Recombinant Human Mullerian Inhibiting Substance Inhibits Epidermal Growth Factor Receptor Tyrosine Kinase

References

• Bertics P. J., Weber W., Cochet C., Gill G. N. Regulation of the epidermal growth factor receptor by phosphorylation. J. Cell. Biochem. 1985; 29: 195–208
   PubMedGoogle Scholar
• Blanchard M. G., Josso N. Source of Anti-Mullerian hormone synthesized by the fetal testis: Mullerian inhibiting activity of fetal bovine sertoli cells in tissue culture. Pediatr. Res. 1974; 8: 968–971
   Google Scholar
• Budzik G. P., Powell S. M., Kamagata S., Donahoe P. K. Mullerian inhibiting substance fractionation by dye affinity chromatography. Cell 1983; 34: 307–314
   Google Scholar
• Budzik G. P., Donahoe P. K., Hutson J. M. A possible purification of Mullerian inhibiting substance and a model for its mechanism of action. Developmental Mechanisms: Normal and Abnormal, J. W. Lash, J. Saxen. Liss, New York 1985; 207–223
   Google Scholar
• Carpenter G., King L., Jr, Cohen S. Epidermal growth factor stimulates phosphorylation in membrane preparations in vitro. Nature 1978; 276: 409–410
   PubMed Web of Science ®Google Scholar
• Carpenter G., King L., Jr, Cohen S. Rapid enhancement of protein phosphorylation in A-431 cell membrane preparatins by epidermal growth factor. J. Biol. Chem. 1979; 254: 4884–4891
   PubMed Web of Science ®Google Scholar
• Cassel D., Glasser L. Proteolytic cleavage of epidermal growth factor receptor. A Ca2+-dependent, sulfhydryl-sensitive proteolytic system in A-431 cells. J. Biol. Chem. 1982; 257: 9845–9848
   Google Scholar
• Cate R. L., Mattaliano R. J., Hession C., Tizard R., Farber N. M., Cheung A., Ninfa E. G., Frey A. Z., Gash D. J., Chow E. P., Fisher R. A., Bertonis J. M., Torres G., Wallner B. P., Ramachandran K. L., Ragin R. C., Manganaro T. F., MacLaughlin D. T., Donahoe P. K. Isolation of the bovine and human genes for Mullerian inhibiting substance and expression of the human gene in animal cells. Cell 1986; 45: 685–698
   PubMed Web of Science ®Google Scholar
• Cate R. L., Ninfa E. G., Pratt D., MacLaughlin D. T., Donahoe P. K. Development of Mullerian inhibiting substance as an anti-cancer drug. Cold Spring Harbor Symp. Quant. Biol. 1987; 51: 641–647
   Google Scholar
• Cooper J. A., Sefton B. M., Hunter T. Detection and quantification of phosphotyrosine in proteins. Methods Enzymol. 1983; 99: 387–402
   PubMed Web of Science ®Google Scholar
• Coughlin J. P., Donahoe P. K., Budzik G. P., MacLaughlin D. T. Mullerian inhibiting substance blocks autophos-phorylation of the EGF receptor by inhibiting tyrosine kinase. Mol. Cell. Endocrinol. 1987; 49: 75–86
   PubMed Web of Science ®Google Scholar
• Dandliker W. B., Alonso R., de Saussure V. A., Kierszenbaum F., Levison S. A., Schapiro H. C. The effect of chaotropic ions on the dissociation of antigen-antibody complexes. Biochemistry 1967; 6: 1460–1467
   PubMed Web of Science ®Google Scholar
• Di Fiore P. P., Pierce J. H., Kraus M. H., Segatto O., King C. R., Aaronson S. A. erbB-2 is a potent oncogene when overexpressed in N1H-3T3 cells. Science 1987; 237: 178–182
   PubMed Web of Science ®Google Scholar
• Donahoe P. K., Ito Y., Hendren W. H. A graded organ culture assay for the detection of Mullerian inhibiting substance. J. Surg. Res 1977a; 23: 141–148
   Google Scholar
• Donahoe P. K., Ito Y., Morikawa Y., Hendren W. H. Mullerian inhibiting substance in human testes after birth. J. Pediatr. Surg. 1977b; 12: 323–330
   Google Scholar
