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Text
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URL Address
<a href="http://doi.org/10.1016/j.yjmcc.2008.10.022" target="_blank" rel="noreferrer noopener">http://doi.org/10.1016/j.yjmcc.2008.10.022</a>
Pages
186–192
Issue
2
Volume
46
Dublin Core
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Title
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Cardiac myofibroblast differentiation is attenuated by alpha(3) integrin blockade: potential role in post-MI remodeling.
Publisher
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Journal of molecular and cellular cardiology
Date
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2009
2009-02
Subject
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Animals; Cell Differentiation/*physiology; Collagen Type VI/*metabolism/physiology; Fibroblasts/*cytology; Immunoblotting; Integrin alpha3/*metabolism; Male; Myocardial Infarction/*metabolism; Myocardium/*cytology; Protein Binding; Rats
Creator
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Bryant Jennifer E; Shamhart Patricia E; Luther Daniel J; Olson Erik R; Koshy John C; Costic Donald J; Mohile Monica V; Dockry Michelle; Doane Kathleen J; Meszaros J Gary
Description
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Cardiac fibroblasts and myofibroblasts are responsible for post-MI remodeling which occurs via regulation of extracellular matrix (ECM). Accelerated post-MI remodeling leads to excessive ECM deposition and fibrosis, contributing to impaired contractile function, arrhythmias, and heart failure. We have previously reported that type VI collagen induces myofibroblast differentiation in cultured cardiac fibroblasts, and that type VI collagen and myofibroblast content were both elevated in the myocardium 20 weeks post-MI. The purpose of this study was to determine the expression patterns of type VI collagen and myofibroblast content in early post-myocardial infarction (MI) remodeling to gain insight into whether type VI collagen induces in vivo myofibroblast differentiation via specific matrix-receptor interactions. Adult male Sprague-Dawley rats were anesthetized and left coronary arteries were permanently ligated. Histological tissue sections and whole tissue protein lysates were obtained from infarcted and non-infarcted areas of MI hearts and sham operated controls. At 3 days post-MI, we observed a significant increase in alpha(3) integrin expression (2.02+/-0.18 fold); at 7 days post-infarction both type VI collagen (2.27+/-0.18 fold) and myofibroblast (4.65+/-0.6 fold) content increased. By 14 days myofibroblast content returned to sham control levels, although type VI collagen (2.42+/-0.11 fold) was still elevated. In vitro cross-linking confirmed that the alpha(3) integrin interacts with type VI collagen, and alpha(3) integrin function blocking antibodies inhibited the differentiation of isolated cardiac fibroblasts. Collectively, our in vitro results indicate that the alpha(3) integrin receptor interacts with type VI collagen to promote myofibroblast differentiation, and that this interaction may impact in vivo post-MI remodeling.
Identifier
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<a href="http://doi.org/10.1016/j.yjmcc.2008.10.022" target="_blank" rel="noreferrer noopener">10.1016/j.yjmcc.2008.10.022</a>
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Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
2009
Animals
Bryant Jennifer E
Cell Differentiation/*physiology
Collagen Type VI/*metabolism/physiology
Costic Donald J
Department of Integrative Medical Sciences
Doane Kathleen J
Dockry Michelle
Fibroblasts/*cytology
Immunoblotting
Integrin alpha3/*metabolism
Journal of molecular and cellular cardiology
Koshy John C
Luther Daniel J
Male
Meszaros J Gary
Mohile Monica V
Myocardial Infarction/*metabolism
Myocardium/*cytology
NEOMED College of Medicine
Olson Erik R
Protein Binding
Rats
Shamhart Patricia E