Biology:ADAMTS

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ADAMTS (short for a disintegrin and metalloproteinase with thrombospondin motifs) is a family of multidomain extracellular protease enzymes.[1] 19 members of this family have been identified in humans, the first of which, ADAMTS1, was described in 1997.[2] Known functions of the ADAMTS proteases include processing of procollagens and von Willebrand factor as well as cleavage of aggrecan, versican, brevican and neurocan, making them key remodeling enzymes of the extracellular matrix. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration.[3][4] Homologous subfamily of ADAMTSL (ADAMTS-like) proteins, which lack enzymatic activity, has also been described.[5] Most cases of thrombotic thrombocytopenic purpura arise from autoantibody-mediated inhibition of ADAMTS13.

Like ADAMs, the name of the ADAMTS family refers to its disintegrin and metalloproteinase activity, and in the case of ADAMTS, the presence of a thrombospondin motif.

ADAMTS family members

Clinical findings and distribution of affected organs in individuals with Mendelian disorders caused by pathogenic mutations in different ADAMTS family genes. Predominant and recurrently reported clinical presentations of eight ADAMTS genes with a strong causal relationship to Mendelian disorders are marked according to organ. Heterogeneous distribution of affected organ types indicates the phenotypic heterogeneity among hereditary disorders caused by pathogenic germline mutations in ADAMTS genes. From a review by Rim et al., 2020[6]

See also

  • A disintegrin and metalloproteinase (ADAM) family
  • ADAMTSL family (ADAMTS-like proteins)

References

  1. ↑ Brocker, C; Vasiliou, V; Nebert, DW (Oct 2009). "Evolutionary divergence and functions of the ADAM and ADAMTS gene families.". Human Genomics 4 (1): 43–55. doi:10.1186/1479-7364-4-1-43. PMID 19951893. 
  2. ↑ Porter, Sarah; Clark, Ian M.; Kevorkian, Lara; Edwards, Dylan R. (15 February 2005). "The ADAMTS metalloproteinases". Biochemical Journal 386 (1): 15–27. doi:10.1042/BJ20040424. PMID 15554875. 
  3. ↑ Apte, Suneel (2004). "A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: the ADAMTS family". The International Journal of Biochemistry & Cell Biology 15 (6): 981–985. doi:10.1016/j.biocel.2004.01.014. PMID 20036837. 
  4. ↑ Kelwick, Richard; Desanlis, Ines; Wheeler, Grant N; Edwards, Dylan R (2015-05-30). "The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family" (in En). Genome Biology 16 (1): 113. doi:10.1186/s13059-015-0676-3. PMID 26025392. 
  5. ↑ Cormier-Daire V, Le Goff C (2011). "The ADAMTS(L) family and human genetic disorders". Human Molecular Genetics 20 (R2): R163–R167. doi:10.1093/hmg/ddr361. PMID 21880666. 
  6. ↑ "Genomic Landscape and Mutational Spectrum of ADAMTS Family Genes in Mendelian Disorders Based on Gene Evidence Review for Variant Interpretation". Biomolecules 10 (3): 449. March 2020. doi:10.3390/biom10030449. PMID 32183147. 
  7. ↑ METH-2 silencing and promoter hypermethylation in NSCLC



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