Acute exercise induced changes in rat skeletal muscle mRNAs and proteins regulating type IV collagen content

Koskinen, Satu; Wang, W.; Ahtikoski, Anne; Kjær, Michael; Han, Xiaoyan; Komulainen, Jyrki; Kovanen, Vuokko; Takala, Tuomo

doi:10.1152/ajpregu.2001.280.5.r1292

Cited by 94 publications

(132 citation statements)

References 47 publications

(41 reference statements)

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“…Contrary to our results for resistance exercise, TIMP1 was not induced with cycling exercise, but MMP9 was induced, suggesting that MMPs and TIMPs display specificity to the mode of exercise, a hypothesis that is supported by animal exercise studies (9,37). With respect to aging muscle, decreased resting levels and a dampened response to exercise for MMP2 and TIMP1 may diminish satellite cell function since in culture MMP2 is produced by human satellite cells and has been shown to be necessary for migration of mouse cells (19,26).…”

Section: Discussioncontrasting

confidence: 96%

Aging alters gene expression of growth and remodeling factors in human skeletal muscle both at rest and in response to acute resistance exercise

Dennis

Przybyla

Gurley

et al. 2008

Physiological Genomics

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The purpose of this investigation was to compare expression of genes that function in inflammation and stress, cell structure and signaling, or remodeling and growth in skeletal muscle of young (32 ± 7 yr, n = 15) and elderly (72 ± 5 yr, n = 16) healthy subjects before and after a bout of resistance leg exercises. A real-time RT-PCR method was used to screen 100 transcripts in v. lateralis biopsies obtained before and 72 h postexercise. The screen identified 15 candidates for differential expression due to aging and/or exercise that were measured quantitatively. The median levels of four mRNAs (insulin-like growth factor-1 and its binding protein IGFBP5, ciliary neurotrophic factor, and the metallopeptidase MMP2) were significantly affected by aging and were greater (1.6- to 2.3-fold, P ≤ 0.05) in the young than elderly muscle at both time points. The median levels of three mRNAs were significantly ( P ≤ 0.05) affected by exercise in the young. The metallopeptidase inhibitor TIMP1 and α-cardiac actin mRNAs increased 2-fold and 6.5-fold, respectively, and GDF8 (myostatin) mRNA decreased by 50%. However, elderly muscle did not display any significant changes in gene expression postexercise. Thus, aging muscle shows decreased levels at rest and an impaired response to exercise for a number of mRNAs for factors potentially involved in muscle growth and remodeling. Future studies must determine the functional importance of these gene expression changes to protein synthesis, satellite cell activity, and other processes that are directly involved in the mechanisms of muscle hypertrophy.

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Section: Discussioncontrasting

confidence: 96%

Aging alters gene expression of growth and remodeling factors in human skeletal muscle both at rest and in response to acute resistance exercise

Dennis

Przybyla

Gurley

et al. 2008

Physiological Genomics

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“…It was previously shown that reorganization of basement membrane compounds needs certain time [15]. As type IV collagen plays a role in regenerative process on extracellular matrix (ECM), including matrix-associated signals and membrane-associated receptors that underline muscle fiber-matrix interactions, it shows how complicated is the evaluation of the functional significance of type IV collagen metabolism [28].…”

Section: Referencesmentioning

confidence: 99%

The effect of unloading and reloading on the extracellular matrix in skeletal muscle: changes in muscle strength and motor activity

Riso¹,

Ahtikoski²,

Takala³

et al. 2010

Biol Sport

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“…Proteolytic degradation of collagen is initiated by matrix metalloproteases (MMPs), and inhibited by tissue inhibitors of metalloproteases (TIMPs). Changes in expression of MMPs and TIMPs were reported in skeletal muscles under hyper-and hypo-active conditions such as joint immobilization (1), unloading (8), tenotomy (26), and running (16). In denervated muscles, the mRNA or protein level expression of MMPs has been investigated in several studies (7,15,21); however, no results are available about the effects of TIMPs.…”

mentioning

confidence: 99%

Regulation of connective tissue remodeling in the early phase of denervation in a rat skeletal muscle

et al. 2013

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Denervation alters the metabolism of the extracellular matrix (ECM) in skeletal muscle; however, the underlying mechanisms of ECM remodeling are not fully understood. The aim of this study was to elucidate the dynamic features of the ECM regulatory process in the early phase of denervated skeletal muscle in male Wistar rats. We investigated the expression of collagens (total, type I, and type III), transforming growth factor beta 1 (TGF-β1), and matrix metalloproteases (MMPs) together with their endogenous inhibitors (TIMPs), at the mRNA and/or protein level in the soleus muscles of control animals and at days 3, 7, and 14 post-denervation. Expression of mRNA encoding collagens was decreased at days 3 and 7, and had recovered by day 14, in parallel with total collagen protein content. Content of TGF-β1 protein was elevated sequentially, up to a maximum of 158% at day 14 post-denervation (P < 0.05), as was TIMP-2 mRNA expression (272% at day 14), whereas MMP-1, MMP-2, and TIMP-1 mRNA expression was not affected at any stage. The initial reduction of collagen mRNA may be responsible for hypoactivity caused by the disappearance of contractile function. Recovery of collagen mRNA/protein at day 14 may be due mainly to the suppressive effects of TGF-β1 on collagen degradation via TIMP-2 upregulation.Denervation causes degenerative changes in skeletal muscles, such as a rapid decrease in muscle volume followed by a reduction in the cross-sectional area of myofibers (2, 22, 24), alteration of myofiber types (22), and disarrangement of sarcomere structures (22). Denervation-induced changes are also observed in intramuscular connective tissue. Intramuscular connective-tissue collagen is mainly composed of types I and III (17). The connective tissue has an important role for muscle function. Length-force characteristics have been shown to be altered by the rupture of intramuscular connective tissue after fasciotomy (14). Therefore, changes in the components of intramuscular connective tissues may impair normal skeletal muscle function, often accompanied by a disturbance in joint mobility. Several studies have reported quantitative changes in intramuscular connective tissue subsequent to non-physiological conditions, but results were inconsistent across studies. Denervation (2, 23), immobilization (13, 24), or unloading (19) lead to increases in collagen concentration in rat calf muscles. Deposition of type-I and -III collagen in the perimysium and epimysium of the gastrocnemius muscle was observed at day 7 post-denervation (23). Concentration of hydroxyproline, a major component of collagen protein, was also increased at 1 and

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Acute exercise induced changes in rat skeletal muscle mRNAs and proteins regulating type IV collagen content

Cited by 94 publications

References 47 publications

Aging alters gene expression of growth and remodeling factors in human skeletal muscle both at rest and in response to acute resistance exercise

Aging alters gene expression of growth and remodeling factors in human skeletal muscle both at rest and in response to acute resistance exercise

The effect of unloading and reloading on the extracellular matrix in skeletal muscle: changes in muscle strength and motor activity

Regulation of connective tissue remodeling in the early phase of denervation in a rat skeletal muscle

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