• Donahoe P. K., Ito Y., Price J. M., Hendren W. H. Mullerian inhibiting substance activity in bovine fetal, newborn and prepubertal testes. Biol. Reprod. 1977c; 16: 238–243
   Google Scholar
• Donahoe P. K., Cate R. L., MacLaughlin D. T., Epstein J., Fuller A. F., Takahashi M., Coughlin J. P., Ninfa E. G., Taylor L. Mullerian inhibiting substance: Gene structure and mechanism of action of a fetal regressor. Recent Prog. Horm. Res. 1987; 43: 431–467
   Google Scholar
• Hutson J. M., Fallat M. E., Kamagata S., Donahoe P. K., Budzik G. P. Phosphorylation events during Mullerian duct regression. Science 1984; 223: 586–1589
   PubMed Web of Science ®Google Scholar
• Kasuga M., White M. F., Kahn C. R. Phosphorylation of the insulin receptor in cultured hepatoma cells and a solubilized system. Methods Enzymol. 1985; 109: 609–621
   PubMedGoogle Scholar
• King C. S., Cooper J. A. Effects of protein kinase C activation after epidermal growth factor binding on epidermal growth factor receptor phosphorylation. J. Biol. Chem. 1986; 261: 10073–10078
   PubMedGoogle Scholar
• Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685
   PubMed Web of Science ®Google Scholar
• Lowry O. H., Rosebrougth N. J., Farr A. L., Randall R. J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 1951; 193: 765–775
   Google Scholar
• Pang D. T., Sharma B. R., Shafer J. A., White M. F., Kahn C. R. Predominance of tyrosine phosphorylation of insulin receptors during the initial response of intact cells to insulin. J. Biol. Chem. 1985; 260: 7131–7136
   PubMedGoogle Scholar
• Pepinsky R. B., Sinclair L. K., Chow E. P., Mattaliano R. J., Manganaro T. F., Donahoe P. K., Cate R. L. Proteolytic Processing of Mullerian. Inhibiting Substance Produces a Transforming Growth Factor-β-like Fragment. J. Biol. Chem. 1988; 263: 18961–18964
   PubMed Web of Science ®Google Scholar
• Picard J., Josso N. Purification of testicular anti-Mullerian hormone allowing direct visualization of the pure glycoprotein and determination of yield and purification factor. Mol. Cell. Endocrinol. 1984; 34: 23–29
   Google Scholar
• Picon R. Action due testicule foetal sur le development in vitro des canaux de Muller chez le rat. Arch. Anat. Microsc. Morphol. Exp. 1969; 58: 1–19
   Google Scholar
• Shima H., Donahoe P. K., Budzik G. P., Kamagata D., Hudson P., Mudgett-Hunter M. Production of monoclonal antibodies for affinity purification of bovine Mullerian inhibiting substance activity. Hybridoma 1984; 3: 210–214
   Google Scholar
• Takahashi M., Hayashi M., Manganaro T. F., Donahoe P. K. The ontogeny of Mullerian inhibiting substance in granulosa cells of the bovine ovarian follicle. Biol. Reprod. 1986a; 35: 447–453
   Google Scholar
• Takahashi M., Koide S. S., Donahoe P. K. Mullerian inhibiting substance as oocyte meiosis inhibitor. Mol. Cell. Endocrinol. 1986b; 47: 225–234
   Google Scholar
• Thom D., Powell A. J., Lloyd C. W., Rees D. A. Rapid isolation of plasma membranes in high yield from cultured fibroblasts. Biochem 1977; 168: 187–194
   Google Scholar
• Towbin H., Staehelin T., Gorden J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA 1979; 76: 4350–4354
   PubMed Web of Science ®Google Scholar
• Tsafriri A., Picard J. Y., Josso N. Immunopurified anti-Mullerian hormone does not inhibit spontaneous resumption of meiosis in vitro of rat oocytes. Biol. Reprod. 1988; 38: 481–485
   Google Scholar
• Ueno S., Manganaro T., Donahoe P. K. Human recombinant Mullerian inhibiting substance inhibition of rat oocyte meiosis is reversed by epidermal growth in vitro. Endocrinology 1988; 123: 1652–1659
   PubMed Web of Science ®Google Scholar