant-in-aid 9950062N from the American Heart
Association.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.
To whom correspondence should be addressed: Metabolic Research
Unit, University of California, 513 Parnassus Ave., P. O. Box 0540, San Francisco, CA 94143. Tel.: 415-476-2729; Fax: 415-476-1660; E-mail:
gardner@itsa.ucsf.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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