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Association of the Tetraspan Protein CD9 with Integrins on the Surface of S‐16 Schwann Cells
Author(s) -
Hadjiargyrou Michael,
Kaprielian Zaven,
Kato Nobuo,
Patterson Paul H.
Publication year - 1996
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1996.67062505.x
Subject(s) - integrin , microbiology and biotechnology , tetraspanin , neurite , schwann cell , transmembrane protein , glycoprotein , cell adhesion , immunofluorescence , cell , neural cell adhesion molecule , biology , chemistry , antibody , immunology , receptor , biochemistry , in vitro
The cell surface glycoprotein CD9 is a member of a group of proteins known as the “tetraspan” or “transmembrane 4 superfamily.” Previous work with non‐neural cells has shown that CD9 associates in cis with integrins and small GTP‐binding proteins on the cell surface. To extend our recent findings showing that perturbation of CD9 alters Schwann cell adhesion, proliferation, and migration, as well as neurite outgrowth in sympathetic neurons, we have searched for CD9‐associated proteins in S‐16 Schwann cells. We demonstrate here that CD9 is specifically coprecipitated from S‐16 cell extracts by antibodies against integrins α3, α6, and β1. In addition, double immunofluorescence labeling and co‐capping experiments indicate that CD9 is specifically colocalized with these integrins on the cell membrane of S‐16 Schwann cells.