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
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
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光学蛋白与胶原原纤维结合的分析确定了间隙区域中的单个结合位点，并且对含有胶原蛋白 II、XI 或 V/XI 的细异型原纤维具有高度特异性
DOI：
10.1101/2020.06.02.129403
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发表时间：
2020
期刊：
影响因子：
--
通讯作者：
Hansen U
中科院分区：
文献类型：
--
作者：
Hansen U
Opticin是细胞外基质富含亮氨酸的小重复蛋白/蛋白多糖(SLRP)家族的III类成员，存在于玻璃体和软骨中。它最初被发现与玻璃体胶原纤维表面有关，其他几个SLRP也已知与胶原纤维结合，有些情况下它会改变纤维的形态。本研究的目的是研究视蛋白与玻璃体和软骨中发现的含有II型胶原的纤维的结合。用金标记的电子显微镜研究表明，opticin与玻璃体和薄软骨胶原纤维特异性地结合在胶原D期缝隙区域中与e2染色带相对应的单一位置；这是首次证明III型SLRP与胶原纤维的结合位置。Opticin不能结合来自软骨的厚的软骨胶原纤维或由II型胶原形成的结缔组织，但对含有II型胶原蛋白和XI或V/XI的异型胶原纤维表现出高度的特异性。比较了视蛋白缺失和野生型小鼠的玻璃体胶原纤维，发现纤维形态和直径没有差异。同样，在玻璃体纤维形成实验中，视黄素并不影响纤维的形成。我们认为，当视蛋白与胶原纤维结合时，它不仅不会影响其形态，反而会阻碍其他分子与纤维表面的结合，和/或充当连接胶原纤维与其他非胶原分子的中间桥梁。
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 formedin vitrofrom 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 vitrofibrillogenesis 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.
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影响因子：
4.8
作者：
K. Meek;J. A. Chapman;R. Hardcastle
通讯作者：
R. Hardcastle
影响因子：
3.9
作者：
Eyre, DR;Wu, JJ;Weis, MA
通讯作者：
Weis, MA
影响因子：
4.4
作者：
Bishop, PN;Holmes, DF;Bos, KJ
通讯作者：
Bos, KJ
DOI：
10.1016/s0021-9258(18)98361-4
发表时间：
1993-05
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Richard Mayne;R. G. Brewton;P. M. Mayne;John Baker
通讯作者：
Richard Mayne;R. G. Brewton;P. M. Mayne;John Baker
影响因子：
4.8
作者：
Le Goff, MM;Hindson, VJ;Bishop, PN
通讯作者：
Bishop, PN