Interactions of the Scid or Beige Mutations with the Viable Motheaten Mutation

References

• Shultz L. D., Coman D. R., Bailey C. L., Beamer Sidman W. G.C.L. “Viable motheaten”, a new allele at the motheaten locus. I. Pathology. Am. J. Pathology 1984; 116: 179–192
   PubMed Web of Science ®Google Scholar
• Shultz L. D. Pleiotropic effects of deleterious alleles at the “motheaten” locus. Cur. Top. Microbiol. Immunol. 1988; 137: 216–222
   PubMed Web of Science ®Google Scholar
• Rossi G. A., Hunninghake G. W., Kawanami O., Ferrans V. J., Hansen C. T. and Crystal R.G. Motheaten mice: an animal model with an inherited form of interstitial lung disease. Am. Rev. Respir. Dis. 1985; 131: 150–158
   PubMed Web of Science ®Google Scholar
• Sidman C. L., Shultz L. D., Hardy R. R., Hayakawa K., Herzenberg L. A. Production of Immunoglobulin isotypes by Ly-1+ B cells in viable motheaten and normal mice. Science 1986; 232: 1423–1425
   PubMed Web of Science ®Google Scholar
• Kuntz L., Fonteneau P., Loor F. Common and individual features of the humoral immunity dysregulation of mice homozygous at the viable motheaten (mev) mutation. Immunology Letters 1990; 24: 97–102
   PubMed Web of Science ®Google Scholar
• Tsui H. W., Siminovitch K. A., Souza L. D., Tsui F. W.L. Motheaten and viable motheaten mice have mutations in the haemopoietic cell phosphatase gene. Nature Genetics 1993; 4: 124–129
   PubMed Web of Science ®Google Scholar
• Kozlowski M., Mlinaric-Rascan I., Feng G.-S., Shen R., Pawson T., Siminovitch K. A. Expression and catalytic activity of the tyrosine phosphatase PTP1C is severely impaired in motheaten and viable motheaten mice. J. Exp. Med. 1993; 178: 2157–2163
   PubMed Web of Science ®Google Scholar
• Shultz L. D., Schweitzer P. A., Rajan T. V., Yi T., Ihle J. N., Matthews R. J., Thomas M. L., Beier D. R. Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine-phosphatase (Hcph) gene. Cell 1993; 73: 1445–1454
   PubMed Web of Science ®Google Scholar
• Yi T., Cleveland J. L., Ihle J. N. Identification of novel protein tyrosine phosphatases of hematopoietic cells by polymerase chain reaction amplification. Blood 1991; 78: 2222–2228
   PubMed Web of Science ®Google Scholar
• Yi T., Cleveland J. L., Ihle J. N. Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p 12–13. Mol. Cell. Biol. 1992; 12: 836–846
   PubMedGoogle Scholar
• Plutzky J., Neel B. G., Rosenberg R. D. Isolation of a src homology 2-containing tyrosine phosphatase. Proc. Natl Acad. Sci USA 1992; 89: 1123–1127
   PubMedGoogle Scholar
• Matthews R. J., Bowne D. B., Flores E., Thomas M. L. Characterization of hematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences. Mol. Cell. Biol. 1992; 12: 2396–2405
   PubMed Web of Science ®Google Scholar
• Shultz L. D. Hematopoiesis and models of immunodeficiency. Sem. Immunol. 1991; 3: 397–408
   PubMedGoogle Scholar
• Kuntz L., Velin D., Pflumio F., Loor F. Adoptive transfer of viable motheaten humoral autoimmunity in cyclophosphamide-immunodepressed beige recipient mice. Immunology 1990; 70: 520–526
   PubMed Web of Science ®Google Scholar
• Kuntz L., Pflumio F., Velin D., Loor F. Adoptive transfer of viable motheaten (mev) humoral autoimmunity: IgM to IgG switch of the hyperglobunemia in nude, beige mouse recipients. Immunology 1990; 71: 341–346
   PubMed Web of Science ®Google Scholar
• Kuntz L., Montecino-Rodriguez E., Jachez B., Roman D., Loor F. Adoptive transfer of viable motheaten pathology in sublethally irradiated beige recipient mice. Immunology 1991; 73: 356–362
   PubMedGoogle Scholar
• Bosma M. J., Carroll A. M. The scid mouse mutant. Annu. Rev. Immunol. 1991; 9: 323–350
   PubMed Web of Science ®Google Scholar
