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. 1983 Mar;80(6):1626–1630. doi: 10.1073/pnas.80.6.1626

Involvement of spectrin in cell-surface receptor capping in lymphocytes.

W J Nelson, C A Colaço, E Lazarides
PMCID: PMC393655  PMID: 6572928

Abstract

Human and mouse lymphocytes of T- and B-cell lineages express a protein (Mr, 240,000) that crossreacts with antibodies raised against chicken erythrocyte alpha-spectrin as judged by immunofluorescence, immunoprecipitation, and immunoautoradiography; by the same criteria, antibodies raised against chicken erythrocyte beta-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 alpha-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 alpha-spectrin antiserum shows that in all cases a polypeptide with the same apparent molecular weight as erythrocyte alpha-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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ash J. F., Louvard D., Singer S. J. Antibody-induced linkages of plasma membrane proteins to intracellular actomyosin-containing filaments in cultured fibroblasts. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5584–5588. doi: 10.1073/pnas.74.12.5584. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bennett V., Davis J., Fowler W. E. Brain spectrin, a membrane-associated protein related in structure and function to erythrocyte spectrin. Nature. 1982 Sep 9;299(5879):126–131. doi: 10.1038/299126a0. [DOI] [PubMed] [Google Scholar]
  3. Bourguignon L. Y., Singer S. J. Transmembrane interactions and the mechanism of capping of surface receptors by their specific ligands. Proc Natl Acad Sci U S A. 1977 Nov;74(11):5031–5035. doi: 10.1073/pnas.74.11.5031. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Branton D., Cohen C. M., Tyler J. Interaction of cytoskeletal proteins on the human erythrocyte membrane. Cell. 1981 Apr;24(1):24–32. doi: 10.1016/0092-8674(81)90497-9. [DOI] [PubMed] [Google Scholar]
  5. Burridge K. Direct identification of specific glycoproteins and antigens in sodium dodecyl sulfate gels. Methods Enzymol. 1978;50:54–64. doi: 10.1016/0076-6879(78)50007-4. [DOI] [PubMed] [Google Scholar]
  6. Cheung W. Y. Calmodulin plays a pivotal role in cellular regulation. Science. 1980 Jan 4;207(4426):19–27. doi: 10.1126/science.6243188. [DOI] [PubMed] [Google Scholar]
  7. De Petris S. Inhibition and reversal of capping by cytochalasin B, vinblastine and colchicine. Nature. 1974 Jul 5;250(461):54–56. doi: 10.1038/250054a0. [DOI] [PubMed] [Google Scholar]
  8. Donnelly M. S., Weinberg D. S., Skarin A. T., Levine H. D. Sick sinus syndrome with seroconstrictive pericarditis in malignant lymphoma involving the heart: a case report. Med Pediatr Oncol. 1981;9(3):273–277. doi: 10.1002/mpo.2950090311. [DOI] [PubMed] [Google Scholar]
  9. Dragsten P., Henkart P., Blumenthal R., Weinstein J., Schlessinger J. Lateral diffusion of surface immunoglobulin, Thy-1 antigen, and a lipid probe in lymphocyte plasma membranes. Proc Natl Acad Sci U S A. 1979 Oct;76(10):5163–5167. doi: 10.1073/pnas.76.10.5163. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Edelman G. M. Surface modulation in cell recognition and cell growth. Science. 1976 Apr 16;192(4236):218–226. doi: 10.1126/science.769162. [DOI] [PubMed] [Google Scholar]
  11. Flanagan J., Koch G. L. Cross-linked surface Ig attaches to actin. Nature. 1978 May 25;273(5660):278–281. doi: 10.1038/273278a0. [DOI] [PubMed] [Google Scholar]
  12. Glenney J. R., Jr, Glenney P., Weber K. Erythroid spectrin, brain fodrin, and intestinal brush border proteins (TW-260/240) are related molecules containing a common calmodulin-binding subunit bound to a variant cell type-specific subunit. Proc Natl Acad Sci U S A. 1982 Jul;79(13):4002–4005. doi: 10.1073/pnas.79.13.4002. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Glenney J. R., Jr, Glenney P., Weber K. F-actin-binding and cross-linking properties of porcine brain fodrin, a spectrin-related molecule. J Biol Chem. 1982 Aug 25;257(16):9781–9787. [PubMed] [Google Scholar]
