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Absence of laminin α1 chain in the skeletal muscle of dystrophic dy/dy mice
Author(s) -
Tiger CarlFredrik,
Gullberg Donald
Publication year - 1997
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/(sici)1097-4598(199712)20:12<1515::aid-mus6>3.0.co;2-b
Subject(s) - laminin , blot , immunohistochemistry , skeletal muscle , duchenne muscular dystrophy , muscular dystrophy , microbiology and biotechnology , monoclonal antibody , biology , antibody , chemistry , endocrinology , medicine , immunology , biochemistry , extracellular matrix , gene
In Duchenne muscular dystrophy (DMD) and laminin α2 defective congenital muscular dystrophies (CMD) there are reports of an induction of laminin α1 chain in regenerating muscle fibers. These studies are based on immunohistochemistry data with one monoclonal antibody alone. Based on these data we sought to establish if the laminin α1 chain is induced in the muscle of dy/dy mice. We found no evidence of induction of laminin α1 chain protein or mRNA in dystrophic dy/dy skeletal muscle fibers as determined by immunohistochemistry, Western blotting, Northern blotting, or PCR analysis. Our data point to the need for additional immunological reagents specific for human laminin‐α1 to resolve whether the conflicting data on laminin‐α1 distribution in human and mouse tissues is due to species differences or, alternatively, due to differences in reagent specificity. Our data might be important when designing therapy strategies for CMD. © 1997 John Wiley & Sons, Inc. Muscle Nerve 20: 1515–1524, 1997