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Laminin α1 chain mediated reduction of laminin α2 chain deficient muscular dystrophy involves integrin α7β1 and dystroglycan
Author(s) -
Gawlik Kinga I.,
Mayer Ulrike,
Blomberg Kristina,
Sonnenberg Arnoud,
Ekblom Peter,
Durbeej Madeleine
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.02.027
Subject(s) - laminin , sarcolemma , dystroglycan , muscular dystrophy , integrin , itga7 , chemistry , congenital muscular dystrophy , transgene , genetically modified mouse , chain (unit) , microbiology and biotechnology , protein subunit , myocyte , biology , extracellular matrix , biochemistry , gene , genetics , cell , physics , astronomy
Transgenically introduced laminin (LN) α1 chain prevents muscular dystrophy in LNα2 chain deficient mice. We now report increased integrin α7Bβ1D synthesis in dystrophic LNα2 chain deficient muscle. Yet, immunofluorescence demonstrated a reduced expression of integrin α7B subunit at the sarcolemma. Transgenic expression of LNα1 chain reconstituted integrin α7B at the sarcolemma. Expression of α‐ and β‐dystroglycan is enhanced in LNα2 chain deficient muscle and normalized by transgenic expression of LNα1 chain. We suggest that LNα1 chain in part ameliorates the development of LNα2 chain deficient muscular dystrophy by retaining the binding sites for integrin α7Bβ1D and α‐dystroglycan, respectively.