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MMP‐9 overexpression improves myogenic cell migration and engraftment
Author(s) -
Morgan Jennifer,
Rouche Andrée,
Bausero Pedro,
Houssaïni Amal,
Gross Jacqueline,
Fiszman Marc Y.,
Alameddine Hala S.
Publication year - 2010
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.21737
Subject(s) - matrix metalloproteinase , zymography , cell migration , blot , cell , microbiology and biotechnology , tissue inhibitor of metalloproteinase , biology , metalloproteinase , matrix metalloproteinase inhibitor , cell culture , chemistry , cancer research , biochemistry , gene , genetics
Myoblast migration requires matrix metalloproteinase (MMP) activity but the contribution of individual MMPs or tissue inhibitors of matrix metalloproteinase (TIMPs), particularly MMP‐9 and TIMP‐1, is lacking. Using two clones derived for differential regulation of MMP‐2, MMP‐9, and TIMP‐1, we correlated protein expression with cell migration. MMP/TIMP regulation was determined by zymography, western blots, and quantitative reverse transcriptase–polymerase chain reaction (qRT‐PCR). Cell migration was compared in vitro and after grafting into nude – mdx mouse muscles. C2M9 clones produced high MMP‐9 and low MMP‐2, and migrated better than C2F clones, which secreted low MMP‐9, but overexpressed MMP‐2 and TIMP‐1. Improvement of C2F invasion by MMP‐9 and inhibition of C2M9 migration by MMP‐9 inhibitor I confirmed the role of MMP‐9 and pointed to potential inhibition by TIMP‐1. Higher complementation achieved by C2M9 grafts corroborated the beneficial effect of MMP‐9 overexpression. Modulation of MMP‐9 expression opens perspectives for improved efficacy of cell therapy for muscular dystrophies. Muscle Nerve, 2010