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Regulation of TIMP‐2, MT1‐MMP, and MMP‐2 expression during C2C12 differentiation
Author(s) -
Lluri Gentian,
Jaworski Diane M.
Publication year - 2005
Publication title -
muscle and nerve
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.025
H-Index - 145
eISSN - 1097-4598
pISSN - 0148-639X
DOI - 10.1002/mus.20383
Subject(s) - myogenesis , matrix metalloproteinase , c2c12 , extracellular matrix , microbiology and biotechnology , proteases , biology , myocyte , cellular differentiation , skeletal muscle , downregulation and upregulation , chemistry , endocrinology , biochemistry , enzyme , gene
Matrix metalloproteinases (MMPs) are zinc‐dependent proteases capable of degrading extracellular matrix components. The activity of these proteases is tightly regulated through the actions of the tissue inhibitors of metalloproteinases (TIMPs). Although the regulation of MMPs and TIMPs during physiological and pathological remodeling has been investigated in a number of systems, almost nothing is known about their role in skeletal muscle differentiation. To investigate the role of MMP‐mediated proteolysis during myogenesis, the regulation of TIMP‐2, MT1‐MMP, and MMP‐2 expression was investigated during differentiation of the mouse myoblastic C2C12 cell line. We show that this trio is upregulated coincident with myogenesis. The more diffuse spatial distribution of TIMP‐2 relative to MT1‐MMP and MMP‐2 suggests that TIMP‐2 may exert MMP‐independent functions during myogenesis. Elucidating the regulation of these molecules during muscle differentiation in vitro may lead to a better understanding of their role in pathological processes in muscle tissue in vivo. Muscle Nerve, 2005