  14. Goodman S. R., Zagon I. S., Kulikowski R. R. Identification of a spectrin-like protein in nonerythroid cells. Proc Natl Acad Sci U S A. 1981 Dec;78(12):7570–7574. doi: 10.1073/pnas.78.12.7570. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Granger B. L., Lazarides E. Synemin: a new high molecular weight protein associated with desmin and vimentin filaments in muscle. Cell. 1980 Dec;22(3):727–738. doi: 10.1016/0092-8674(80)90549-8. [DOI] [PubMed] [Google Scholar]
  16. Hubbard B. D., Lazarides E. Copurification of actin and desmin from chicken smooth muscle and their copolymerization in vitro to intermediate filaments. J Cell Biol. 1979 Jan;80(1):166–182. doi: 10.1083/jcb.80.1.166. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Klausner R. D., Bhalla D. K., Dragsten P., Hoover R. L., Karnovsky M. J. Model for capping derived from inhibition of surface receptor capping by free fatty acids. Proc Natl Acad Sci U S A. 1980 Jan;77(1):437–441. doi: 10.1073/pnas.77.1.437. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Koch G. L., Smith M. J. An association between actin and the major histocompatibility antigen H-2. Nature. 1978 May 25;273(5660):274–278. doi: 10.1038/273274a0. [DOI] [PubMed] [Google Scholar]
  19. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  20. Lazarides E., Nelson W. J. Expression of spectrin in nonerythroid cells. Cell. 1982 Dec;31(3 Pt 2):505–508. doi: 10.1016/0092-8674(82)90306-3. [DOI] [PubMed] [Google Scholar]
  21. Levine J., Willard M. Fodrin: axonally transported polypeptides associated with the internal periphery of many cells. J Cell Biol. 1981 Sep;90(3):631–642. doi: 10.1083/jcb.90.3.631. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Lingappa V. R., Lingappa J. R., Prasad R., Ebner K. E., Blobel G. Coupled cell-free synthesis, segregation, and core glycosylation of a secretory protein. Proc Natl Acad Sci U S A. 1978 May;75(5):2338–2342. doi: 10.1073/pnas.75.5.2338. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Loor F. Binding and redistribution of lectins on lymphocyte membrane. Eur J Immunol. 1974 Mar;4(3):210–220. doi: 10.1002/eji.1830040311. [DOI] [PubMed] [Google Scholar]
  24. Nelson W. J., Lazarides E. Expression of the beta subunit of spectrin in nonerythroid cells. Proc Natl Acad Sci U S A. 1983 Jan;80(2):363–367. doi: 10.1073/pnas.80.2.363. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Nicolson G. L. Transmembrane control of the receptors on normal and tumor cells. I. Cytoplasmic influence over surface components. Biochim Biophys Acta. 1976 Apr 13;457(1):57–108. doi: 10.1016/0304-4157(76)90014-9. [DOI] [PubMed] [Google Scholar]
  26. Palfrey H. C., Schiebler W., Greengard P. A major calmodulin-binding protein common to various vertebrate tissues. Proc Natl Acad Sci U S A. 1982 Jun;79(12):3780–3784. doi: 10.1073/pnas.79.12.3780. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Repasky E. A., Granger B. L., Lazarides E. Widespread occurrence of avian spectrin in nonerythroid cells. Cell. 1982 Jul;29(3):821–833. doi: 10.1016/0092-8674(82)90444-5. [DOI] [PubMed] [Google Scholar]
  28. Salisbury J. L., Condeelis J. S., Maihle N. J., Satir P. Calmodulin localization during capping and receptor-mediated endocytosis. Nature. 1981 Nov 12;294(5837):163–166. doi: 10.1038/294163a0. [DOI] [PubMed] [Google Scholar]
  29. Sobue K., Muramoto Y., Fujita M., Kakiuchi S. Calmodulin-binding protein of erythrocyte cytoskeleton. Biochem Biophys Res Commun. 1981 Jun 16;100(3):1063–1070. doi: 10.1016/0006-291x(81)91931-8. [DOI] [PubMed] [Google Scholar]
  30. Stackpole C. W., Aoki T., Boyse E. A., Old L. J., Lumley-Frank J., De Harven E. Cell surface antigens: serial sectioning of single cells as an approach to topographical analysis. Science. 1971 Apr 30;172(3982):472–474. doi: 10.1126/science.172.3982.472. [DOI] [PubMed] [Google Scholar]
  31. Weihing R. R. The cytoskeleton and plasma membrane. Methods Achiev Exp Pathol. 1979;8:42–109. [PubMed] [Google Scholar]

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