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1 Division of Kinesiology and Health and 2 Department of Animal Science, University of Wyoming, Laramie, Wyoming 82071; and 3 Department of Animal Sciences, Ohio State University, Wooster, Ohio 44691
We examined the temporal relationship between
messages (type I and type III mRNAs) for the principal fibrillar
procollagens and subsequent collagen accretion, cross-linking, and
decorin expression in the left ventricle (LV) postmyocardial infarction (post-MI). We sought to determine 1) what role the
proteoglycan decorin plays in extracellular matrix (ECM) remodeling
known to take place as a consequence of MI and 2) the extent
skeletal muscle ECM is altered early post-MI. Therefore, after
surgically induced production of small- to moderate-sized infarcts
(~20% of LV mass), extent and time course of ECM remodeling was
evaluated in remaining viable LV free wall and in slow- [soleus
(SOL)] and fast-twitch [gastrocnemius (GAST)] skeletal muscles.
Decorin, collagen, and hydroxylysylpyridinium cross-link concentrations
and 
1(I) (type I) and 1(III) (type III) procollagen mRNAs were
measured in LVs from noninfarcted controls and at 72 h, 1, 2, 5, and 13 wk post-MI. These same data were collected in SOL and GAST
muscles at all time points except 13 wk. Type I procollagen mRNA
increased at both 72-h and 1-wk time points in LVs. Type III
procollagen mRNA was elevated at 1 wk, returning to baseline by 2 wk
post-MI. Collagen concentration was significantly increased by 1 wk,
more than doubled by 5 wk, and was elevated 129% by 13 wk in the
remaining viable LV. LV decorin expression was unaltered at early time
points, but increased 38% at 5 wk post-MI and doubled by 13 wk
post-MI. In skeletal muscle, procollagen mRNAs were transiently altered in SOL and GAST muscles without any demonstrable effect on the measured
ECM parameters. This study reports, for the first time, the
upregulation time course of decorin and its relationship to increased
HP cross-linking and accumulation of collagen in viable myocardium
post-MI.
cardiac remodeling; collagen cross-linking; procollagen mRNA
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