• Hoskin D. H., Anderson S. K., Stankova J., Haliotis T., Roder J. C. Immunological and nonimmunological consequences of the beige mutation. In Immunological disorders in mice, B. Rihova, V. Vetvicka. CRC Press, Boston 1991; 251–263
   Google Scholar
• Takeuchi K. H., Swanks R. T. Inhibitors of elastase and cathepsine G in Chédiak-Higashi (beige) neutrophils. J. Biol. Chem. 1989; 264: 7431–7436
   PubMed Web of Science ®Google Scholar
• Schrijver G., Schalkwijk J., Robben J. C.M., Assmann K. J.M., Koene R. A.P. Antiglomerular basement membrane nephritis in beige mice. J. Exp. Med. 1989; 169: 1435–1448
   PubMed Web of Science ®Google Scholar
• Starcher B., Williams I. The beige mouse: role of neutrophil elastase in the development of pulmonary emphysema. Exp. Lung. Res. 1989; 15: 785–800
   PubMed Web of Science ®Google Scholar
• Froidevaux S., Loor F. A quick procedure for identifying doubly homozygous immunodeficient scidbeige mice. J. Immunol. Methods 1991; 137: 275–279
   PubMedGoogle Scholar
• Jachez B., Montecino-Rodriguez E.-M., Fonteneau P., Loor F. Partial expression of the Ipr locus in the heterozygous state: presence of autoantibodies. 1988; 64: 31–40
   Google Scholar
• Klein-Schneegans A-S., Gavéiaux C., Fonteneaus P., Loor F. Indirect double sandwich ELISA for the specific and quantitative measurement of mouse IgM, IgA and IgG subclasses. J. Immunol. Methods 1989; 119: 117–125
   PubMed Web of Science ®Google Scholar
• Klein-Schneegans A. S., Kuntz L., Fonteneaus P., Loor F. An indirect asymetrical sandwich ELISA using anti-allotype antibodies for the specific and quantitative measurement of the mouse IgG2a of the Igh-1b allotype. J. Immunol. Methods 1989; 125: 207–213
   PubMed Web of Science ®Google Scholar
• Froidevaux S., Kuntz L., Velin D., Loor F. Different nature of the proliferation defects of gld, Ipr and mev C57BL/6 mouse lymphoid cell. Autoimmunity 1991; 10: 233–240
   PubMed Web of Science ®Google Scholar
• Roman D. Ph.D. thesis, University of Strasbourg, France 1994
   Google Scholar
• Hayes S. M., Shutlz L. D., Greiner D. L. Thymic involution in viable motheaten (mev) mice is associated with a loss of intrathymic precursor activity. Dev. Immunol. 1992; 2: 191–205
   Google Scholar
• Shen S.-H., Bastein L., Posner B. I., Chretien P. A protein-tyrosine phosphatase with sequence similarity to the SH2 domain of the protein-tyrosine kinases. Nature 1991; 352: 736–739
   PubMedGoogle Scholar
• Shultz L. D., Sidman C. L. Genetically determined murine models of immunodeficiency. Annu. Rev. Immunol. 1987; 5: 367–403
   PubMed Web of Science ®Google Scholar
• Scribner C. L., Hansen C. T., Klinman D. M., Steinberg A. D. The interaction of the xid and me genes. J. Immunol. 1987; 138: 3611–3617
   PubMed Web of Science ®Google Scholar
• Koo G. C., Rosen H., Sirotina A., Ma X.-D., Shult L. D. Anti-CD11b antibody prevents immunopathologic changes in viable moth-eaten bone marrow chimeric mice. J. Immunol. 1993; 151: 6733–6741
   Google Scholar
• Lorenz U., Ravichandran K. S., Pei D., Walsh C. T., Burakoff S. J., Neel B. G. Lck-dependent tyrosyl phosphorylation of the phosphotyrosine phosphatase SH-PTP1 in murine T cells. Mol. Cell. Biol. 1994; 14: 1824–1834
   PubMedGoogle Scholar
• Shultz L. D., Coman D. R., Lyons B. L., Sidman C. L., Taylor S. Development of plasmacytoid cells with Russel bodies in autoimmune “viable motheaten” mice. Am. J. Pathol. 1987; 127: 38–50
   PubMed Web of Science ®Google Scholar
• Cyster J. G., Goodnow C. C. Protein Tyrosine phosphatase 1C negatively regulates antigen receptor signaling in B lymphocytes and determines thresholds for negative selection. Immunity 1995; 2: 13–24
   PubMed Web of Science ®Google Scholar