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Cited by 961

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy

Open access
Brenman, Jay E, Chao, Daniel S, Xia, Houhui, Aldape, Ken, Bredt, David S·1995·Cell
DOI 10.1016/0092-8674(95)90471-9
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Abstract

Nitric oxide (NO) is synthesized in skeletal muscle by neuronal-type NO synthase (nNOS), which is localized to sarcolemma of fast-twitch fibers. Synthesis of NO in active muscle opposes contractile force. We show that nNOS partitions with skeletal muscle membranes owing to association of nNOS with dystrophin, the protein mutated in Duchenne muscular dystrophy (DMD). The dystrophin complex interacts with an N-terminal domain of nNOS that contains a GLGF motif. mdx mice and humans with DMD evince a selective loss of nNOS protein and catalytic activity from muscle membranes, demonstrating a novel role for dystrophin in localizing a signaling enzyme to the myocyte sarcolemma. Aberrant regulation of nNOS may contribute to preferential degeneration of fast-twitch muscle fibers in DMD.

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Metadata

Authors
Brenman, J. E., Chao, D. S., Xia, H., Aldape, K., & Bredt, D. S.
Venue
Cell
Publisher
Elsevier BV
Published
1995-09
Volume
82
Issue
5
Pages
743-752
ISSN
0092-8674 (ISSN-L)
DOI
10.1016/0092-8674(95)90471-9
OpenAlex
W2059155059
Cited by
961
References
3
FWCI
16.93
Type
journal article
Language
en
Open access
bronze

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