The cysteine-rich domain regulates ADAM protease function in vivo

Journal of Cell Biology

Volumn 159, Issue 5, 2002, Pages 893-902

  Smith, Katherine M ^a   Gaultier, Alban ^a,b   Cousin, Helene ^a   Alfandari, Dominique ^a   White, Judith M ^a   DeSimone, Douglas W ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

^b SORBONNE UNIVERSITÉ   (France)

Author keywords

ADAM; Cysteine rich; Disintegrin; Metalloprotease; Xenopus

Indexed keywords

ADAM 13 METALLOPROTEASE; ADAM PROTEASE; CYSTEINE; DISINTEGRIN; METALLOPROTEINASE; PROTEINASE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CELL SURFACE; CONTROLLED STUDY; EMBRYO; ENZYME ACTIVITY; ENZYME REGULATION; ENZYME SPECIFICITY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; XENOPUS LAEVIS;

ADAM PROTEINS; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CELL MEMBRANE; CHIMERA; CYSTEINE; DISINTEGRINS; EMBRYO, NONMAMMALIAN; EXOCRINE GLANDS; EXTRACELLULAR MATRIX; GENE EXPRESSION REGULATION, DEVELOPMENTAL; GENE EXPRESSION REGULATION, ENZYMOLOGIC; HYPERPLASIA; MEMBRANE GLYCOPROTEINS; MEMBRANE PROTEINS; METALLOENDOPEPTIDASES; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NEURAL CREST; PROTEIN STRUCTURE, TERTIARY; RNA, MESSENGER; SEQUENCE ALIGNMENT; XENOPUS LAEVIS; XENOPUS PROTEINS;

ANIMALIA; XENOPUS LAEVIS;

EID: 0037049544     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200206023     Document Type: Article

References (48)

