MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains

Journal of Cell Biology

Volumn 132, Issue 4, 1996, Pages 717-726

  Weskamp, Gisela ^a   Krätzschmar, Jörn ^a,b   Reid, Martha S ^a   Blobel, Carl P ^a  

^a MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

^b BAYER PHARMA AG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DISINTEGRIN; GLYCOPROTEIN; LIGAND; METALLOPROTEINASE; SNAKE VENOM;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CELL MEMBRANE; CERCOPITHECIDAE; CYTOPLASM; IMMUNOBLOTTING; IMMUNOFLUORESCENCE; MOUSE; NONHUMAN; NORTHERN BLOTTING; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN LOCALIZATION;

3T3 CELLS; ADAM PROTEINS; AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CLONING, MOLECULAR; DISINTEGRINS; DNA, COMPLEMENTARY; HUMANS; MEMBRANE PROTEINS; METALLOENDOPEPTIDASES; MICE; MOLECULAR SEQUENCE DATA; PEPTIDES; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SRC HOMOLOGY DOMAINS;

ANIMALIA; CERCOPITHECIDAE; SERPENTES;

EID: 0030049705     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.132.4.717     Document Type: Article

References (49)

1. Albelda, S.M., and C.A. Buck 1990. Integrins and other cell adhesion molecules. FASEB. (Fed Am. Soc. Exp Biochem.) 4:2868-2880
2. Alexandropoulos, K., G. Cheng, and D Baltimore. 1995. Proline-rich sequences that bind to Src homology 3 domains with individual specificities. Proc Natl Acad. Sci. USA 92:3110-3114
3. Almeida, E.A. C., A.-P.J. Huovila, A E Sutherland, L.E. Stephens, P G. Calarco, L.M. Shaw, A.M Mercurio, A. Sonnenberg, P. Primakoff, D G. Myles, et al. 1995. Mouse egg integrin α6β1 functions as a sperm receptor. Cell. 81:1095-1104.
4. Barker, H.L., A.C.F Perry, R Jones, and L. Hall. 1994. Sequence and expression of a monkey testicular transcript encoding tMDC I, a novel member of the metalloprotease-like, disintegrin-like, cysteine-rich (MDC) protein family. Biochem. Biophys. Acta 1218:429-431.
5. Birkedal-Hansen, H. 1995. Proteolytic remodeling of extracellular matrix. Curr. Opin. Cell Biol. 7:728-735.
6. Blobel, C P., and J.M. White. 1992 Structure, function and evolutionary relationship of proteins containing a disintegrin domain Curr. Opin. Cell Biol. 4 760-765.
7. Blobel, C.P., D G. Myles, P. Primakoff, and J.W White. 1990. Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilization competence. J Cell Biol 111:69-78.
8. Blobel, C.P., T G. Wolfsberg, C.W. Turck, D.G. Myles, P. Primakoff, and J.M. White. 1992. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature (Lond.). 356:248-252.
9. Chomczynski, P , and N. Sacchi. 1987 Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-cholroform extraction. Anal. Biochem. 162:156-159.
10. Creemer, J.W M., R.J. Siezen, A.J.M Roebroek, T.A Y. Ayoubi, D. Huylebroeck, and W.J.M. Van de Ven 1993 Modulation of furin-mediated proprotein processing activity by site directed mutagenesis. J. Biol. Chem. 268:21826-21834.
11. Emi, M., T. Katagiri, Y. Harada, H Saito, J. Inazawa, I. Ito, F. Kasumi, and Y Nakamura. 1993. A novel metalloprotease/disintegrin-like gene at 17q21.3 is somatically rearranged in two primary breast cancers. Nature Genet 5 151-157.
12. Feng, S , J.K Chen, H. Yu, J. Simon, and S. Schreiber. 1994. Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions. Science (Wash. DC). 266:1241-1247.
13. Fuller, R.S , A.J. Brake, and J. Thorner. 1989. Intracellular targeting and structural conservation of a prohormone processing protease. Science (Wash. DC.) 246:482-486.
14. Gould, R.J M.A. Polokoff, P.A. Friedman, T.F. Huang, J.C. Holt, J.J. Cook, and S. Niewiarowski. 1990. Disintegrins: a family of integrin inhibitory proteins from viper venoms. Proc. Soc Exp. Biol Med 195 168-171.
15. Harlow, E , and D Lane 1988. Antibodies, a Laboratory Manual. Cold Spring Harbor Laboratories, Cold Spring Harbor NY. pp. 53-138.
16. Heinlein, U.A.O., S. Wallat, A. Senftleben, and L. Lemaire. 1994. Male germ cell-expressed mouse gene TAZ83 encodes a putative, cysteine rich transmembrane protein (cyritestin) sharing homologies with snake venom toxins and sperm egg fusion proteins. Dev. Growth Diff. 36:49-58.
17. Huang, T.F., J.C. Holt, E.P. Kirby, and S. Niewiarowski. 1989. Trigramin: primary structure and its inhibition of von Willebrand factor binding to glycoprotein IIb/IIIa complex on human platelets. Biochemistry. 28:661-666.
18. Huang, T.F., J.C. Holt, H. Lukasiewicz, and S. Niewiarowski. 1987. Trigramin: a low molecular weight peptide inhibiting fibrinogen interaction with glycoprotein IIb-IIIa complex receptors expressed on platelets. J. Biol Chem. 262:16157-16163.
19. Hynes, R.O. 1987. Integrins: a family of cell surface receptors. Cell. 48:549-554.
20. Hynes, R.O. 1992. Integrins: versatility, modulation, and signaling in cell adhesion. Cell. 69:11-25.
21. Katagiri, T., Y. Harada, M. Emi, and Y. Nakamura. 1995. Human metalloprotease/disintegrin-like (MDC) gene: exon-intron organization and alternative splicing. Cytogenet. Cell Genet. 68:39-44
