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Science 28 September 1984:
Vol. 225. no. 4669, pp. 1489 - 1491
DOI: 10.1126/science.6147899
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Articles

Science, Vol 225, Issue 4669, 1489-1491
Copyright © 1984 by American Association for the Advancement of Science

articles

Inhibition of collagen fibril formation in vitro and subsequent cross-linking by glucose

YH Lien, R Stern, JC Fu, and RC Siegel

Glucose inhibits collagen fibril formation in vitro. A linear dose response was observed, with half-maximum inhibition of fibril formation occurring at 50 mM glucose. Nonfibrillar collagen cannot be cross-linked by lysyl oxidase, an enzyme that catalyzes the initial cross-linking reaction. The degree of decreased fibril formation correlated with the loss of ability of the collagen to serve as a substrate for lysyl oxidase. Collagen that is not cross-linked is unstable and more susceptible to collagenolytic attack. Interference with collagen cross-linking and more rapid degradation may explain the decreased amounts of interstitial collagen and the poor healing of wounds associated with diabetes mellitus.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Lysyl Oxidase Activity in the Ocular Tissues and the Role of LOX in Proliferative Diabetic Retinopathy and Rhegmatogenous Retinal Detachment.
K. Coral, N. Angayarkanni, J. Madhavan, M. Bharathselvi, S. Ramakrishnan, K. Nandi, P. Rishi, N. Kasinathan, and S. Krishnakumar (2008)
Invest. Ophthalmol. Vis. Sci. 49, 4746-4752
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Science. ISSN 0036-8075 (print), 1095-9203 (online)