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(Received for publication, August 19, 1997, and in revised form, September 5, 1997)
From the There is currently a great interest in
identifying laminin isoforms expressed in developing and regenerating
skeletal muscle. Laminin
Volume 272, Number 45,
Issue of November 7, 1997
pp. 28590-28595
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Presence of Laminin
5 Chain and Lack of Laminin 1 Chain
during Human Muscle Development and in Muscular Dystrophies
,
and
Department of Animal Physiology, Uppsala
University, BMC, Box 596, S-751 24 Uppsala, Sweden,
§ The Cutaneous Biology Research Center, Harvard Medical
School, Massachusetts General Hospital, Charlestown, MA 02142-1299, and
the ¶ Department of Anatomy, Umeå University, S-901 87 Umeå, Sweden
1 has been reported to localize to human
fetal muscle and to be induced in muscular dystrophies based on
immunohistochemistry with the monoclonal antibody 4C7, suggested to
recognize the human laminin 1 chain. Nevertheless, there seems to be
no expression of laminin 1 protein or mRNA in developing or
dystrophic mouse skeletal muscle fibers. To address the discrepancy
between the results obtained in developing and dystrophic human and
mouse muscle we expressed the E3 domain of human laminin 1 chain as a recombinant protein and made antibodies specific for human laminin 1 chain (anti-hLN-1G4/G5). We also made antibodies to the human laminin 5 chain purified from placenta. In the present report we
show that hLN-1G4/G5 antibodies react with a 400-kDa laminin 1
chain and that 4C7 reacts with a 380-kDa laminin 5 chain. Immunohistochemistry with the hLN-1G4/G5 antibody and 4C7 revealed that the two antibodies stained human kidney, developing and dystrophic muscle in distinct patterns. Our data indicate that the previously reported expression patterns in developing, adult, and dystrophic human
muscle tissues with 4C7 should be re-interpreted as an expression of
laminin 5 chain. Our data are also consistent with earlier work in
mouse, indicating that laminin 1 is largely an epithelial laminin
chain not present in developing or dystrophic muscle fibers.
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