EC Number   |
General Information |
Reference |
|---|
   3.4.24.14 | evolution |
the enzyme belongs to the a disintegrin and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch |
734611 |
| 3.4.24.14 | evolution |
the enzyme belongs to the disintegrin A and metalloproteinase with thrombospondin type I domain proteases (ADAMTS) family, M12B ADAM branch |
734611 |
| 3.4.24.14 | evolution |
the procollagen N-propeptidase belongs to the 'a disintegrin and metalloproteinase with thrombospondin type I domain' proteases (ADAMTS) family, M12B ADAM branch. Beside their specific enzymatic activity, the members are characterized by the presence of four thrombospondin type I domains (TSR1) and a C-terminal procollagen N-proteinase (PNP) domain comprising a protease-and-lacunin (PLAC) domain |
754590 |
| 3.4.24.14 | evolution |
the procollagen N-propeptidase belongs to the 'a disintegrin and metalloproteinase with thrombospondin type I domain' proteases (ADAMTS) family, M12B ADAM branch. Beside their specific enzymatic activity, the members are characterized by the presence of four thrombospondin type I domains (TSR1) and a C-terminal procollagen N-proteinase (PNP) domain comprising a protease-and-lacunin (PLAC) domain. ADAMTS14 is coexpressed with ADAMTS2 |
754590 |
| 3.4.24.14 | malfunction |
ADAMTS 3, one of the procollagen proteinases, is decreased in severe obstructive sleep apnea (OSA), overview. Lack of ADAMTS 3 proteinase may contribute to process of sleep apnea due to insufficient collagen syntheses |
755550 |
| 3.4.24.14 | malfunction |
Adamts2-deficient mice phenotype, overview. The absence of ADAMTS2 activity leads to the dermatosparactic type of Ehlers-Danlos syndrome, also previously known as EDS-type VIIC |
734611 |
| 3.4.24.14 | malfunction |
an anti-tumoral activity is also observed when using cells expressing recombinant deleted forms of ADAMTS-2, including catalytically inactive enzyme |
717467 |
| 3.4.24.14 | malfunction |
in absence of ADAMTS2 activity (Ehlers-Danlos syndrome, dermatosparactic type) accumulation of processed alpha alpha1 and alpha2 chains, pNalpha1 and pNalpha2, is observed |
754632 |
| 3.4.24.14 | malfunction |
in Adamts2-KO mouse livers, collagen fibers are thinner and more irregular than in the control littermates, which correlated also with faster collagen degradation. Fragility of the skin occurs in Adamts2-KO mice |
754590 |
| 3.4.24.14 | malfunction |
in vivo, the formation of tumors in nude mice by HEK cells is strongly reduced when they overexpress ADAMTS2, an observation that is correlated to a reduced intratumoral vascularization but that might also involve direct anti-tumor effects. The absence of ADAMTS2 activity leads to a different type of disease, the dermatosparactic type of Ehlers-Danlos syndrome (EDS, also previously known as EDS-type VIIC). The main clinical manifestation of this rare genetic disease is the fragility of the skin, as in Adamts2-KO mice, but joint laxity is usually only moderate, which contrasts with the hypermobility in arthrochalasic EDS. The arthrochalasic type of EDS, caused by mutations affecting the aminoprocollagen cleavage site in alpha1 or alpha2 type I procollagen, is mainly characterized by joint hyperlaxity while skin collagen fibers are only moderately affected. EDS phenotypes, overview |
754590 |
