1
Views
2
CrossRef citations to date
0
Altmetric
Cell Growth and Development

Tyrosine Phosphorylation of a c-Src-Like Protein Is Increased in Membranes of CD4- CD8- T Lymphocytes from lpr/lpr Mice

, , , , &
Pages 4914-4922 | Received 13 Mar 1989, Accepted 27 Jul 1989, Published online: 01 Apr 2023

LITERATURE CITED

  • Amrein, K. E., and B. M. Sefton. 1988. Mutation of a site of tyrosine phosphorylation in the lymphocyte-specific tyrosine protein kinase, p56lck, reveals its oncogenic potential in fibroblasts. Proc. Natl. Acad. Sci. USA 85:4247–4251.
  • Anderson, S. K., C. P. Gibbs, A. Tanaka, H.-J. Kung, and D. J. Fujita. 1985. Human cellular src gene: nucleotide sequence and derived amino acid sequence of the region coding for the carboxy-terminal two-thirds of pp60c-src. Mol. Cell. Biol. 5:1122–1129.
  • Andrews, B. S., R. A. Eisenberg, A. N. Theofilopoulos, S. Izui, C. B. Wilson, P. J. McConahey, E. D. Murphy, J. B. Roths, and F. J. Dixon. 1978. Spontaneous murine lupus-like syndromes. Clinical and immunopathological manifestations in several strains. J. Exp. Med. 148:1198–1215.
  • Badley, J. E., G. A. Bishop, T. St. John, and J. Frelinger. 1988. A simple, rapid method for the purification of poly A+ RNA. BioTechniques 6:114–116.
  • Bolen, J. B., A. Veillette, A. M. Schwartz, V. Deseau, and N. Rosen. 1987. Activation of pp60c-src protein kinase activity in human colon carcinoma. Proc. Natl. Acad. Sci. USA 84:2251–2255.
  • Budd, R. C., M. Schreyer, G. C. Miescher, and H. R. MacDonald. 1987. T cell lineages in the thymus of lpr/lpr mice: evidence for parallel pathways of normal and abnormal T cell development. J. Immunol. 139:2200–2210.
  • Cartwright, C. A., W. Eckhart, S. Simon, and P. L. Kaplan. 1987. Cell transformation by pp60c-src mutated in the carboxyterminal regulatory domain. Cell 49:83–91.
  • Casnellie, J. E., M. L. Harrison, K. E. Hellstrom, and E. G. Krebs. 1982. A lymphoma protein with an in vitro site of tyrosine phosphorylation homologous to that in pp60src. J. Biol. Chem. 257:13877–13879.
  • Casnellie, J. E., M. L. Harrison, K. E. Hellstrom, and E. G. Krebs. 1983. A lymphoma cell line expressing elevated levels of tyrosine protein kinase activity. J. Biol. Chem. 258:10738–10742.
  • Casnellie, J. E., and R. J. Lamberts. 1986. Tumor promoters cause changes in the state of phosphorylation and apparent molecular weight of a tyrosine protein kinase in T lymphocytes. J. Biol. Chem. 261:4921–4925.
  • Ceredig, R., D. P. Dialynas, F. W. Fitch, and H. R. MacDonald. 1983. Precursors of T cell growth factor producing cell in the thymus: ontogeny, frequency and quantitative recovery in a subpopulation of phenotypically mature thymocytes defined by monoclonal antibody GK-1.5. J. Exp. Med. 158:1654–1671.
  • Ceredig, R., J. W. Lowenthal, M. Nabholz, and H. R. MacDonald. 1985. Expression of interleukin-2 receptors as a differentiation marker on intrathymic stem cells. Nature (London) 314:98–100.
  • Chackalaparampil, I., and D. Shalloway. 1988. Altered phosphorylation and activation of pp60c-src during fibroblast mitosis. Cell 52:801–810.
  • Cooper, J. A., K. L. Gould, C. A. Cartwright, and T. Hunter. 1986. Tyr527 is phosphorylated in pp60c-src: implications for regulation. Science 231:1431–1434.
  • Courtneidge, S. A.. 1985. Activation of the pp60c-src kinase by middle T binding or by déphosphorylation. EMBO J. 4:1471–1477.
  • Croghan, T. W., J. Evans, J.-L. Davignon, J. P. Allison, R. A. Eisenberg, J. A. Frelinger, and P. L. Cohen. 1989. Diminished expression of the T cell receptor on the expanded lymphocyte population in MRL/Mp-lpr/lpr mice. Autoimmunity 2:97–111.
  • Davignon, J. L., P. L. Cohen, and R. A. Eisenberg. 1988. Rapid T cell receptor modulation accompanies lack of in vitro mitogenic responsiveness of double negative T cells to anti-CD3 monoclonal antibody in MRL/Mp-lpr/lpr mice. J. Immunol. 141:1848–1854.
