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T‐cadherin and signal‐transducing molecules co‐localize in caveolin‐rich membrane domains of vascular smooth muscle cells
Author(s) -
Philippova M.P,
Bochkov V.N,
Stambolsky D.V,
Tkachuk V.A,
Resink T.J
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00598-5
Subject(s) - cadherin , chemistry , vascular smooth muscle , microbiology and biotechnology , biophysics , ve cadherin , signal (programming language) , membrane , cell adhesion molecule , smooth muscle , biology , biochemistry , cell , computer science , endocrinology , programming language
Cadherins are a family of cellular adhesion proteins mediating homotypic cell‐cell binding. In contrast to classical cadherins, T‐cadherin does not possess the transmembrane and cytosolic domains known to be essential for tight mechanical coupling of cells, and is instead attached to the cell membrane by a glycosylphosphatidylinositol (GPI) anchor. This study explores the hypothesis that T‐cadherin might function as a signal‐transducing protein. Membranes from human and rat vascular smooth muscle cells were fractionated using Triton X‐100 solubilization and density gradient centrifugation techniques. We demonstrate that T‐cadherin is enriched in a minor detergent‐insoluble low‐density membrane domain and co‐distributes with caveolin, a marker of caveolae. This domain was enriched in other GPI‐anchored proteins (CD‐59, uPA receptor) and signal‐transducing molecules (Gαs protein and Src‐family kinases), but completely excluded cell‐cell and cell‐matrix adhesion molecules (N‐cadherin and β1‐integrin). Coupling of T‐cadherin with signalling molecules within caveolae might enable cellular signal transduction.