Matrix metalloproteinase-2 mediates stretch-induced activation of skeletal muscle satellite cells in a nitric oxide-dependent manner

Michiko Yamada, Yoriko Sankoda, Ryuichi Tatsumi, Wataru Mizunoya, Yoshihide Ikeuchi, Kenji Sunagawa, Ronald E. Allen

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Abstract

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.

Original languageEnglish
Pages (from-to)2183-2191
Number of pages9
JournalInternational Journal of Biochemistry and Cell Biology
Volume40
Issue number10
DOIs
Publication statusPublished - Mar 12 2008

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Skeletal Muscle Satellite Cells
Hepatocyte Growth Factor
Matrix Metalloproteinase 2
Muscle
Nitric Oxide
Chemical activation
Satellites
Matrix Metalloproteinases
Extracellular Matrix
Recombinant proteins
Endopeptidases
Tissue Inhibitor of Metalloproteinase-1
Nitric Oxide Donors
Nitroprusside
Conditioned Culture Medium
Cell culture
Recombinant Proteins
Nitric Oxide Synthase
Zinc
Rats

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Cell Biology

Cite this

Matrix metalloproteinase-2 mediates stretch-induced activation of skeletal muscle satellite cells in a nitric oxide-dependent manner. / Yamada, Michiko; Sankoda, Yoriko; Tatsumi, Ryuichi; Mizunoya, Wataru; Ikeuchi, Yoshihide; Sunagawa, Kenji; Allen, Ronald E.

In: International Journal of Biochemistry and Cell Biology, Vol. 40, No. 10, 12.03.2008, p. 2183-2191.

Research output: Contribution to journalArticle

Yamada, Michiko ; Sankoda, Yoriko ; Tatsumi, Ryuichi ; Mizunoya, Wataru ; Ikeuchi, Yoshihide ; Sunagawa, Kenji ; Allen, Ronald E. / Matrix metalloproteinase-2 mediates stretch-induced activation of skeletal muscle satellite cells in a nitric oxide-dependent manner. In: International Journal of Biochemistry and Cell Biology. 2008 ; Vol. 40, No. 10. pp. 2183-2191.
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AU - Sunagawa, Kenji

AU - Allen, Ronald E.

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