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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1998-6-8
|
| pubmed:abstractText |
Previous findings have led to speculations that decreased concentration of nNOS (neuronal nitric oxide synthase) may underlie some aspects of the pathophysiology of dystrophic muscle. We have tested whether the sparing of extraocular muscles (EOM) in muscular dystrophy is attributable to the presence of normal nNOS concentration and distribution in these muscles. Measurements of total nNOS concentration in control muscle showed that total nNOS comprises approximately 0.05% of total muscle protein, indicating a molar stoichiometry of approximately 60 and 20 to total dystrophin and syntrophin, respectively. Thus, most muscle nNOS is either not associated with the dystrophin complex, or binds to yet unidentified sites in the complex. nNOS concentration was at least two-fold greater in C57 EOM and tibialis anterior (TA) compared with mdx samples. No significant differences in nNOS concentration in EOM versus TA in either mdx or C57 mice were observed, nNOS was concentrated at the sarcolemma of all C57 samples, while mdx nNOS displayed a cytosolic distribution, except in fibers that reverted to express dystrophin. These data show that mdx EOM are spared by a mechanism other than normalized concentration and location of nNOS.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Dystrophin,
http://linkedlifedata.com/resource/pubmed/chemical/Dystrophin-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/syntrophin
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Feb
|
| pubmed:issn |
0960-8966
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
8
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
22-9
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:9565987-Aging,
pubmed-meshheading:9565987-Animals,
pubmed-meshheading:9565987-Cytosol,
pubmed-meshheading:9565987-Dystrophin,
pubmed-meshheading:9565987-Dystrophin-Associated Proteins,
pubmed-meshheading:9565987-Female,
pubmed-meshheading:9565987-Male,
pubmed-meshheading:9565987-Membrane Proteins,
pubmed-meshheading:9565987-Mice,
pubmed-meshheading:9565987-Mice, Inbred C57BL,
pubmed-meshheading:9565987-Mice, Inbred mdx,
pubmed-meshheading:9565987-Muscle, Skeletal,
pubmed-meshheading:9565987-Muscle Development,
pubmed-meshheading:9565987-Muscle Proteins,
pubmed-meshheading:9565987-Muscular Dystrophy, Animal,
pubmed-meshheading:9565987-Nitric Oxide Synthase,
pubmed-meshheading:9565987-Oculomotor Muscles,
pubmed-meshheading:9565987-Reference Values,
pubmed-meshheading:9565987-Sarcolemma
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Sparing of mdx extraocular muscles from dystrophic pathology is not attributable to normalized concentration or distribution of neuronal nitric oxide synthase.
|
| pubmed:affiliation |
Department of Physiological Science, University of California, Los Angeles 90095-1527, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|