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Gene Review:

adam33 - ADAM metallopeptidase domain 33

Xenopus laevis

Smith, K.M. et al., Alfandari, D. et al., Cousin, H. et al., Alfandari, D. et al., Kuriyama, S. et al., et al.

Alfandari, Cousin, Gaultier, Smith, White, Darribère, DeSimone,

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Disease relevance of ADAM13

When expressed in embryos, ADAM13 induces hyperplasia of the cement gland, whereas ADAM10 does not [1].

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

We call this cDNA, and the 915-amino-acid protein it encodes, ADAM 13, X-ADAM 13 RNA is expressed during embryogenesis from the midblastula stage through tadpole stage 45 [4].
Our data suggest that X-ADAM 13 may be involved in neural crest cell adhesion and migration as well as myoblast differentiation [4].
The cytoplasmic domain of ADAM13 contains three potential SH3 (Src homology type 3) binding sites, suggesting that this region may support interactions with intracellular proteins [3].

Anatomical context of ADAM13

X-ADAM 13 is localized to somitic mesoderm and cranial neural crest cells during gastrulation, neurulation, and in tail bud stages [4].
Using Xenopus XTC cells, we demonstrate that ADAM13 and X-PACSIN2 colocalize to membrane ruffles and cytoplasmic vesicles [3].
While adam13 is expressed in the somitic mesoderm and in neural crest cells, but not in adult testis, xmdc13 expression is low and ubiquitous in the developing embryo, but is clearly present in adult testis [5].

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].

References

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]
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]
PACSIN2 is a regulator of the metalloprotease/disintegrin ADAM13. Cousin, H., Gaultier, A., Bleux, C., Darribère, T., Alfandari, D. Dev. Biol. (2000) [Pubmed]
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]
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]
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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