metalloproteinase

(redirected from Metalloprotease)
Also found in: Dictionary.

me·tal·lo·pro·tein·ase

(met'a-lō-prō'tēn-āz),
A family of protein-hydrolyzing endopeptidases that contain zinc ions as part of the active structure.

me·tal·lo·pro·tein·ase

(mĕ-tal'ō-prō'tēn-ās)
A family of protein-hydrolyzing endopeptidases that contain zinc ions as part of the active structure.
References in periodicals archive ?
67) The function of GON-1, a homolog of human ADAMTS9 metalloprotease, made us recognize that an important domain (GON domain) in the C-terminus, which is not related to protease but plays a critical role for cells to normally secrete proteins, has been ignored because the metalloprotease domain is so obvious.
A ~90 kDa band was observed by zymography corresponding to metalloprotease activity (FIG.
Patients who reached success at 12 weeks were those who started with lower baseline levels of matrix metalloprotease, or lower or intermediate baseline levels of serine protease," Dr.
Large multimers are assembled in a normal fashion but straight after secretion they bind spontaneously to platelets and are cleaved by ADAMTS 13, a disintegrin-like and metalloprotease domain with thrombosponding type 1 motifs (12).
The Extracellular metalloprotease of Vibrio tubiashii is a major virulence factor for Pacific oyster (Crassostrea gigas) larvae.
Polymorphisms in a disintegrin and metalloprotease 33 gene and the risk of chronic obstructive pulmonary disease: a meta-analysis.
As stated, a number of disease states involve overexpression of matrix metalloproteases, and there exist diseases in which mutations result in overexpression of MMP-13 and premature development of osteoarthritis.
CD 10 is a single-chain, 90-110-kDa cell surface zinc dependent metalloprotease inactivating various bioactive neuropeptides.
Decreased metalloprotease 9 induction, cardiac fibrosis, and higher autophagy after pressure overload in mice lacking the transcriptional regulator p8.
A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: the ADAMTS family.
Membrane type 1 matrix metalloprotease cleaves laminin-10 and promotes prostate cancer cell migration.
Matrix metalloprotease (MMP) is an endopeptidase expressed in human urine whenever cancer is present.