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Lysyl Oxidase as a Potential Therapeutic Target
Drug News & Perspectives, 2008Lysyl oxidase (LOX) is a copper-dependent amine oxidase that catalyzes the covalent cross-link of collagens and elastin in the extracellular environment, thereby determining the mechanical properties of extracellular matrix (ECM) and connective tissues. ECM remodeling is a common feature of diverse pathologic processes.
Cristina, Rodríguez +2 more
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Identification of the disulfide bonds of lysyl oxidase
Journal of Neural Transmission, 2010Proteolytic digestion of bovine aortic lysyl oxidase followed by tandem mass spectrometry has enabled assignment of all five disulfide bonds. The results indicate that the enzyme has a very stable central core containing three disulfide bonds, the lysyl tyrosyl quinone cross-link and the copper.
Xi, Chen, Frederick T, Greenaway
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Simplified assay for lysyl oxidase activity
Analytical Biochemistry, 1977Abstract A simplified method for the assay of lysyl oxidase activity was developed. The method is based on the measurement of tritiated water released by enzyme action from labeled protein-bound lysine and hydroxylysine. Trichloroacetic acid (TCA) supernates of the incubation mixtures are passed through small Dowex 50 (H+) columns and the effluents ...
J, Melet, G D, Vianden, B N, Bachra
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Targeting the lysyl oxidases in tumour desmoplasia
Biochemical Society Transactions, 2019The extracellular matrix (ECM) is a fundamental component of tissue microenvironments and its dysregulation has been implicated in a number of diseases, in particular cancer. Tumour desmoplasia (fibrosis) accompanies the progression of many solid cancers, and is also often induced as a result of many frontline chemotherapies.
Jessica L. Chitty +2 more
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Changes in lysyl oxidase (LOX) distribution and its decreased activity in keratoconus corneas
Experimental Eye Research, 2012Ľubica Dudáková +2 more
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Lysyl oxidase: Properties, specificity, and biological roles inside and outside of the cell
Journal of Cellular Biochemistry, 2003Herbert M Kagan, Wande Li
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