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rdf:type |
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lifeskim:mentions |
umls-concept:C0007634,
umls-concept:C0017262,
umls-concept:C0185023,
umls-concept:C0185117,
umls-concept:C0237497,
umls-concept:C0248537,
umls-concept:C0439855,
umls-concept:C1314939,
umls-concept:C1314972,
umls-concept:C1710236,
umls-concept:C1947904,
umls-concept:C1999228,
umls-concept:C2825781,
umls-concept:C2911684
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pubmed:issue |
1
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pubmed:dateCreated |
1996-9-25
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pubmed:abstractText |
Dystrophin and alpha- and gamma-sarcoglycans were newly expressed in BC3H1 cells during differentiation induced by serum withdrawal. These proteins formed a tight complex with other dystophin-associated proteins (DAPs), as detected by immunoprecipitation with anti-dystrophin antibody. Integrins beta 1 and beta 3, vinculin, and focal adhesion kinase were also detected in the same immunoprecipitate. In a cell adhesion assay, differentiated BC3H1 cells attached more efficiently to type I collagen-coated dishes than nondifferentiated cells and loss of alpha-sarcoglycan induced by antisense ODN in differentiated cells resulted in significant inhibition of cell adhesion. Thus dystrophin and DAPs, at least partly, form a complex with the focal adhesion proteins in differentiated BC3H1 cells and alpha-sarcoglycan seems to modulate the function of the focal adhesion complex in these cells.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, Serum-Free,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dystrophin,
http://linkedlifedata.com/resource/pubmed/chemical/Focal Adhesion Kinase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Focal Adhesion Protein-Tyrosine...,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotides, Antisense,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Ptk2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Sarcoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Vinculin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
225
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11-5
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8769087-Animals,
pubmed-meshheading:8769087-Base Sequence,
pubmed-meshheading:8769087-Binding Sites,
pubmed-meshheading:8769087-Blood,
pubmed-meshheading:8769087-Cell Adhesion Molecules,
pubmed-meshheading:8769087-Cell Differentiation,
pubmed-meshheading:8769087-Cell Line,
pubmed-meshheading:8769087-Culture Media, Serum-Free,
pubmed-meshheading:8769087-Cytoskeletal Proteins,
pubmed-meshheading:8769087-Dystrophin,
pubmed-meshheading:8769087-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8769087-Focal Adhesion Kinase 1,
pubmed-meshheading:8769087-Focal Adhesion Protein-Tyrosine Kinases,
pubmed-meshheading:8769087-Immunoblotting,
pubmed-meshheading:8769087-Integrins,
pubmed-meshheading:8769087-Kinetics,
pubmed-meshheading:8769087-Membrane Glycoproteins,
pubmed-meshheading:8769087-Mice,
pubmed-meshheading:8769087-Molecular Sequence Data,
pubmed-meshheading:8769087-Oligonucleotides, Antisense,
pubmed-meshheading:8769087-Protein Binding,
pubmed-meshheading:8769087-Protein-Tyrosine Kinases,
pubmed-meshheading:8769087-Sarcoglycans,
pubmed-meshheading:8769087-Vinculin
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pubmed:year |
1996
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pubmed:articleTitle |
Expression of a dystrophin-sarcoglycan complex in serum-deprived BC3H1 cells and involvement of alpha-sarcoglycan in substrate attachment.
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pubmed:affiliation |
Department of Molecular Physiology, National Cardiovascular Center Research Institute, Osaka, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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