Linked Life Data

9394043

Source:http://linkedlifedata.com/resource/pubmed/id/9394043

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-2-2
pubmed:abstractText
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 1 (NMDAR-1) has been detected in the postjunctional sarcolemma of rat diaphragm, providing a clue as to the possible source of Ca2+ ions that are necessary for NOS I 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. NOS I was also present in the extrajunctional sarcolemma of this fiber type. Dystrophin, beta-dystroglycan, alpha-sarcoglycan, 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 I at neuromuscular junctions of type II fibers. The evidence that glutamate may function as a messenger molecule at vertebrate neuromuscular junction is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0302-766X
pubmed:author
pubmed:issnType
Print
pubmed:volume
291
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
57-63
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:9394043-Animals, pubmed-meshheading:9394043-Cricetinae, pubmed-meshheading:9394043-Cytoskeletal Proteins, pubmed-meshheading:9394043-Dystroglycans, pubmed-meshheading:9394043-Dystrophin, pubmed-meshheading:9394043-Female, pubmed-meshheading:9394043-Gerbillinae, pubmed-meshheading:9394043-Guinea Pigs, pubmed-meshheading:9394043-Male, pubmed-meshheading:9394043-Membrane Glycoproteins, pubmed-meshheading:9394043-Membrane Proteins, pubmed-meshheading:9394043-Mesocricetus, pubmed-meshheading:9394043-Mice, pubmed-meshheading:9394043-Mice, Inbred mdx, pubmed-meshheading:9394043-Muscle, Skeletal, pubmed-meshheading:9394043-Muscle Fibers, Skeletal, pubmed-meshheading:9394043-Neuromuscular Junction, pubmed-meshheading:9394043-Nitric Oxide Synthase, pubmed-meshheading:9394043-Rats, pubmed-meshheading:9394043-Rats, Wistar, pubmed-meshheading:9394043-Receptors, N-Methyl-D-Aspartate, pubmed-meshheading:9394043-Sarcoglycans, pubmed-meshheading:9394043-Sarcolemma, pubmed-meshheading:9394043-Species Specificity, pubmed-meshheading:9394043-Spectrin, pubmed-meshheading:9394043-Utrophin
pubmed:year
1998
pubmed:articleTitle
Co-localization of nitric oxide synthase I (NOS I) and NMDA receptor subunit 1 (NMDAR-1) at the neuromuscular junction in rat and mouse skeletal muscle.
pubmed:affiliation
Institute of Anatomy, Department of Molecular Anatomy and Cell Biology, University Clinic Benjamin Franklin, Free University of Berlin, D-14195 Berlin, Germany.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't