A disintegrin and metalloproteinase with thrombospondin motifs 8 is an
enzyme that in humans is encoded by the ADAMTS8gene.[5][6]
Function
This gene encodes a member of the
ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of the family share several distinct protein modules, including a propeptide region, a
metalloproteinase domain, a
disintegrin-like domain, and a
thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of
C-terminal TS motifs, and some have unique C-terminal domains. The enzyme encoded by this gene contains two C-terminal TS motifs, and disrupts angiogenesis in vivo.[6]
Clinical significance
A number of disorders have been mapped in the vicinity of this gene, most notably lung neoplasms.[6]
Wågsäter D, Björk H, Zhu C, et al. (2008). "ADAMTS-4 and -8 are inflammatory regulated enzymes expressed in macrophage-rich areas of human atherosclerotic plaques". Atherosclerosis. 196 (2): 514–22.
doi:
10.1016/j.atherosclerosis.2007.05.018.
PMID17606262.
Porter S, Span PN, Sweep FC, et al. (2006). "ADAMTS8 and ADAMTS15 expression predicts survival in human breast carcinoma". Int. J. Cancer. 118 (5): 1241–7.
doi:
10.1002/ijc.21476.
PMID16152618.
S2CID20711295.
Georgiadis KE, Hirohata S, Seldin MF, Apte SS (2000). "ADAM-TS8, a novel metalloprotease of the ADAM-TS family located on mouse chromosome 9 and human chromosome 11". Genomics. 62 (2): 312–5.
doi:
10.1006/geno.1999.6014.
PMID10610729.
External links
The
MEROPS online database for peptidases and their inhibitors:
M12.226
A disintegrin and metalloproteinase with thrombospondin motifs 8 is an
enzyme that in humans is encoded by the ADAMTS8gene.[5][6]
Function
This gene encodes a member of the
ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of the family share several distinct protein modules, including a propeptide region, a
metalloproteinase domain, a
disintegrin-like domain, and a
thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of
C-terminal TS motifs, and some have unique C-terminal domains. The enzyme encoded by this gene contains two C-terminal TS motifs, and disrupts angiogenesis in vivo.[6]
Clinical significance
A number of disorders have been mapped in the vicinity of this gene, most notably lung neoplasms.[6]
Wågsäter D, Björk H, Zhu C, et al. (2008). "ADAMTS-4 and -8 are inflammatory regulated enzymes expressed in macrophage-rich areas of human atherosclerotic plaques". Atherosclerosis. 196 (2): 514–22.
doi:
10.1016/j.atherosclerosis.2007.05.018.
PMID17606262.
Porter S, Span PN, Sweep FC, et al. (2006). "ADAMTS8 and ADAMTS15 expression predicts survival in human breast carcinoma". Int. J. Cancer. 118 (5): 1241–7.
doi:
10.1002/ijc.21476.
PMID16152618.
S2CID20711295.
Georgiadis KE, Hirohata S, Seldin MF, Apte SS (2000). "ADAM-TS8, a novel metalloprotease of the ADAM-TS family located on mouse chromosome 9 and human chromosome 11". Genomics. 62 (2): 312–5.
doi:
10.1006/geno.1999.6014.
PMID10610729.
External links
The
MEROPS online database for peptidases and their inhibitors:
M12.226