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      Resistance exercise increases active MMP and β1‐integrin protein expression in skeletal muscle

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          Abstract

          Recent studies indicate that matrix metalloproteinases (MMPs) and critical linkage proteins in the extracellular matrix (ECM) regulate skeletal muscle mass, although the effects of resistance training (RT) on protein expression and activity are unclear. Thus, the purpose of the present study was to investigate the effects of RT on MMP activity and expression of ECM‐related proteins. Ten male Sprague–Dawley rats were randomly assigned to 1 bout (1B) or 18 bouts (18B) of electrical stimulation. The right gastrocnemius muscle was isometrically contracted via percutaneous electrical stimulation (five sets of 5 sec stimulation × five contractions/set with 5 sec interval between contractions and 3 min rest between sets) once (1B) or every other day for 5 weeks (18B). The left leg served as a control. Activity of MMP‐2 and MMP‐9, determined via gelatin zymography, was increased ( P <0.05) immediately after 1B. However, MMP activation was not evident following 18B. No changes in collagen IV, laminin α2, α7‐integrin, or ILK protein expression were detected immediately following 1B or 18B. However, β1‐integrin protein expression was significantly increased ( P <0.05) with 18B. Our results suggest that resistance exercise activates MMPs during the initial phase of RT but this response is attenuated with continuation of RT.

          Abstract

          Recent studies indicate that matrix metalloproteinases (MMPs) and critical linkage proteins in the extracellular matrix (ECM) regulate skeletal muscle mass, although the effects of resistance training (RT) on protein expression and activity are unclear. Our results suggest that resistance exercise activates MMPs during the initial phase of RT but this response is attenuated with continuation of RT.

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          Coomassie staining as loading control in Western blot analysis.

          In Western blotting, immunodetection of housekeeping proteins is routinely performed to detect differences in electrophoresis loading. The present work describes a much faster and simpler protein staining method, which is compatible with ordinary blocking conditions. In addition, the method can be used after immunodetection with superior linearity compared to ordinary staining methods. After immunoblotting and staining, protein bands can be further identified using peptide mass fingerprinting.
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            Structural, biochemical, cellular, and functional changes in skeletal muscle extracellular matrix with aging.

            The extracellular matrix (ECM) of skeletal muscle is critical for force transmission and for the passive elastic response of skeletal muscle. Structural, biochemical, cellular, and functional changes in skeletal muscle ECM contribute to the deterioration in muscle mechanical properties with aging. Structural changes include an increase in the collagen concentration, a change in the elastic fiber system, and an increase in fat infiltration of skeletal muscle. Biochemical changes include a decreased turnover of collagen with potential accumulation of enzymatically mediated collagen cross-links and a buildup of advanced glycation end-product cross-links. Altered mechanotransduction, poorer activation of satellite cells, poorer chemotactic and delayed inflammatory responses, and a change in modulators of the ECM are important cellular changes. It is possible that the structural and biochemical changes in skeletal muscle ECM contribute to the increased stiffness and impairment in force generated by the contracting muscle fibers seen with aging. The cellular interactions provide and potentially coordinate an adaptation to mechanical loading and ensure successful regeneration after muscle injury. Some of the changes in skeletal muscle ECM with aging may be preventable with resistance or weight training, but it is clear that more human studies are needed on the topic. © 2011 John Wiley & Sons A/S.
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              Translational signaling responses preceding resistance training-mediated myofiber hypertrophy in young and old humans.

              While skeletal muscle protein accretion during resistance training (RT)-mediated myofiber hypertrophy is thought to result from upregulated translation initiation signaling, this concept is based on responses to a single bout of unaccustomed resistance exercise (RE) with no measure of hypertrophy across RT. Further, aging appears to affect acute responses to RE, but whether age differences in responsiveness persist during RT leading to impaired RT adaptation is unclear. We therefore tested whether muscle protein fractional synthesis rate (FSR) and Akt/mammalian target of rapamycin (mTOR) signaling in response to unaccustomed RE differed in old vs. young adults, and whether age differences in acute responsiveness were associated with differences in muscle hypertrophy after 16 wk of RT. Fifteen old and 21 young adult subjects completed the 16-wk study. The phosphorylation states of Akt, S6K1, ribosomal protein S6 (RPS6), eukaryotic initiation factor 4E (eIF4E) binding protein (4EBP1), eIF4E, and eIF4G were all elevated (23-199%) 24 h after a bout of unaccustomed RE. A concomitant 62% increase in FSR was found in a subset (6 old, 8 young). Age x time interaction was found only for RPS6 phosphorylation (+335% in old subjects only), while there was an interaction trend (P = 0.084) for FSR (+96% in young subjects only). After 16 wk of RT, gains in muscle mass, type II myofiber size, and voluntary strength were similar in young and old subjects. In conclusion, at the level of translational signaling, we found no evidence of impaired responsiveness among older adults, and for the first time, we show that changes in translational signaling after unaccustomed RE were associated with substantial muscle protein accretion (hypertrophy) during continued RT.
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                Author and article information

                Journal
                Physiol Rep
                Physiol Rep
                physreports
                phy2
                Physiological Reports
                Wiley Periodicals, Inc.
                2051-817X
                November 2014
                20 November 2014
                : 2
                : 11
                : e12212
                Affiliations
                [1 ]Department of Life Sciences, The University of Tokyo, Tokyo, Japan
                [2 ]Faculty of Sport and Health Science, Ritsumeikan University, Shiga, Japan
                [3 ]Graduate School of Health and Sport Science, Nippon Sport Science University, Tokyo, Japan
                [4 ]Department of Kinesiology and Community Health, Beckman Institute for Advanced Science and Technology, University of Illinois, Urbana, Illinois
                Author notes
                CorrespondenceRiki Ogasawara, Department of Life Sciences, The University of Tokyo, 3‐8‐1 Komaba, Meguro, Tokyo 153‐8902, Japan. Tel: +81‐3‐5454‐6868 Fax: +81‐3‐5454‐4317 E‐mail: ogasawara@ 123456idaten.c.u-tokyo.ac.jp
                Article
                phy212212
                10.14814/phy2.12212
                4255818
                25413329
                7960371e-16ec-4eac-9832-76d1e863de16
                © 2014 The Authors. Physiological Reports published by Wiley Periodicals, Inc. on behalf of the American Physiological Society and The Physiological Society.

                This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

                History
                : 04 September 2014
                : 22 October 2014
                : 24 October 2014
                Categories
                Original Research

                exercise,gelatinases,integrin,mtor,muscle hypertrophy
                exercise, gelatinases, integrin, mtor, muscle hypertrophy

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