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Published March 15, 1983 | public
Journal Article Open

Involvement of spectrin in cell-surface receptor capping in lymphocytes


Human and mouse lymphocytes of T- and B-cell lineages express a protein (Mr, 240,000) that crossreacts with antibodies raised against chicken erythrocyte α-spectrin as judged by immunofluorescence, immunoprecipitation, and immunoautoradiography; by the same criteria, antibodies raised against chicken erythrocyte β-spectrin do not react with any lymphocyte polypeptide. In all T and B cells analyzed, before surface-directed ligand challenge with concanavalin A and surface immunoglobulins the polypeptide antigenically related to erythrocyte α-spectrin is distributed diffusely at the plasma membrane. Upon challenge, the redistribution of this polypeptide is concurrent with that of the cell-surface receptors initially in patches and then in a cap. Immunoprecipitation of NaDodSO4-solubilized lymphocytes with erythrocyte α-spectrin antiserum shows that in all cases a polypeptide with the same apparent molecular weight as erythrocyte α-spectrin is precipitated. Variable amounts of another polypeptide (Mr, 235,000) are also coimmunoprecipitated. Immunoprecipitations and subsequent immunoautoradiography show that the lymphocyte polypeptide doublet has a composition similar to that of (brain) fodrin, a polypeptide doublet that previously has been found mainly in the cells of nervous tissue.

Additional Information

© 1983 by the National Academy of Sciences. Communicated by Leroy E. Hood, November 18, 1982. We are grateful to the following members of the Division of Biology, California Institute of Technology, who donated the lymphoid cell lines used in this study: Drs. D. Teplow, E. Rothenberg, A. Orn, J. Brockes, and L. Carlsson. We are also grateful to Dr. L.E. Hood for his helpful comments on the manuscript. This work was supported by grants from the National Institutes of Health, the National Science Foundation, and the Muscular Dystrophy Association of America and by a Biomedical Research Support grant to the Division of Biology, California Institute of Technology. W.J.N. was also supported by an International Fellowship from the Cancer Research Campaign awarded by the International Union Against Cancer; C.A.L.S.C. was supported by a British-American Research Fellowship from the American Heart Association and the British Heart Foundation; E.L. is a recipient of a Research Career Development Award from the National Institutes of Health. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.


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