1. Alfandari, D., C.A. Whittaker, D.W. DeSimone, and T. Darribere. 1995. Integrin αv subunit is expressed on mesodermal cell surfaces during amphibian gastrulation. Dev. Biol. 170:249-261.
2. Alfandari, D., T.G. Wolfsberg, J.M. White, and D.W. DeSimone. 1997. ADAM 13: A novel ADAM expressed in somatic mesoderm and neural crest cells during Xenopus laevis development. Dev. Biol. 182:314-330.
3. Alfandari, D., H. Cousin, A. Gaultier, K. Smith, J.M. White, T. Darribere, and D.W. DeSimone. 2001. Xenopus ADAM 13 is a metalloprotease required for cranial neural crest cell migration. Curr. Biol. 11:918-930.
4. Amour, A., C.G. Knight, A. Webster, P.M. Slocombe, P.E. Stephens, V. Knauper, A.J. Docherty, and G. Murphy. 2000. The in vitro activity of ADAM- 10 is inhibited by TIMP-1 and TIMP-3. FEBS Lett. 473:275-279.
5. Baragi, V.M., C.J. Fliszar, M.C. Conroy, Q.Z. Ye, J.M. Shipley, and H.G. Welgus. 1994. Contribution of the C-terminal domain of metalloproteinases to binding by tissue inhibitor of metalloproteinases. C-terminal truncated stromelysin and matrilysin exhibit equally compromised binding affinities as compared to full-length stromelysin. J. Biol. Chem. 269:1269-12697.
6. Bauvois, B. 2001. Transmembrane proteases in focus: Diversity and redundancy? J. Leukoc. Biol. 70:11-17.
7. Bigler, D., Y. Takahashi, M.S. Chen, E.A. Almeida, L. Osbourne, and J.M. White. 2000. Sequence-specific interaction between the disintegrin domain of mouse ADAM 2 (fertilin β) and murine eggs. Role of the α(6) integrin subunit. J. Biol. Chem. 275:11576-11584.
8. Blobel, C.P. 2000. Remarkable roles of proteolysis on and beyond the cell surface. Curr. Opin. Cell Biol. 12:606-612.
9. Bridges, L.C., P.H. Tani, K.R. Hanson, C.M. Roberts, M.B. Judkins, and R.D. Bowditch. 2002. The lymphocyte metalloprotease MDC-L (ADAM 28) is a ligand for the integrin α4β1. J. Biol. Chem. 277:3784-3792.
10. Chomczynski, P., and N. Sacchi. 1987. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156-159.
11. Cousin, H., A. Gaultier, C. Bleux, T. Darribere, and D. Alfandari. 2000. PACSIN2 is a regulator of the metalloprotease/disintegrin ADAM13. Dev. Biol. 227:197-210.
12. Dale, L., and C.M. Jones. 1999. BMP signalling in early Xenopus development. Bioessays. 21:751-760.
13. Dale, L., and F.C. Wardle. 1999. A gradient of BMP activity specifies dorsal-ventral fates in early Xenopus embryos. Semin. Cell Dev. Biol. 10:319-326.
14. De Meester, I., S. Korom, J. Van Damme, and S. Scharpe. 1999. CD26, let it cut or cut it down. Immunol. Today. 20:367-375.
15. Eto, K., C. Huet, T. Tarui, S. Kupriyanov, H.Z. Liu, W. Puzon-McLaughlin, X.P. Zhang, D. Sheppard, E. Engvall, and Y. Takada. 2002. Functional classification of ADAMs based on a conserved motif for binding to integrin α9β1: Implications for sperm-egg binding and other cell interactions. J. Biol. Chem. 277:17804-17810.
16. Evans, J.P. 2001. Fertilin β and other ADAMs as integrin ligands: Insights into cell adhesion and fertilization. Bioessays. 23:628-639.
17. Fambrough, D., D. Pan, G.M. Rubin, and C.S. Goodman. 1996. The cell surface metalloprotease/disintegrin kuzbanian is required for axonal extension in Drosophila. Proc. Natl. Acad. Sci. USA. 93:13233-13238.
18. Gammill, L.S., and H. Sive. 1997. Identification of otx2 target genes and restrictions in ectodermal competence during Xenopus cement gland formation. Development. 124:471-481.
19. Gammill, L.S., and H. Sive. 2000. Coincidence of otx2 and BMP4 signaling correlates with Xenopus cement gland formation. Mech. Dev. 92:217-226.
20. Gaultier, A., H. Cousin, T. Darribere, and D. Alfandari. 2002. ADAM13 disintegrin and cysteine-rich domains bind to the second heparin-binding domain of fibronectin. J. Biol. Chem. 277:23336-23344.
21. Harland, R.M. 1991. In situ hybridization: An improved whole-mount method for Xenopus embryos. Methods Cell Biol. 36:685-695.
22. Howard, L., K.K. Nelson, R.A. Maciewicz, and C.P. Blobel. 1999. Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1. J. Biol. Chem. 274: 31693-31699.
23. Iba, K., R. Albrechtsen, B. Gilpin, C. Frohlich, F. Loechel, A. Zolkiewska, K. Ishiguro, T. Kojima, W. Liu, J.K. Langford, et al. 2000. The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to β1 integrin-dependent cell spreading. J. Cell Biol. 149:1143-1156.
