Abstract
Tyrosine phosphorylation of cytoskeletal proteins at adhesive junctions has been speculated to play a role in the regulation of cell signaling at these sites. Previously, monoclonal antibodies were generated against phosphotyrosine-containing proteins from Rous sarcoma virus-transformed chick embryo fibroblasts, resulting in two antibodies which recognized antigens of 76 and 215 kDa that localized to focal contacts. We have now localized the 215-kDa antigen to a number of adhesive junctions in vivo, including the zonula adherens, intercalated discs, and myotendinous and neuromuscular junctions. In sections of skeletal muscle and in isolated myofibrils, the 215-kDa protein was localized to the I-band. By immunoprecipitation and immunoblot analysis, we determined that the 215-kDa antigen cross-reacts with a polyclonal anti-tensin antibody.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Antibodies, Monoclonal
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Avian Sarcoma Viruses / genetics
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Cell Adhesion Molecules / analysis*
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Cell Adhesion Molecules / immunology
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Chick Embryo
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Cross Reactions
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Epithelial Cells
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Fibroblasts / cytology
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Fluorescent Antibody Technique
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Immunoblotting
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Intercellular Junctions / ultrastructure*
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Lens, Crystalline / cytology
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Microfilament Proteins / analysis*
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Microfilament Proteins / immunology
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Molecular Weight
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Muscle, Smooth / cytology
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Muscles / cytology
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Myocardium / cytology
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Myofibrils / ultrastructure
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Phosphoproteins / analysis*
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Phosphorylation
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Phosphotyrosine
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Rats
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Tensins
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Tyrosine / analogs & derivatives
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Tyrosine / analysis
Substances
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Antibodies, Monoclonal
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Cell Adhesion Molecules
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Microfilament Proteins
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Phosphoproteins
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Tensins
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Tns1 protein, rat
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Phosphotyrosine
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Tyrosine