ADAMTS10 explained

A disintegrin and metalloproteinase with thrombospondin motifs 10 is an enzyme that in humans is encoded by the ADAMTS10 gene.^[1]

This gene belongs to the ADAMTS (a disintegrin and metalloproteinase domain with thrombospondin type-1 motifs) family of zinc-dependent proteases. ADAMTS proteases are complex secreted enzymes containing a prometalloprotease domain of the reprolysin type attached to an ancillary domain with a highly conserved structure that includes at least one thrombospondin type 1 repeat. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration. The product of this gene plays a major role in growth and in skin, lens, and heart development. It is also a candidate gene for autosomal recessive Weill-Marchesani syndrome.

Further reading

• Tang BL . ADAMTS: a novel family of extracellular matrix proteases. . Int. J. Biochem. Cell Biol. . 33 . 1 . 33–44 . 2001 . 11167130 . 10.1016/S1357-2725(00)00061-3 .
• Faivre L, Dollfus H, Lyonnet S . Clinical homogeneity and genetic heterogeneity in Weill-Marchesani syndrome. . Am. J. Med. Genet. A . 123 . 2 . 204–7 . 2004 . 14598350 . 10.1002/ajmg.a.20289 . 13600027 . etal.
• Apte SS . A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: the ADAMTS family. . Int. J. Biochem. Cell Biol. . 36 . 6 . 981–5 . 2004 . 15094112 . 10.1016/j.biocel.2004.01.014 .
• Faivre L, Mégarbané A, Alswaid A . Homozygosity mapping of a Weill-Marchesani syndrome locus to chromosome 19p13.3-p13.2. . Hum. Genet. . 110 . 4 . 366–70 . 2002 . 11941487 . 10.1007/s00439-002-0689-3 . 10463979 . etal.
• Strausberg RL, Feingold EA, Grouse LH . Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. . Proc. Natl. Acad. Sci. U.S.A. . 99 . 26 . 16899–903 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . 2002PNAS...9916899M . etal. free .
• Brandenberger R, Wei H, Zhang S . Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation. . Nat. Biotechnol. . 22 . 6 . 707–16 . 2005 . 15146197 . 10.1038/nbt971 . 27764390 . etal.
• Fu GK, Wang JT, Yang J . Circular rapid amplification of cDNA ends for high-throughput extension cloning of partial genes. . Genomics . 84 . 1 . 205–10 . 2005 . 15203218 . 10.1016/j.ygeno.2004.01.011 . etal.
• Somerville RP, Jungers KA, Apte SS . Discovery and characterization of a novel, widely expressed metalloprotease, ADAMTS10, and its proteolytic activation. . J. Biol. Chem. . 279 . 49 . 51208–17 . 2005 . 15355968 . 10.1074/jbc.M409036200 . free .
• Charrier L, Yan Y, Driss A . ADAM-15 inhibits wound healing in human intestinal epithelial cell monolayers. . Am. J. Physiol. Gastrointest. Liver Physiol. . 288 . 2 . G346–53 . 2005 . 15358598 . 10.1152/ajpgi.00262.2004 . etal.
• Dagoneau N, Benoist-Lasselin C, Huber C . ADAMTS10 mutations in autosomal recessive Weill-Marchesani syndrome. . Am. J. Hum. Genet. . 75 . 5 . 801–6 . 2005 . 15368195 . 10.1086/425231 . 1182109 . etal.

External links

• GeneReviews/NIH/NCBI/UW entry on Weill-Marchesani Syndrome
• The MEROPS online database for peptidases and their inhibitors: M12.235

Notes and References

1. Web site: Entrez Gene: ADAMTS10 ADAM metallopeptidase with thrombospondin type 1 motif, 10.