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Analysis of opticin binding to collagen fibrils identifies a single binding site in the gap region and a high specificity towards thin heterotypic fibrils containing collagens II, and XI or V/XI.
bioRxiv - Biochemistry Pub Date : 2020-06-02 , DOI: 10.1101/2020.06.02.129403
Uwe Hansen , David F. Holmes , Peter Bruckner , Paul N. Bishop

Opticin is a class III member of the extracellular matrix small leucine-rich repeat protein/proteoglycan (SLRP) family found in vitreous humour and cartilage. It was first identified associated with the surface of vitreous collagen fibrils and several other SLRPs are also known to bind collagen fibrils and it some cases alter fibril morphology. The purpose of this study was to investigate the binding of opticin to the collagen II-containing fibrils found in vitreous and cartilage. Electron microscopic studies using gold labelling demonstrated that opticin binds vitreous and thin cartilage collagen fibrils specifically at a single site in the gap region of the collagen D-period corresponding to the e2 stain band; this is the first demonstration of the binding site of a class III SLRP on collagen fibrils. Opticin did not bind thick cartilage collagen fibrils from cartilage or tactoids formed in vitro from collagen II, but shows high specificity for thin, heterotypic collagen fibrils containing collagens II, and XI or V/XI. Vitreous collagen fibrils from opticin null and wild-type mice were compared and no difference in fibril morphology or diameter was observed. Similarly, in vitro fibrillogenesis experiments showed that opticin did not affect fibril formation. We propose that when opticin is bound to collagen fibrils, rather than influencing their morphology it instead hinders the binding of other molecules to the fibril surfaces and/or act as an intermediary bridge linking the collagen fibrils to other non-collagenous molecules.

中文翻译:

对视蛋白与胶原原纤维结合的分析鉴定了在间隙区域中的单个结合位点,并且对含有胶原II和XI或V / XI的稀异型原纤维具有高特异性。

Opticin是在玻璃体液和软骨中发现的富含亮氨酸的小重复蛋白/蛋白聚糖(SLRP)家族的细胞外基质的III类成员。它首先被鉴定为与玻璃状胶原原纤维的表面有关,并且还已知其他几种SLRP结合胶原原纤维,并且在某些情况下会改变原纤维的形态。这项研究的目的是研究视黄蛋白与在玻璃体和软骨中发现的含胶原II的原纤维的结合。使用金标记的电子显微镜研究表明,视黄蛋白在胶原蛋白D周期与e2染色带相对应的间隙区域中的单个位置上特异性结合玻璃体和软骨软骨原纤维。这是第III类SLRP在胶原纤维上的结合位点的首次证明。Opticin不会结合由胶原II体外形成的软骨或触觉产生的厚软骨胶原原纤维,但对含有胶原II和XI或V / XI的稀薄的异型胶原原纤维具有高特异性。比较了来自视黄素无效小鼠和野生型小鼠的玻璃体胶原原纤维,未观察到原纤维形态或直径的差异。同样,体外原纤维形成实验表明,视黄蛋白不影响原纤维形成。我们提出当视蛋白与胶原原纤维结合时,而不是影响其形态,而是阻碍其他分子与原纤维表面的结合和/或充当将胶原原纤维与其他非胶原分子连接的中间桥。含有胶原蛋白II和XI或V / XI的异型胶原蛋白原纤维。比较了来自视黄素无效小鼠和野生型小鼠的玻璃体胶原原纤维,未观察到原纤维形态或直径的差异。同样,体外原纤维形成实验表明,视黄蛋白不影响原纤维形成。我们提出当视蛋白与胶原原纤维结合时,而不是影响其形态,而是阻碍其他分子与原纤维表面的结合和/或充当将胶原原纤维与其他非胶原分子连接的中间桥。含有胶原蛋白II和XI或V / XI的异型胶原蛋白原纤维。比较了来自视黄素无效小鼠和野生型小鼠的玻璃体胶原原纤维,未观察到原纤维形态或直径的差异。同样,体外原纤维形成实验表明,视黄蛋白不影响原纤维形成。我们提出当视蛋白与胶原原纤维结合时,而不是影响其形态,而是阻碍其他分子与原纤维表面的结合和/或充当将胶原原纤维与其他非胶原分子连接的中间桥。体外原纤维形成实验表明,视黄蛋白不影响原纤维形成。我们提出当视蛋白与胶原原纤维结合时,而不是影响其形态,而是阻碍其他分子与原纤维表面的结合和/或充当将胶原原纤维与其他非胶原分子连接的中间桥。体外原纤维形成实验表明,视黄蛋白不影响原纤维形成。我们提出当视蛋白与胶原原纤维结合时,而不是影响其形态,而是阻碍其他分子与原纤维表面的结合和/或充当将胶原原纤维与其他非胶原分子连接的中间桥。
更新日期:2020-06-02
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