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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0017968,
umls-concept:C0018787,
umls-concept:C0036208,
umls-concept:C0079259,
umls-concept:C0185117,
umls-concept:C0386312,
umls-concept:C0449432,
umls-concept:C0521324,
umls-concept:C1135918,
umls-concept:C1179435,
umls-concept:C1524073,
umls-concept:C1548799,
umls-concept:C1705248,
umls-concept:C2911684
|
| pubmed:issue |
25
|
| pubmed:dateCreated |
1996-8-13
|
| pubmed:abstractText |
Caveolae are microdomains of the plasma membrane that have been implicated in signal transduction. Caveolin, a 21-24-kDa integral membrane protein, is a principal component of the caveolae membrane. Recently, we and others have identified a family of caveolin-related proteins; caveolin has been retermed caveolin-1. Caveolin-3 is most closely related to caveolin-1, but caveolin-3 mRNA is expressed only in muscle tissue types. Here, we examine (i) the expression of caveolin-3 protein in muscle tissue types and (ii) its localization within skeletal muscle fibers by immunofluorescence microscopy and subcellular fractionation. For this purpose, we generated a novel monoclonal antibody (mAb) probe that recognizes the unique N-terminal region of caveolin-3, but not other members of the caveolin gene family. A survey of tissues and muscle cell types by Western blot analysis reveals that the caveolin-3 protein is selectively expressed only in heart and skeletal muscle tissues, cardiac myocytes, and smooth muscle cells. Immunolocalization of caveolin-3 in skeletal muscle fibers demonstrates that caveolin-3 is localized to the sarcolemma (muscle cell plasma membrane) and coincides with the distribution of another muscle-specific plasma membrane marker protein, dystrophin. In addition, caveolin-3 protein expression is dramatically induced during the differentiation of C2C12 skeletal myoblasts in culture. Using differentiated C2C12 skeletal myoblasts as a model system, we observe that caveolin-3 co-fractionates with cytoplasmic signaling molecules (G-proteins and Src-like kinases) and members of the dystrophin complex (dystrophin, alpha-sarcoglycan, and beta-dystroglycan), but is clearly separated from the bulk of cellular proteins. Caveolin-3 co-immunoprecipitates with antibodies directed against dystrophin, suggesting that they are physically associated as a discrete complex. These results are consistent with previous immunoelectron microscopic studies demonstrating that dystrophin is localized to plasma membrane caveolae in smooth muscle cells.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Cav3 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cav3 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Caveolin 3,
http://linkedlifedata.com/resource/pubmed/chemical/Caveolins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dystroglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Dystrophin,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sarcoglycans
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
21
|
| pubmed:volume |
271
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
15160-5
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:8663016-Amino Acid Sequence,
pubmed-meshheading:8663016-Animals,
pubmed-meshheading:8663016-Antibodies, Monoclonal,
pubmed-meshheading:8663016-Aorta,
pubmed-meshheading:8663016-Blotting, Western,
pubmed-meshheading:8663016-Caveolin 3,
pubmed-meshheading:8663016-Caveolins,
pubmed-meshheading:8663016-Cell Line,
pubmed-meshheading:8663016-Cercopithecus aethiops,
pubmed-meshheading:8663016-Cytoskeletal Proteins,
pubmed-meshheading:8663016-Dystroglycans,
pubmed-meshheading:8663016-Dystrophin,
pubmed-meshheading:8663016-Epitopes,
pubmed-meshheading:8663016-Female,
pubmed-meshheading:8663016-Immunohistochemistry,
pubmed-meshheading:8663016-Membrane Glycoproteins,
pubmed-meshheading:8663016-Membrane Proteins,
pubmed-meshheading:8663016-Mice,
pubmed-meshheading:8663016-Mice, Inbred BALB C,
pubmed-meshheading:8663016-Molecular Sequence Data,
pubmed-meshheading:8663016-Muscle, Skeletal,
pubmed-meshheading:8663016-Muscle, Smooth, Vascular,
pubmed-meshheading:8663016-Muscle Proteins,
pubmed-meshheading:8663016-Myocardium,
pubmed-meshheading:8663016-Rats,
pubmed-meshheading:8663016-Sarcoglycans,
pubmed-meshheading:8663016-Sarcolemma,
pubmed-meshheading:8663016-Transfection
|
| pubmed:year |
1996
|
| pubmed:articleTitle |
Expression of caveolin-3 in skeletal, cardiac, and smooth muscle cells. Caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins.
|
| pubmed:affiliation |
Whitehead Institute for Biomedical Research, Cambridge, Massachusetts 02142-1479, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|