(redirected from Gelatinases)
Also found in: Encyclopedia.


Pepsin B; a metalloproteinase that hydrolyzes gelatin and a number of types of collagen. See: pepsin.



MMP-2; MMP-9

Metalloproteinases that cleave gelatin, or nondenatured collagen. Two forms of gelatinase, A and B, have been identified. Gelatinase A (MMP-2) has a molecular weight of about 72,000, and gelatinase B (MMP-9) has a molecular weight of about 92,000. Both are involved in cancer angiogenesis and metastasis and are blocked by a variety of naturally occurring and synthetic inhibitors.
References in periodicals archive ?
Tetracyclines are a class of antibiotics which inhibit the catalytic activity of human collagenases and gelatinases, especially MMPs.
An increase in the expression of gelatinases in tumour cells in patients diagnosed with renal carcinoma was demonstrated.
All bacterial isolates from the Nile tilapia culture water were subjected to the tests of virulence factor expression, with the help of the following exoenzymes: gelatinase (GEL), elastase (Elas), caseinase (CAS), lipase (LIP), phospholipase (Phos) and haemolytic activity ([beta]-hemolysis in sheep blood) ([beta]-hem), following the methodologies of Rust, Messing, and Iglewski (1994), Rodrigues, Ribeiro, Alves, and Hofer (1993) and Furniss and Donovan (1979).
MMP-2, MMP-3, MMP-9, MMP-13, and MT1-MMP have all been identified in neuronal nuclei and gelatinases (MMP-2 and MMP-9) and MMP-3 have been implicated in the progression of infarct volume and neuronal death in animal models of stroke and ischemic stroke patients [9,16,18, 23, 29-33].
Collagenases, gelatinases, stromelysin-3, matrilysin, MT1-MMP [99], and stromelysin-1 [100] are considered the most closely associated to the invasive phenotype.
Gelatinases, endonuclease and Vascular Endothelial Growth Factor during development and regression of swine luteal tissue.
In the present study, we compared the selectivity of SalA on collagenases and gelatinases which are two kinds of MMPs that play important roles in aortic remodeling.
Unemori EN, Hibbs MS, Amento EP (1991) Constitutive expression of a 92kD gelatinase (type V collagenase) by rheumatoid synovial fibroblasts and its induction in normal human fibroblasts by inflammatory cytokines.
We assessed putative MMP activity using gelatinase activity in organ homogenates with the EnzChek gelatinase assay kit (Invitrogen, Carlsbad, CA).
2010) have studied gelatinases MMP-2 and MMP9 in both normal tissues and the ones with benign and malignant lesions in different species, including dogs, since MMPs are proteolytic enzymes capable of degrading components of connective tissue, such as the ECM, during tissue remodeling, which occurs in physiologic and pathologic conditions (EGEBLAD & WERB, 2002; MOOK et al.