  • Earp, H. S., K. S. Austin, S. C. Buessow, R. Dy, and G. Y. Gillespie. 1984. Membranes from T and B lymphocytes have different patterns of tyrosine phosphorylation. Proc. Natl. Acad. Sci. USA 81:2347–2351.
  • Earp, H. S., K. S. Austin, G. Y. Gillespie, S. C. Buessow, A. A. Davies, and P. J. Parker. 1985. Characterization of distinct tyrosine-specific protein kinases in B and T lymphocytes. J. Biol. Chem. 260:4351–4356.
  • Evans, J. L., W. J. Boyle, and J. P.-Y. Ting. 1987. Molecular basis of elevated c-myb expression in the abnormal L3T4-, Lyt-2- T lymphocytes of autoimmune mice. J. Immunol. 139:3497–3505.
  • Fowlkes, B. J., L. Edison, B. Mathieson, and T. M. Chused. 1985. Early T lymphocytes: differentiation in vivo of adult intrathymic precursor cells. J. Exp. Med. 162:802–822.
  • Golden, A., S. P. Nemeth, and J. S. Brugge. 1986. Blood platelets express high levels of the pp60c-src-specific tyrosine kinase activity. Biochemistry 83:852–856.
  • Gould, K. L., J. R. Woodgett, J. A. Cooper, J. E. Buss, D. Shalloway, and T. Hunter. 1985. Protein kinase C phosphorylates pp60src at a novel site. Cell 42:849–857.
  • Harrison, M. L., P. S. Low, and R. L. Geahlen. 1984. T and B lymphocytes express distinct tyrosine protein kinases. J. Biol. Chem. 259:9348–9350.
  • Hunter, T., and J. A. Cooper. 1985. Protein-tyrosine kinases. Annu. Rev. Biochem. 54:897–930.
  • Izui, S., V. E. Kelley, K. Masuda, H. Yoshida, J. B. Roths, and E. D. Murphy. 1984. Induction of various autoantibodies by mutant gene lpr in several strains of mice. J. Immunol. 133:227–233.
  • Jove, R., and H. Hanafusa. 1987. Cell transformation by the viral src oncogene. Annu. Rev. Cell Biol. 3:31–56.
  • Jove, R., S. Kornbluth, and H. Hanafusa. 1987. Enzymatically inactive p60c-src mutant with altered ATP-binding site is fully phosphorylated in its carboxy-terminal regulatory region. Cell 50:937–943.
  • Katagiri, K., T. Katagiri, R. A. Eisenberg, J. Ting, and P. L. Cohen. 1987. Interleukin 2 responses of lpr and normal L3T4- /Lyt2- T cells induced by TPA plus A23187. J. Immunol. 138:149–156.
  • Katagiri, T., P. L. Cohen, and R. A. Eisenberg. 1988. The lpr gene causes an intrinsic T cell abnormality that is required for hyperproliferation. J. Exp. Med. 167:741–751.
  • Kato, J. Y., T. Takeya, C. Grandori, H. Iba, J. B. Levy, and H. Hanafusa. 1986. Amino acid substitutions sufficient to convert the nontransforming p60c-src protein to a transforming protein. Mol. Cell. Biol. 6:4155–4160.
  • Kawakami, T., C. Y. Pennington, and K. C. Robbins. 1986. Isolation and oncogenic potential of a novel human src-like gene. Mol. Cell. Biol. 6:4195–4201.
  • Kmiecik, T. F., and D. Shalloway. 1987. Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation. Cell 49:65–73.
  • Levy, J. B., H. Iba, and H. Hanafusa. 1986. Activation of the transforming potential of p60c-src by a single amino acid change. Proc. Natl. Acad. Sci. USA 83:4228–4232.
  • Lipsich, L. A., A. J. Lewis, and J. S. Brugge. 1983. Isolation of monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses. J. Virol. 48:352–360.
  • Marth, J. D., J. A. Cooper, C. S. King, S. F. Ziegler, D. A. Tinker, R. W. Overall, E. G. Krebs, and R. M. Perlmutter. 1988. Neoplastic transformation induced by an activated lymphocytespecific protein tyrosine kinase (pp56lck). Mol. Cell. Biol. 8:540–550.
  • Marth, J. D., R. Peet, E. G. Krebs, and R. M. Perlmutter. 1985. A lymphocyte-specific protein tyrosine kinase gene is rearranged and overexpressed in the murine T cell lymphoma LSTRA. Cell 43:393–404.
  • Martinez, R., B. Mathey-Prevot, A. Bernards, and D. Baltimore. 1987. Neuronal pp60c-src contains a six-amino acid insertion relative to its non-neuronal counterpart. Science 237:411–415.
  • Menko, S., and D. Boettiger. 1988. Inhibition of chicken embryo lens differentiation and lens junction formation in culture by pp60v-src. Mol. Cell. Biol. 8:1414–1420.
  • Moria, A. O., J. Schreurs, A. Miyajima, and J. Y. J. Wang. 1988. Hematopoietic growth factors activate the tyrosine phosphorylation of distinct sets of proteins in interleukin-3-dependent murine cell lines. Mol. Cell Biol. 8:2214–2218.
