matrilysin

matrix metalloproteinase 7

A 19-kD enzyme encoded on chromosome 11q21-q22 which degrades fibronectin, gelatins and other matrix substrates.

Cytokine inducers 
BTC, EGF, FGF-a, FGF-b, FGF-9, FGF-10, hourG-β1, IL-1α, IL-1β, IL-4, IL-10, TGF-β1, TNF-α.
 
Substrates
Collagens IV and X; gelatin; aggrecan; decorin; proteoglycan link protein; fibronectin and laminin; insoluble fibronectin fibrils; entactin; large and small tenascin-C; osteonectin; β4 intergrin; elastin; casein; transferrin; MBP; α1-AT; GST-TNF/TNF peptide; plasminogen; MMP-1; MMP-2; MMP-9; MMP-9/TIMP-1 complex.

matrilysin

A member of the matrix metalloproteinase enzyme family that is expressed by many tumor cells and plays a part in tissue invasion and metastasis.
References in periodicals archive ?
Wakefield, "Active matrilysin (MMP-7) in human pterygia: potential role in angiogenesis," Investigative Ophthalmology & Visual Science, vol.
Senior, "Matrilysin is much more efficient than other matrix metalloproteinases in the proteolytic inactivation of [[alpha].sub.1]-antitrypsin," Biochemical and Biophysical Research Communications, vol.
Association of matrilysin expression with recurrence and poor prognosis in human esophageal squamous cell carcinoma.
A study involving 156 patients, who underwent radical nephrectomy due to RCC, was focused on the assessment of matrilysin 1 in relation to the aggressiveness and malignancy of this tumour.
Matrilysin (MMP7) promotes invasion of ovarian cancer cells by activation of progelatinase.
Tissue inhibitor of metalloproteinase-1 moderates airway reepithelialization by regulating matrilysin activity.
Still, other studies report that matrilysin (uterine metalloproteinase) generates the active soluble form of FasL [48, 49].
Among the MMPs, MMP-7, known as matrilysin, has a broad spectrum of proteolytic activity capable of cleaving various types of extracellular matrix [15].
Collagenases, gelatinases, stromelysin-3, matrilysin, MT1-MMP [99], and stromelysin-1 [100] are considered the most closely associated to the invasive phenotype.
Up-Regulated Expression Of Matrilysin And Neutrophil Collagenase in Human Herniated Discs.
Hypochlorous acid generated by myeloperoxidase modifies adjacent tryptophan and glycine residues in the catalytic domain of matrix metalloproteinase-7 (matrilysin): an oxidative mechanism for restraining proteolytic activity during inflammation.