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J. Biol. Chem., Vol. 275, Issue 39, 30387-30393, September 29, 2000
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From the Prolonged serum deprivation induces a
structurally and functionally contractile phenotype in about 1/6 of
cultured airway myocytes, which exhibit morphological elongation and
accumulate abundant contractile apparatus-associated proteins. We
tested the hypothesis that transcriptional activation of genes encoding these proteins accounts for their accumulation during this phenotypic transition by measuring the transcriptional activities of the murine
SM22 and human smooth muscle myosin heavy chain promoters during
transient transfection in subconfluent, serum fed or 7 day
serum-deprived cultured canine tracheal smooth muscle cells. Contrary
to our expectation, SM22 and smooth muscle myosin heavy chain promoter
activities (but not viral murine sarcoma virus-long terminal
repeat promoter activity) were decreased in long term serum-deprived myocytes by at least 8-fold. Because serum response factor (SRF) is a required transcriptional activator of these and other
smooth muscle-specific promoters, we evaluated the expression and
function of SRF in subconfluent and long term serum-deprived cells.
Whole cell SRF mRNA and protein were maintained at high levels in
serum-deprived myocytes, but SRF transcription-promoting activity,
nuclear SRF binding to consensus CArG sequences, and nuclear SRF
protein were reduced. Furthermore, immunocytochemistry revealed
extranuclear redistribution of SRF in serum-deprived myocytes; nuclear
localization of SRF was restored after serum refeeding. These results
uncover a novel mechanism for physiological control of smooth
muscle-specific gene expression through extranuclear redistribution of
SRF and consequent down-regulation of its transcription-promoting activity.
Physiological Control of Smooth Muscle-specific Gene Expression
through Regulated Nuclear Translocation of Serum Response Factor*
§,§,,,,,,,,,,,
,, and
Departments of Medicine, Pediatrics,
Pathology, and Pharmacology and Physiological Science, University of
Chicago, the ¶ Howard Hughes Medical Institute, University of
Chicago, Chicago, Illinois 60637, the Center for
Cardiovascular Research, University of Rochester,
Rochester, New York 14642, and the ** Department of Medicine,
University of Pennsylvania,
Philadelphia, Pennsylvania 19104
*
This work was supported by NHLBI, National Institutes of
Health Grants HL56399, HL64095, HL63314, HL20592, HL62572, and HL54685. Immunofluorescence studies were supported by the University of Chicago
Cancer Research Center Digital Light Microsopy Facility.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: University of
Chicago, 5841 S. Maryland Ave., MC 6026, Chicago, IL 60637. Tel.: 773-702-6790; Fax: 773-702-4736; E-mail:
jsolway@medicine.bsd.uchicago.edu.
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