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Gene Review

adam33  -  ADAM metallopeptidase domain 33

Xenopus laevis

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Disease relevance of ADAM13


High impact information on ADAM13

  • Using chimeric constructs, we find that the metalloprotease domain of ADAM10 can substitute for that of ADAM13, but that specificity for cement gland expansion requires a downstream extracellular domain of ADAM13 [1].
  • These and other results reveal that the cysteine-rich domain of ADAM13 cooperates intramolecularly with the ADAM13 metalloprotease domain to regulate its function in vivo [1].
  • In addition, ectopic expression of wild-type ADAM 13 results in a gain-of-function phenotype in embryos, namely the abnormal positioning of trunk neural-crest cells [2].
  • We focused our study on X-PACSIN2 protein because it colocalizes with ADAM13 in migrating neural crest cells during embryonic development [3].
  • ADAM13 is a cell surface metalloprotease expressed in cephalic neural crest cells during early Xenopus development [3].

Biological context of ADAM13


Anatomical context of ADAM13


Associations of ADAM13 with chemical compounds

  • We address this important question by analyzing the relative contributions of downstream extracellular domains (disintegrin, cysteine rich, and EGF-like repeat) of the ADAM13 metalloprotease during Xenopus laevis development [1].

Other interactions of ADAM13

  • Microinjection of Xerl mRNA into 2- or 4-cell stage embryos indicated that Xerl overexpression caused the regional expansion of XlSox-2- and NCAM-positive neural plate, which was concomitant with the outer shift of ADAM13-positive region [6].

Analytical, diagnostic and therapeutic context of ADAM13

  • Sequence analyses of the X-ADAM 13 metalloprotease and disintegrin domains indicate that the protein is likely to be involved in both proteolytic and cell-adhesive functions [4].
  • RESULTS: Using a tissue transplantation technique, we show that Xenopus CNC cells overexpressing wild-type ADAM 13 migrate along the same hyoid, branchial, and mandibular pathways used by normal CNC cells [2].


  1. The cysteine-rich domain regulates ADAM protease function in vivo. Smith, K.M., Gaultier, A., Cousin, H., Alfandari, D., White, J.M., DeSimone, D.W. J. Cell Biol. (2002) [Pubmed]
  2. Xenopus ADAM 13 is a metalloprotease required for cranial neural crest-cell migration. Alfandari, D., Cousin, H., Gaultier, A., Smith, K., White, J.M., Darribère, T., DeSimone, D.W. Curr. Biol. (2001) [Pubmed]
  3. PACSIN2 is a regulator of the metalloprotease/disintegrin ADAM13. Cousin, H., Gaultier, A., Bleux, C., Darribère, T., Alfandari, D. Dev. Biol. (2000) [Pubmed]
  4. ADAM 13: a novel ADAM expressed in somitic mesoderm and neural crest cells during Xenopus laevis development. Alfandari, D., Wolfsberg, T.G., White, J.M., DeSimone, D.W. Dev. Biol. (1997) [Pubmed]
  5. Neural crest-specific and general expression of distinct metalloprotease-disintegrins in early Xenopus laevis development. Cai, H., Krätzschmar, J., Alfandari, D., Hunnicutt, G., Blobel, C.P. Dev. Biol. (1998) [Pubmed]
  6. Xerl, a novel CNS-specific secretory protein, establishes the boundary between neural plate and neural crest. Kuriyama, S., Kinoshita, T. Int. J. Dev. Biol. (2001) [Pubmed]
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