Matrix metalloproteinases (MMPs) are thought to play important roles during enamel and dentin biomineralization. Previously, membrane type-1 matrix metalloproteinase (MT1-MMP) was localized to the plasma membranes of ameloblasts and odontoblasts of the developing tooth. The best-characterized function of MT1-MMP is to initiate the activation of gelatinase A (MMP-2). Thus, we hypothesized that g...

Abdominal aortic aneurysms (AAA) are characterized by disruption and degradation of the elastic media, yet the elastolytic proteinases involved and their cellular sources are undefined. We examined if 92-kD gelatinase, an elastolytic matrix metalloproteinase, participates in the pathobiology of AAA. Gelatin zymography of conditioned medium from normal, atheroocclusive disease (AOD), or AAA tiss...

Gelatinase A, a member of the matrix metalloproteinase (MMP) family, plays an important role during angiogenesis. It is constitutively expressed by human endothelial cells as a latent enzyme and requires activation. Thrombin is the only described physiological inducer of gelatinase A in human endothelial cells. In this study, we investigated the mechanisms of gelatinase A activation by another ...

We report here that a 92-kD gelatinolytic metalloproteinase is expressed as protein and mRNA in human osteoarthritic cartilage, but not in normal adult articular cartilage. Western immunoblotting demonstrated that the 92-kD gelatinolytic activity corresponded to 92-kD type IV collagenase/gelatinase (gelatinase B); mRNA for gelatinase B was identified by Northern blotting. Chondrocytes from norm...

An e.l.i.s.a. was developed using specific polyclonal rabbit antibodies against human neutrophil gelatinase. This assay, in contrast to the functional assay, is independent of activation of gelatinase, and is specific for the detection of gelatinase in both its reduced and unreduced forms. Using this assay, we were able to demonstrate a difference between the subcellular localization of gelatin...

Members of the gelatinase subclass of the matrix metalloproteinase family have the capacity to degrade denatured collagens of all types and native types IV, V, and VII collagens. The authors identified the metalloproteinase species of the gelatinase class produced by the cells of rabbit corneal tissue. Two different molecular forms of gelatinase, visualized as enzymatic activities, that undergo...

Previous studies have correlated release of the 92 kDa type IV collagenase/gelatinase by tumor cells in culture with metastatic potential. We have now demonstrated that the ability of tumor cells that do not express the 92 kDa gelatinase to induce release of this metalloproteinase from normal fibroblasts may also be associated with the metastatic phenotype. A transformed rat embryo cell line, 2...

PURPOSE The regulation of the trabecular meshwork's extracellular matrix is poorly understood and may involve a family of secreted proteinases, the matrix metalloproteinases. Because the trabecular extracellular matrix has been hypothesized to affect intraocular pressure, an evaluation was made of the ability of two cellular modulators to change the levels of matrix metalloproteinases in the me...

A competitive and a sandwich enzyme linked immunosorbent assay (ELISA) were developed for human leukocyte collagenase and gelatinase. The competitive assay could detect 0.5 ng collagenase and 0.05 ng gelatinase. The detection limit of the sandwich ELISA was 0.05 ng for collagenase and 0.02 ng for gelatinase. No cross reactivity between human leukocyte collagenase and gelatinase was detected. Th...

Previous investigators have proposed that gelatinase, a metalloproteinase found in neutrophils, is stored in a novel secretory compartment distinct from the two major granule populations, azurophilic and specific. To locate this proteinase in human neutrophils we reacted the cells for peroxidase and then applied monospecific polyclonal antibodies to human neutrophil gelatinase to immunolabel ul...