Regular ArticleThe Prevention of Collagen Breakdown in Bovine Nasal Cartilage by TIMP, TIMP-2 and a Low Molecular Weight Synthetic Inhibitor
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Comparison of gene expression of tissue inhibitor of matrix metalloproteinase-1 between continuous and intermittent distraction osteogenesis: A quantitative study on rabbits
2012, Journal of Cranio-Maxillofacial SurgeryCitation Excerpt :Therefore, as an important regulator of MMPs, TIMPs play a pivotal role in the regulation of osteogenesis and remodeling during bone healing. The raise in TIMP-1 may prevent ECM from degradation, and also improves matrix accumulation and bone deposition (Shimizu et al., 1990; Everts et al., 1992; Ellis et al., 1994). Previous studies have focused on the effect of different distraction rates and the microenvironment of distraction osteogenesis.
Plasminogen activator inhibitor-1 deficient mice are protected from angiotensin II-induced fibrosis
2011, Archives of Biochemistry and BiophysicsCitation Excerpt :The accumulation of fibrin matrices was determined immunofluorometrically, as described previously [21]. Hydroxyproline content was quantitated colorimetrically from liver samples using the chloramine T method as described by Ellis et al. [22] with minor modifications [19]. The activity of tissue-type plasminogen activator (tPA) and urokinase-type plasminogen activator (uPA) were determined in liver and plasma samples as described by Bezerra et al. [23], with minor modifications [19].
Alleviative effects of s-allyl cysteine and s-ethyl cysteine on MCD diet-induced hepatotoxicity in mice
2008, Food and Chemical ToxicologyUnderstanding the role of tissue degrading enzymes and their inhibitors in development and disease
2006, Best Practice and Research: Clinical RheumatologyThe mammalian chitinase-like lectin, YKL-40, binds specifically to type I collagen and modulates the rate of type I collagen fibril formation
2006, Journal of Biological ChemistryCitation Excerpt :Diffuse Fibril Assay for Collagenase Activity—The assay is a modification of that previously described by Cawston and Barrett (62) and was performed using 3H-acetylated bovine type I collagen from calf skin (62, 63). The concentration of the collagen was estimated by hydroxyproline assay, using a modification of existing methods (65, 66). Ice-cold collagen (400 μg ml-1 in 50 mm Tris-HCl, pH 7.6, 200 mm NaCl, 0.02% w/v sodium azide) was diluted to 20 μgml-1 in a final volume of 100 μl with ice-cold cacodylate buffer with 50 mm NaCl containing recombinant human MMP-1 (diluted to 3.25 or 1.625 μgml-1) and/or purified YKL-40 from chondrocyte cultures (25, 50, or 100 μg ml-1).