ADAMTS
ADAMTS (A Disintegrin And Metalloproteinase with Thrombospondin Motifs) is a family of peptidases.[1] 19 members of this family have been identified in humans. Known functions of the ADAMTS proteases include processing of procollagens and von Willebrand factor as well as cleavage of aggrecan, versican, brevican and neurocan. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration.[2]
Family members are:
- ADAMTS1
- ADAMTS2
- ADAMTS3
- ADAMTS4
- ADAMTS5 (=ADAMTS11)
- ADAMTS6
- ADAMTS7
- ADAMTS8 (or METH-2), an antiangiogenic[3]
- ADAMTS9
- ADAMTS10
- ADAMTS12
- ADAMTS13
- ADAMTS14
- ADAMTS15
- ADAMTS16
- ADAMTS17
- ADAMTS18
- ADAMTS19
- ADAMTS20
See also
- A disintegrin and metalloproteinase (ADAM) family
References
- ^ Brocker, C (2009). "Evolutionary divergence and functions of the ADAM and ADAMTS gene families". Human Genomics. 4 (1): 43–55. PMID 19951893.
{{cite journal}}: Unknown parameter|coauthors=ignored (|author=suggested) (help); Unknown parameter|month=ignored (help) - ^ Apte, Suneel (2004). "A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: the ADAMTS family". The international Journal of Biochemistry and Cell Biology. 15: 981–985. PMID 20036837.
- ^ METH-2 silencing and promoter hypermethylation in NSCLC