22. Kemble, G.W., D.L. Bodian, J. Rose, I.A. Wilson, and J.M. White. 1992. Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin. J. Virol. 66:4940-4950.
23. Kini, R.M., and H J. Evans. 1992. Structural domains in venom proteins: evidence that metalloproteinases and nonenzymatic platelet aggregation inhibitors (disintegrins) from snake venoms are derived by proteolysis from a common precursor. Toxicon. 30:1-29.
24. Krätzschmar, J., B. Haendler, G. Langer, W. Boidol, P. Bringmann, A. Alagon, P. Donner, and W.D. Schleuning. 1991. The plasminogen activator family from the salivary gland of the vampire bat Desmodus rotundus: cloning and expression. Gene (Amst.). 105:229-237.
25. Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.). 227:680-685.
26. Lim, W.A., F.M. Richards, and R. Fox. 1994. Structural determinants of peptide binding orientation and of sequence specificity in SH3 domains. Nature (Lond.). 372:375-379.
27. Mayer, B J., and M.J. Eck. 1995 Minding your p's and q's. Curr Biol. 4: 364-367.
28. Musial, J., S Niewiarowski, B. Rucinski, G J. Stewart, J.J. Cook, J.A. Williams, and L H. Edmunds. 1990. Inhibition of platelet adhesion to surfaces of extracorporeal circuits by disintegrins. Circulation. 82:261-273.
29. Myles, D.G., L.H. Kimmel, C P. Blobel, J.M White, and P. Primakoff. 1994. Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion. Proc. Natl Acad. Sci. USA. 91.4195-4198.
30. Pawson, T. 1995. Protein modules and signalling networks. Nature (Lond.). 373:573-580.
31. Pei, D., and S.J. Weiss. 1995. Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature (Lond.). 375:244-247.
32. Perry, A.C.F., H.L. Barker, R. Jones, and L. Hall. 1994. Genetic evidence for an additional member of the metalloproteinase-like, cysteine rich (MDC) family of mammalian proteins and its abundant expression in the testis. Biochem. Biophys. Acta. 1207:134-137.
33. Perry, A.C.F., P.M. Gichuhi, R. Jones, and L. Hall. 1995. Cloning and analysis of monkey fertilin reveals novel a subunit isoforms. Biochem. J 307: 843-850.
34. Perry, A.C.F., R. Jones, P.J. Barker, and L. Hall. 1992. A mammalian epididymal protein with remarkable sequence similarity to snake venom haemorrhagic peptides. Biochem. J. 286:671-675.
35. Primakoff, P., H. Hyatt, and J. Tredick-Kline. 1987. Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion. J. Cell Biol. 104:141-149.
36. Ruoslahti, E. 1991. Integrins. J. Clin Invest 87(1) 1-5.
37. Scarborough, R.M., J.W. Rose, MA. Naughton, D.R. Phillips, L. Nannizzi, A. Arfsten, A.M. Campbell, and I.F. Charo. 1993. Characterization of the integrin specificities of disintegrins isolated from American Pit Viper Venoms. J. Biol. Chem. 268.1058-1065.
38. Sparks, A B., L.A. Quilliam, J.M. Thorn, C.J. Der, and B.K. Kay. 1994. Identification and characterization of Src SH3 ligands from phage displayed random peptide libraries. J. Biol. Chem. 269:23853-23856.
39. von Heijne, G 1986. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14:4683-4690.
40. Watanabe, T., T Nakagawa, J. Ikemizu, M. Nagahama, K. Murakami, and K. Nakayama. 1992. Sequence requirements for precursor cleavage within the constitutive secretory pathway. J. Biol. Chem. 267:8270-8274.
41. Weskamp, G., and C.P Blobel. 1994. A family of cellular proteins related to snake venom disintegrins. Proc. Natl. Acad. Sci. USA. 91:2748-2751.
42. Weskamp, G., and L.F. Reichardt. 1991. Evidence that biological activity of NGF is mediated through a novel subclass of high affinity receptors Neuron. 6:649-663.
43. White, J.M. 1992. Membrane fusion. Science (Wash. DC). 258:917-924.
44. Wolfsberg, T.G , J.F. Bazan, C.P. Blobel, D.G. Myles, P. Primakoff, and J M. White. 1993. The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: structural, functional and evolutionary implications. Proc. Natl. Acad. Sci. USA. 90: 10783-10787.
45. Wolfsberg, T.G., P. Primakoff, D.G Myles, and J.M. White. 1995 ADAM, a novel family of membrane proteins containing a disintegrin and metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions. J. Cell Biol. 131:1-4.
46. Wolfsberg, T.G., P.D. Straight, R.L. Gerena, A.-P J. Huovila, P. Primakoff, D.G. Myles, and J.M. White. 1995. ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin domain and a metalloprotease domain. Dev. Biol. 169.378-383.
47. Yaffe, D., and O. Saxel. 1977. Serial passaging and differentiation of myogenic cells isolated from dystrophic mouse muscle. Nature (Lond.) 270: 725-727.
48. Yagami-Hiromasa, T., T. Sato, T. Kurisaki, K. Kamijo, Y. Nabeshima, and A. Fujisawa-Sehara. 1995. A metalloprotease-disintegrin participating in myoblast fusion. Nature (Lond.). 377:652-656.
49. Yoshida, S., M Setoguchi, Y Higuchi, S. Akizuki, and S. Yamamoto. 1990. Molecular cloning of cDNA encoding MS2 antigen, a novel cell surface antigen strongly expressed in murine monocytic lineage. Int Immunot. 2: 586-591.