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Gelatinase activity

Qazi and Khachatourians (2007) reported proteases with gelatinase activity released by hydrated conidia of M. anisopliae inhibition and activation studies revealed the presence of various spore-associated metalloprotease isozymes. [Pg.279]

Smith GN Jr, Yu LP Jr, Brandt KD, et al. Oral administration of doxycy-cline reduces collagenase and gelatinase activities in extracts of human osteoarthritic cartilage. J Rheumatol 1998 25 532-535. [Pg.1702]

Lijnen, H.R., et al.. Regulation of gelatinase activity in mice with targeted inactivation of components of the plasminogen/ plasmin system. Thromb Haemost, 1998. 79(6) p. 1171-6. [Pg.142]

Birri, D.J., Brede, D.A., Tessema, G.T., and Nes, I.F. (2013). Bacteriocin production, antibiotic susceptibility and prevalence of haemolytic and gelatinase activity in faecal lactic acid bacteria isolated from healthy Ethiopian infants. Microl) coZ 65, 504-516. [Pg.94]

Herbert CA, Arthur MJ, Robinson C. Augmentation by eosinophils of gelatinase activity in the airway mucosa comparative effects as a putative mediator of epithelial injury. Br J Pharmacol 1996 117 667-674. [Pg.513]

MMPS Gelatinase-B, 92 kDa gelatinase Secreted MM P-9 plays a regulatory role in angiogenesis not only through proteolytic activity but also through other downstream angiogenic factors... [Pg.746]

The matrix metalloproteinases are inhibited by specific endogenous tissue inhibitor of metalloproteinases (TIMPs), which comprise a family of four protease inhibitors TIMP-1, TIMP-2, TIMP-3, and TIMP-4. Overall, all MMPs are inhibited by TIMPs once they are activated but the gelatinases (MMP-2 and MMP-9) can form complexes with TIMPs when the enzymes are in the latent form. [Pg.1201]

Figure 5.7. Translocation of cytochrome b to the plasma membrane. In non-stimulated cells, only a small proportion of the total cellular pool of cytochrome b is present on the plasma membrane. The major pool of this cytochrome is located on the membranes of specific granules, gelatinase-containing granules and secretory vesicles. During activation (e.g. by fMet-Leu-Phe or PMA) or priming (e.g. by cytokines), some of these subcellular pools of cytochrome b molecules are translocated to the plasma membrane, thereby increasing the level of surface cytochrome b. Figure 5.7. Translocation of cytochrome b to the plasma membrane. In non-stimulated cells, only a small proportion of the total cellular pool of cytochrome b is present on the plasma membrane. The major pool of this cytochrome is located on the membranes of specific granules, gelatinase-containing granules and secretory vesicles. During activation (e.g. by fMet-Leu-Phe or PMA) or priming (e.g. by cytokines), some of these subcellular pools of cytochrome b molecules are translocated to the plasma membrane, thereby increasing the level of surface cytochrome b.
Furthermore, the myeloperoxidase systems can stimulate secretion of serotonin from platelets, histamine release from mast cells and the activation of latent collagenase and latent gelatinase of neutrophils. [Pg.171]

Observations of neutrophil function in whole blood and after purification have led to the realisation that many commonly-used purification procedures partially prime neutrophils, presumably by mobilising the more easily-activated subcellular stores of surface molecules (i.e. gelatinase-containing granules or secretory vesicles). [Pg.242]

Total PA activity Total PA activity Collagenase 1 Collagenase 1 CB-Iike enzyme Trypsin-like enzyme Chymotrypsin-like enzyme 92-kDa gelatinase Heparanase... [Pg.146]

In a study conducted by Szardenings et various combinatorial libraries of DPKs scaffolds were created to design and evaluate the activity of DPKs as inhibitors of the matrix metalloproteinases, namely, collegenase-1 and gelatinase B. This study created structure-activity relationships (SAR) for side chains attached to a DPK core structure. These enzymes are therapeutic targets with indications in the treatment of cancer, arthritis, autoimmunity, and cardiovascular disease. [Pg.682]

Ray JM, Stetler-Stevenson WG. Gelatinase A activity directly modulates melanoma call adhesion and spreading. EMBO J 1995 14 908-917. [Pg.390]


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See also in sourсe #XX -- [ Pg.15 ]




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