  • Morse, H. C., III, W. F. Davidson, R. A. Yetter, E. D. Murphy, J. B. Roths, and R. L. Coffman. 1982. Abnormalities induced by the mutant gene lpr: expansion of a unique lymphocyte subset. J. Immunol. 129:2612–2615.
  • Mountz, J. D., A. D. Steinberg, D. M. Klinman, and H. R. Smith. 1984. Autoimmunity and increased c-myb transcription. Science 226:1087–1089.
  • Nemazee, D. A., S. Studer, M. Steinmetz, Z. Dembic, and M. Kiefer. 1985. The lymphoproliferating cells of MRL-lpr/lpr mice are a polyclonal population that bear the T lymphocyte receptor for antigen. Eur. J. Immunol. 15:760–764.
  • O'Farrell, P. H.. 1975. High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250:4007–4021.
  • Parsons, S. J., D. J. McCarley, C. Ely, D. C. Benjamin, and J. T. Parsons. 1984. Monoclonal antibodies to Rous sarcoma virus p60src react with enzymatically active cellular pp60src of avian and mammalian origin. J. Virol. 51:272–282.
  • Piwnica-Worms, H., K. B. Saunders, T. M. Roberts, A. E. Smith, and S. H. Cheng. 1987. Tyrosine phosphorylation regulates the biochemical and biological properties of pp60c-src. Cell 49:75–82.
  • Raveche, E. S., A. D. Steinberg, A. L. DeFranco, and J.-H. Tjio. 1982. Cell cycle analysis of lymphocyte activation in normal and autoimmune strains of mice. J. Immunol. 129:1219–1226.
  • Saltzman, E. M., R. R. Thom, and J. E. Casnellie. 1988. Activation of a tyrosine protein kinase is an early event in the stimulation of T lymphocytes by interleukin-2. J. Biol. Chem. 263:6956–6959.
  • Samelson, L. E., W. F. Davidson, H. C. Morse III, and R. D. Klausner. 1986. Abnormal tyrosine phosphorylation on T-cell receptor in lymphoproliferative disorders. Nature (London) 324:674–676.
  • Samelson, L. E., M. D. Patel, A. M. Weissman, J. B. Harford, and R. D. Klausner. 1986. Antigen activation of murine T cells induces tyrosine phosphorylation of a polypeptide associated with the T cell antigen receptor. Cell 46:1083–1090.
  • Sarmiento, M., A. L. Glasebrook, and F. W. Fitch. 1980. IgG or IgM monoclonal antibodies reactive with different determinants on the molecular complex bearing Lyt-2 antigen block T cell- mediated cytolysis in the absence of complement. J. Immunol. 125:2665–2672.
  • Schuh, S., and J. S. Brugge. 1988. Investigation of factors that influence phosphorylation of pp60c-src on tyrosine 527. Mol. Cell. Biol. 8:2465–2471.
  • Semba, K., M. Nishizawa, N. Miyajima, M. C. Yoshida, J. Sukegawa, Y. Yamanishi, M. Sasaki, T. Yamamoto, and K. Toyoshima. 1986. yes-related protooncogene, syn, belongs to the protein-tyrosine kinase family. Proc. Natl. Acad. Sci. USA 83:5459–5463.
  • Veillette, A., M. A. Bookman, E. M. Horak, and J. B. Bolen. 1988. The CD4 and CD8 T cell surface antigens are associated with the internal membrane tyrosine-protein kinase p56lck Cell 55:301–308.
  • Veillette, A., I. D. Horak, and J. B. Bolen. 1988. Post-translational alterations of the tyrosine kinase p56lck in response to activators of protein kinase C. Oncogene Res. 2:1–17.
  • Vorona, A. F., and B. M. Sefton. 1986. Expression of a new tyrosine protein kinase is stimulated by retrovirus promoter insertion. Nature (London) 319:682–685.
  • Willman, C. L., C. C. Stewart, J. K. Griffith, S. J. Stewart, and T. B. Tomasi. 1987. Differential expression and regulation of the c-src and c-fgr protooncogenes in myelomonocytic cells. Proc. Natl. Acad. Sci. USA 84:4480–4484.
  • Wofsy, D., R. R. Hardy, and W. E. Seaman. 1984. The proliferating cells in autoimmune MRL/lpr mice lack L3T4, an antigen on helper T cells that is involved in the response to class II major histocompatibility antigens. J. Immunol. 132:2686–2689.
  • Yarden, Y., and A. Ullrich. 1988. Growth factor receptor tyrosine kinases. Annu. Rev. Biochem. 57:443–478.
  • Yokota, S., D. Yuan, T. Katagiri, R. A. Eisenberg, P. Cohen, and J. P.-Y. Ting. 1987. The expression and regulation of c-myb transcription in B6/lpr Lyt-2-, L3T4- T lymphocytes. J. Immunol. 139:2810–2817.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.