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Titolo:
Nitric oxide synthase in skeletal muscle fibers: a signaling component of the dystrophin-glycoprotein complex
Autore:
Grozdanovic, Z; Baumgarten, HG;
Indirizzi:
Freeumorv Berlin, Klinikum Benjamin Franklin, Inst Anat, Dept Neurobiol & T Free Univ Berlin Berlin Germany D-14195 n, Inst Anat, Dept Neurobiol & T
Titolo Testata:
HISTOLOGY AND HISTOPATHOLOGY
fascicolo: 1, volume: 14, anno: 1999,
pagine: 243 - 256
SICI:
0213-3911(199901)14:1<243:NOSISM>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
DUCHENNE-MUSCULAR-DYSTROPHY; DENSITY PROTEIN PSD-95; I NOS-I; STRIATED-MUSCLE; REACTIVE OXYGEN; EXTRACELLULAR-MATRIX; MOUSE SKELETAL; END-PLATE; NEUROMUSCULAR-JUNCTIONS; RELAXING FACTOR;
Keywords:
nitric oxide synthase; nitric oxide; skeletal muscle; dystrophin; muscular dystrophy;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
116
Recensione:
Indirizzi per estratti:
Indirizzo: Grozdanovic, Z Freeumorv Berlin, Klinikum Benjamin Franklin, Inst Anat, Dept Neurobiol & T Free Univ Berlin Konigin Luise Str 15 Berlin Germany D-14195
Citazione:
Z. Grozdanovic e H.G. Baumgarten, "Nitric oxide synthase in skeletal muscle fibers: a signaling component of the dystrophin-glycoprotein complex", HIST HISTOP, 14(1), 1999, pp. 243-256

Abstract

The present review deals with the anatomical distribution, physiological importance, and pathological implications of the neuronal-type nitric oxide synthase (nNOS) in skeletal muscle. Throughout the body, nNOS is located beneath the sarcolemma of skeletal muscle fibers. In rodents, nNOS is enriched in type IIb muscle fibers, but is more homogenously distributed among type II and type I fibers in humans and subhuman primates. It is accumulated on the postsynaptic membrane at the neuromuscular junction. An increased concentration of nNOS is noted at the sarcolemma of muscle spindle fibers, in particular nuclear bag fibers, which belong to type I fibers. The association of nNOS with the sarcolemma is mediated by the dystrophin-glycoprotein complex. Specifically, nNOS is linked to alpha 1-syntrophin through PDZ domain interactions. Possibly, it also directly binds to dystrophin. The activity and expression of nNOS are regulated by both myogenic and neurogenic factors. Besides acetylcholine, glutamate has also been shown to stimulate nNOS, probably acting through N-methyl-D-aspartate receptors, which are colocalized with nNOS at the junctional sarcolemma. Functional studies have implicated nitric oxide as a modulator of skeletal muscle contractility, mitochondrial respiration, carbohydrate metabolism, and neuromuscular transmission. A clinically relevant aspect of nNOS is its absence from the skeletal muscle sarcolemma of patients with Duchenne muscular dystrophy (DMD). A concept is presented which suggests that, as a consequence of the disruption of the dystrophin-glyoprotein complex in DMD, nNOS fails to become attached to the sarcolemma and is subject to downregulation in the cytosol.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 04:58:42