Acceleracted publication -: Decorin binds near the C terminus of type I collagen
Acceleracted publication -: Decorin binds near the C terminus of type I collagen
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DOI：
10.1074/jbc.c000278200
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发表时间：
2000-07-21
影响因子：
4.8
通讯作者：
Iozzo, RV
中科院分区：
文献类型：
--
作者：
Keene, DR;San Antonio, JD;Iozzo, RV
核心蛋白聚糖属于富含亮氨酸的小蛋白聚糖家族，其直接参与控制基质组织和细胞生长。遗传证据表明，核心蛋白聚糖是胶原基质正确组装所必需的。在这里，我们试图建立精确的结合位点的核心蛋白聚糖对I型胶原蛋白。使用旋转阴影电子显微镜和光亲和标记，我们将核心蛋白聚糖蛋白核心的结合位点映射到I型胶原C末端附近的狭窄区域。该区域位于溴化氰肽片段α 1（I）CB 6内，与C末端25 nm相似，位于与胶原纤维D-周期的c（1）带一致的区域。该位置非常接近胶原异源三聚体的主要分子间交联位点之一。因此，核心蛋白聚糖蛋白核心具有独特的结合特异性，可以潜在地调节胶原纤维的稳定性。
Decorin belongs to a family of small leucine-rich proteoglycans that are directly involved in the control of matrix organization and cell growth, Genetic evidence indicates that decorin is required for the proper assembly of collagenous matrices. Here, we sought to establish the precise binding site of decorin on type I collagen. Using rotary shadowing electron microscopy and photoaffinity labeling, we mapped the binding site of decorin protein core to a narrow region near the C terminus of type I collagen. This region is located within the cyanogen bromide peptide fragment alpha 1(I) CB6 and is similar to 25 nm from the C terminus, in a zone that coincides with the c(1) band of the collagen fibril D-period. This location is very close to one of the major intermolecular cross-linking sites of collagen heterotrimers. Thus, decorin protein core possesses a unique binding specificity that could potentially regulate collagen fibril stability.