Quantitative Determination of Collagen Cross-links

羟赖氨酸 赖氨酰氧化酶 桥粒碱 化学 氧化脱氨基 赖氨酸 阿玛多利重排 交叉连接 糖基化 脱氨基 生物化学 戊糖苷 胺气处理 弹性蛋白 氨基酸 有机化学 细胞外基质 聚合物 生物 受体 遗传学
作者
Nicholas C. Avery,Trevor J. Sims,Allen J. Bailey
出处
期刊:Methods in molecular biology [Springer Science+Business Media]
卷期号:: 103-121 被引量:105
标识
DOI:10.1007/978-1-59745-413-1_6
摘要

The primary functional role of collagen is as a supporting tissue and it is now established that the aggregated forms of the collagen monomers are stabilised to provide mechanical strength by a series of intermolecular cross-links. In order to understand the mechanical properties of collagen, it is necessary to identify and quantitatively determine the concentration of the cross-links during their changes with maturation, ageing and disease. These cross-links are formed by oxidative deamination of the ε-amino group of the single lysine or hydroxylysine in the amino and carboxy telopeptides of collagen by lysyl oxidase, the aldehyde formed reacting with a specific lysine or hydroxylysine in the triple helix. The divalent Schiff base and keto-amine bonds so formed link the molecules head to tail and spontaneously convert during maturation to trivalent cross-links, a histidine derivative and cyclic pyridinolines and pyrroles, respectively. These latter bonds are believed to be transverse inter-fibrillar cross-links, and are tissue rather than species specific. We describe the determination of these cross-links in detail. Elastin is also stabilised by cross-linking based on oxidative deamination of most of its lysine residues to yield tetravalent cross-links, desmosine and iso-desmosine, the determination of which is also described. A second cross-linking pathway occurs during ageing (and to a greater extent in diabetes mellitus) involving reaction with tissue glucose. The initial product glucitol-lysine can be determined as furosine and pyridosine, and determination of advanced glycation end-products believed to be cross-links, such as pentosidine, are also described.
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