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Titolo:
COLOCALIZATION OF NITRIC-OXIDE SYNTHASE-I (NOS-I) AND NMDA RECEPTOR SUBUNIT-1 (NMDAR-1) AT THE NEUROMUSCULAR-JUNCTION IN RAT AND MOUSE SKELETAL-MUSCLE
Autore:
GROZDANOVIC Z; GOSSRAU R;
Indirizzi:
FREE UNIV BERLIN,UNIV CLIN BENJAMIN FRANKLIN,DEPT MOL ANAT & CELL BIOL,INST ANAT D-14195 BERLIN GERMANY FREE UNIV BERLIN,UNIV CLIN BENJAMIN FRANKLIN,DEPT MOL ANAT & CELL BIOL,INST ANAT D-14195 BERLIN GERMANY
Titolo Testata:
Cell and tissue research
fascicolo: 1, volume: 291, anno: 1998,
pagine: 57 - 63
SICI:
0302-766X(1998)291:1<57:CONS(A>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLUTAMATE-LIKE IMMUNOREACTIVITY; DUCHENNE MUSCULAR-DYSTROPHY; DENSITY PROTEIN PSD-95; SARCOLEMMA; FIBERS; HISTOCHEMISTRY; EXPRESSION; DEFICIENT;
Keywords:
NITRIC OXIDE SYNTHASE I; NMDA RECEPTORS; SKELETAL MUSCLE; TYPE II FIBERS; NEUROMUSCULAR JUNCTION; NEUROMUSCULAR TRANSMISSION; MDX MICE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
Z. Grozdanovic e R. Gossrau, "COLOCALIZATION OF NITRIC-OXIDE SYNTHASE-I (NOS-I) AND NMDA RECEPTOR SUBUNIT-1 (NMDAR-1) AT THE NEUROMUSCULAR-JUNCTION IN RAT AND MOUSE SKELETAL-MUSCLE", Cell and tissue research, 291(1), 1998, pp. 57-63

Abstract

Nitric oxide synthase I (NOS I) has been localized to the skeletal muscle sarcolemma in a variety of vertebrate species including man. It is particularly enriched at neuromuscular junctions. Recently, the N-methyl-D-aspartate (NMDA) receptor subunit I (NMDAR-1) has been detectedin the postjunctional sarcolemma of rat diaphragm, providing a clue as to the possible source of Ca2+ ions that are necessary for NOS 1 activation. To address this possibility, we studied the distribution of NMDAR-1 and NOS I in mouse and rat skeletal muscles by immunohistochemistry and enzyme histochemistry. NMDAR-1 and NOS I were closely associated at neuromuscular junctions primarily of type II muscle fibers. NOSI was also present in the extrajunctional sarcolemma of this fiber type. Dystrophin, beta-dystroglycan, alpha-sarcoglycan, can, and spectrin were found normally expressed in both the junctional and extrajunctional sarcolemma of both fiber types. By contrast, in the muscle sarcolemma of MDX mice, dystrophin and dystrophin-associated proteins were reduced or absent. NOS I immunoreactivity was lost from the extrajunctional sarcolemma and barely detectable in the junctional sarcolemma. NOS I activity was clearly demonstrable in the junctional sarcolemma by NADPH diaphorase histochemistry, especially when the two-step method was used. NMDAR-1 was not altered. These data suggest that different mechanisms act to attach NOS I to the junctional versus extrajunctional sarcolemma. It may further be postulated that NMDA receptors are involved not only in the regulation but also sarcolemmal targeting of NOS Iat neuromuscular junctions of type II fibers. The evidence that glutamate may function as a messenger molecule at vertebrate neuromuscular junction is discussed.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 22:04:37