24. Ilan, N., and J.A. Madri. 1999. New paradigms of signaling in the vasculature: Ephrins and metalloproteases. Curr. Opin. Biotechnol. 10:536-540.
25. Johnston, R.F., S.C. Pickett, and D.L. Barker. 1990. Autoradiography using storage phosphor technology. Electrophoresis. 11:355-360.
26. Kang, Q., Y. Cao, and A. Zolkiewska. 2001. Direct interaction between the cytoplasmic tail of ADAM 12 and the Src homology 3 domain of p85α activates phosphatidylinositol 3-kinase in C2C12 cells. J. Biol. Chem. 276:24466-24472.
27. Kheradmand, F., and Z. Werb. 2002. Shedding light on sheddases: Role in growth and development. Bioessays. 24:8-12.
28. Kintner, C.R., and D.A. Melton. 1987. Expression of Xenopus N-CAM RNA in ectoderm is an early response to neural induction. Development. 99:311-325.
29. Lee, M.H., V. Verma, K. Maskos, J.D. Becherer, V. Knauper, P. Dodds, A. Amour, and G. Murphy. 2002. The C-terminal domains of TACE weaken the inhibitory action of N-TIMP-3. FEBS Lett. 520:102-106.
30. Lieber, T., S. Kidd, and M.W. Young. 2002. kuzbanian-mediated cleavage of Drosophila Notch. Genes Dev. 16:209-221.
31. Millichip, M.I., D.J. Dallas, E. Wu, S. Dale, and N. McKie. 1998. The metallodisintegrin ADAM10 (MADM) from bovine kidney has type IV collagenase activity in vitro. Biochem. Biophys. Res. Commun. 245:594-598.
32. Moss, M.L., J.M. White, M.H. Lambert, and R.C. Andrews. 2001. TACE and other ADAM proteases as targets for drug discovery. Drug Discov. Today. 6:417-426.
33. Murphy, G., F. Willenbrock, R.V. Ward, M.I. Cockett, D. Eaton, and A.J. Docherty. 1992. The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases. Biochem. J. 283:637-641.
34. Newport, J., and M. Kirschner. 1982. A major developmental transition in early Xenopus embryos: I. Characterization and timing of cellular changes at the midblastula stage. Cell. 30:675-686.
35. Nieuwkoop, P.D., and J. Faber. 1994. Normal Table of Xenopus Laevis (Daudin). Garland Publishing, Inc., New York. 252 pp.
36. Overall, C.M. 2002. Molecular determinants of metalloproteinase substrate specificity: Matrix metalloproteinase substrate binding domains, modules, and exosites. Mol. Biotechnol. 22:51-86.
37. Pan, D., and G.M. Rubin. 1997. Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis. Cell. 90:271-280.
38. Primakoff, P., and D.G. Myles. 2000. The ADAM gene family: Surface proteins with adhesion and protease activity. Trends Genet. 16:83-87.
39. Reddy, P., J.L. Slack, R. Davis, D.P. Cerretti, C.J. Kozlosky, R.A. Blanton, D. Shows, J.J. Peschon, and R.A. Black. 2000. Functional analysis of the domain structure of tumor necrosis factor-α converting enzyme. J. Biol. Chem. 275:14608-14614.
40. Schimmelpfeng, K., S. Gogel, and C. Klambt. 2001. The function of leak and kuzbanian during growth cone and cell migration. Mech. Dev. 106:25-36.
41. Schwettmann, L., and H. Tschesche. 2001. Cloning and expression in Pichia pastorts of metalloprotease domain of ADAM 9 catalytically active against fibronectin. Protein Expr. Purif. 21:65-70.
42. Seiki, M. 1999. Membrane-type matrix metalloproteinases. APMIS. 107:137-143.
43. Sive, H., and L. Bradley. 1996. A sticky problem: The Xenopus cement gland as a paradigm for anteroposterior patterning. Dev. Dyn. 205:265-280.
44. Stocker, W., and W. Bode. 1995. Structural features of a superfamily of zinc-endopeptidases: The metzincins. Curr. Opin. Struct. Biol. 5:383-390.
45. Takahashi, Y., D. Bigler, Y. Ito, and J.M. White. 2001. Sequence-specific interaction between the disintegrin domain of mouse ADAM 3 and murine eggs: Role of β1 integrin-associated proteins CD9, CD81, and CD98. Mol. Biol. Cell. 12:809-820.
46. White, J.M., D. Bigler, M. Chen, Y. Takahashi, and T.G. Wolfsbery. 2002. ADAMs. In Cell Adhesion: Frontiers in Molecular Biology. M. Beckerle, editor. Oxford University Press, Oxford. 189-216.
47. Zhang, X.P., T. Kamata, K. Yokoyama, W. Puzon-McLaughlin, and Y. Takada. 1998. Specific interaction of the recombinant disintegrin-like domain of MDC-15 (metargidin, ADAM-15) with integrin αvβ3. J. Biol. Chem. 273: 7345-7350.
48. Zhu, X., N.P. Bansal, and J.P. Evans. 2000. Identification of key functional amino acids of the mouse fertilin β (ADAM2) disintegrin loop for cell-cell adhesion during fertilization. J. Biol. Chem. 275:7677-7683.