Non-enzymatic glycation of type I collagen diminishes collagen-proteoglycan binding and weakens cell adhesion.
Non-enzymatic glycation of type I collagen diminishes collagen-proteoglycan binding and weakens cell adhesion.
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DOI：
10.1002/jcb.21735
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发表时间：
2008-08-01
影响因子：
4
通讯作者：
Antonio, James D. San
中科院分区：
文献类型：
--
作者：
Reigle, Kristin L.;Di Lullo, Gloria;Turner, Kevin R.;Last, Jerold A.;Chervoneva, Inna;Birk, David E.;Funderburgh, James L.;Elrod, Elizabeth;Germann, Markus W.;Surber, Charles;Sanderson, Ralph D.;Antonio, James D. San
I型胶原蛋白的非酶糖化发生在衰老和糖尿病中，并且可能影响胶原蛋白溶解度、电荷、聚合和分子间相互作用。蛋白聚糖1（PGs）结合I型胶原，并被提议调节原纤维组装、功能和细胞-胶原相互作用。此外，在胶原原纤维上，硫酸角质素（KS）PG结合区与优选的胶原糖化位点重叠。因此，我们研究了通过简单糖基化修饰的胶原蛋白对PG-胶原蛋白相互作用的影响。通过亲和共电泳（ACE），我们发现肝素和KSPGs对糖化胶原蛋白的亲和力降低，但对正常胶原蛋白的亲和力不降低，而硫酸皮肤素（DS）PG核心蛋白聚糖和双糖链聚糖与两者的结合相似，肝素对正常胶原蛋白的亲和力随pH值的增加而降低。圆二色性（CD）光谱显示正常和糖化胶原蛋白呈现三螺旋构象，但是肝素的加入引起沉淀和三螺旋含量的降低--这种作用在糖化胶原蛋白中更为显著。分光光度测定显示糖化胶原蛋白聚合较慢。然而，超微结构分析表明，原纤维组装从正常和糖化胶原蛋白表现出正常的周期性，具有相似的结构和可比的直径分布。表达细胞表面硫酸乙酰肝素PG syndecan-1的B细胞与正常胶原蛋白粘附良好，但不与糖化胶原蛋白粘附，在糖化胶原蛋白上内皮细胞迁移延迟。我们推测，糖基化减少了I型胶原和PG之间的静电相互作用，并可能干扰核心蛋白-胶原协会KSPGs，但不是DSPGs。因此，在体内，胶原蛋白糖化可能削弱PG-胶原蛋白相互作用，从而破坏基质完整性和细胞-胶原蛋白相互作用、粘附和迁移。
Non-enzymatic glycation of type I collagen occurs in aging and diabetes, and may affect collagen solubility, charge, polymerization, and intermolecular interactions. Proteoglycans1(PGs) bind type I collagen and are proposed to regulate fibril assembly, function, and cell-collagen interactions. Moreover, on the collagen fibril a keratan sulfate (KS) PG binding region overlaps with preferred collagen glycation sites. Thus, we examined the effect of collagen modified by simple glycation on PG-collagen interactions. By affinity coelectrophoresis (ACE), we found reduced affinities of heparin and KSPGs for glycated but not normal collagen, whereas the dermatan sulfate (DS)PGs decorin and biglycan bound similarly to both, and that the affinity of heparin for normal collagen decreased with increasing pH. Circular dichroism (CD) spectroscopy revealed normal and glycated collagens to assume triple helical conformations, but heparin addition caused precipitation and decreased triple helical content - effects that were more marked with glycated collagen. A spectrophotometric assay revealed slower polymerization of glycated collagen. However, ultrastructural analyses indicated that fibrils assembled from normal and glycated collagen exhibited normal periodicity, had similar structures and comparable diameter distributions. B-cells expressing the cell surface heparan sulfate PG syndecan-1 adhered well to normal but not glycated collagen, and endothelial cell migration was delayed on glycated collagen. We speculate that glycation diminishes the electrostatic interactions between type I collagen and PGs, and may interfere with core protein-collagen associations for KSPGs but not DSPGs. Therefore in vivo, collagen glycation may weaken PG-collagen interactions, thereby disrupting matrix integrity and cell-collagen interactions, adhesion, and migration.
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影响因子：
7.8
作者：
Chakravarti, S;Magnuson, T;Lass, JH;Jepsen, KJ;LaMantia, C;Carroll, H
通讯作者：
Carroll, H
影响因子：
8.2
作者：
Kuzuya, M;Satake, S;Iguchi, A
通讯作者：
Iguchi, A
影响因子：
4
作者：
GUITTON, JD;LEPAPE, A;MUH, JP
通讯作者：
MUH, JP
影响因子：
15.9
作者：
Echtermeyer, F;Streit, M;Goetinck, PF
通讯作者：
Goetinck, PF
DOI：
10.1016/0304-4165(81)90101-x
发表时间：
1981-01-01
期刊：
BIOCHIMICA ET BIOPHYSICA ACTA
影响因子：
--
作者：
ANDREASSEN, TT;SEYERHANSEN, K;BAILEY, AJ
通讯作者：
BAILEY, AJ