TY - JOUR
T1 - Matrix metalloproteinase-2 mediates stretch-induced activation of skeletal muscle satellite cells in a nitric oxide-dependent manner
AU - Yamada, Michiko
AU - Sankoda, Yoriko
AU - Tatsumi, Ryuichi
AU - Mizunoya, Wataru
AU - Ikeuchi, Yoshihide
AU - Sunagawa, Kenji
AU - Allen, Ronald E.
N1 - Funding Information:
This work was supported by grants-in-aid for Scientific Research from Japan Society for the Promotion of science (JSPS) and by grant funds from Ito Foundation and Uehara Memorial Foundation (all to R.T.). The research was also supported by a grant from JSPS Research Fellowship for Yang Scientists (to M.Y.), and by funds from the Arizona Agriculture Experiment Station and grants from the US Department of Agriculture National Research Initiative Competitive Grant Program and the Muscular Dystrophy Association Grant (all to R.E.A.). Authors thank to Dr. N. Hashimoto, National Institute for Longevity Sciences, Japan for technical guidance for PAX7 immunocytochemistry. The mouse monoclonal anti-BrdU antibody developed by S.J. Kaufman, the anti-desmin antibody developed by D.A. Fischman and the anti-PAX7 antibody developed by A. Kawakami were obtained from the Developmental Studies Hybridoma Bank developed under the auspices of the NICHD and maintained by The University of Iowa, Department of Biological Sciences, Iowa City, IA 52242.
PY - 2008
Y1 - 2008
N2 - When skeletal muscle is stretched or injured, myogenic satellite cells are activated to enter the cell cycle. This process depends on nitric oxide (NO) production, release of hepatocyte growth factor (HGF) from the extracellular matrix, and presentation of HGF to the c-met receptor. Matrix metalloproteinases (MMPs), a large family of zinc-dependent endopeptidases, mediate HGF release from the matrix and this step in the pathway is downstream from NO synthesis [Yamada, M., Tatsumi, R., Kikuiri, T., Okamoto, S., Nonoshita, S., Mizunoya, W., et al. (2006). Matrix metalloproteinases are involved in mechanical stretch-induced activation of skeletal muscle satellite cells. Muscle Nerve, 34, 313-319]. Experiments reported herein provide evidence that MMP2 may be involved in the NO-dependent release of HGF in vitro. Whole lysate analyses of satellite cells demonstrated the presence of MMP2 mRNA and the protein. When rat satellite cells were treated with 30 μM sodium nitroprusside a NO donor or mechanical cyclic stretch for 2 h period, inactive proMMP2 (72 kDa) was converted into 52-kDa form and this processing was abolished by adding a NO synthase inhibitor l-NAME (10 μM) to the stretch culture. The 52-kDa species was also generated by treatment of the recombinant MMP2 protein with 1 μM NOC-7 that can spontaneously release NO under physiological conditions without any cofactor, and its activating activity was demonstrated by applying the NOC-7-treated MMP2 to satellite cell culture. HGF release was detected in NOC-7-MMP2-conditioned media by western blotting; very little HGF was found in media that were generated from cultures receiving NOC-7-treated MMP2 (10 ng/ml) plus 250 ng/ml tissue inhibitor-1 of metalloproteinases. Therefore, results from these experiments provide evidence that NO-activated MMP2 may cause release of HGF from the extracellular matrix of satellite cells and contribute to satellite cell activation.
AB - When skeletal muscle is stretched or injured, myogenic satellite cells are activated to enter the cell cycle. This process depends on nitric oxide (NO) production, release of hepatocyte growth factor (HGF) from the extracellular matrix, and presentation of HGF to the c-met receptor. Matrix metalloproteinases (MMPs), a large family of zinc-dependent endopeptidases, mediate HGF release from the matrix and this step in the pathway is downstream from NO synthesis [Yamada, M., Tatsumi, R., Kikuiri, T., Okamoto, S., Nonoshita, S., Mizunoya, W., et al. (2006). Matrix metalloproteinases are involved in mechanical stretch-induced activation of skeletal muscle satellite cells. Muscle Nerve, 34, 313-319]. Experiments reported herein provide evidence that MMP2 may be involved in the NO-dependent release of HGF in vitro. Whole lysate analyses of satellite cells demonstrated the presence of MMP2 mRNA and the protein. When rat satellite cells were treated with 30 μM sodium nitroprusside a NO donor or mechanical cyclic stretch for 2 h period, inactive proMMP2 (72 kDa) was converted into 52-kDa form and this processing was abolished by adding a NO synthase inhibitor l-NAME (10 μM) to the stretch culture. The 52-kDa species was also generated by treatment of the recombinant MMP2 protein with 1 μM NOC-7 that can spontaneously release NO under physiological conditions without any cofactor, and its activating activity was demonstrated by applying the NOC-7-treated MMP2 to satellite cell culture. HGF release was detected in NOC-7-MMP2-conditioned media by western blotting; very little HGF was found in media that were generated from cultures receiving NOC-7-treated MMP2 (10 ng/ml) plus 250 ng/ml tissue inhibitor-1 of metalloproteinases. Therefore, results from these experiments provide evidence that NO-activated MMP2 may cause release of HGF from the extracellular matrix of satellite cells and contribute to satellite cell activation.
KW - Matrix metalloproteinases
KW - Mechanical stretch
KW - Muscle regeneration
KW - Nitric oxide
KW - Satellite cells
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U2 - 10.1016/j.biocel.2008.02.017
DO - 10.1016/j.biocel.2008.02.017
M3 - Article
C2 - 18403250
AN - SCOPUS:48949107707
SN - 1357-2725
VL - 40
SP - 2183
EP - 2191
JO - International Journal of Biochemistry and Cell Biology
JF - International Journal of Biochemistry and Cell Biology
IS - 10
ER -