Type III collagen can be present on banded collagen fibrils regardless of fibril diameter.
Type III collagen can be present on banded collagen fibrils regardless of fibril diameter.
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DOI：
10.1083/jcb.105.5.2393
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发表时间：
1987-11
期刊：
影响因子：
--
通讯作者：
Burgeson RE
中科院分区：
文献类型：
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作者：
Keene DR;Sakai LY;Bächinger HP;Burgeson RE
识别 III 型胶原蛋白三螺旋内表位的单克隆抗体已用于检查该胶原蛋白类型在人类皮肤、角膜、羊膜、主动脉和肌腱中的分布。这些组织的超微结构检查表明抗体与皮肤、羊膜、主动脉和肌腱中的胶原纤维结合，无论纤维的直径如何。抗体分布不随供体年龄、活检部位或检查组织区域的变化而变化。相比之下，应用于成人角膜的抗体定位于孤立的原纤维，这些原纤维随机出现在整个基质中。这些研究表明，在去除氨基和羧基前肽后，III 型胶原蛋白仍然与胶原纤维相关，并表明皮肤、肌腱和羊膜（以及可能含有 I 型和 III 型胶原蛋白的许多其他组织）的原纤维至少是 I 型和 III 型胶原蛋白的共聚物。
Monoclonal antibodies that recognize an epitope within the triple helix of type III collagen have been used to examine the distribution of that collagen type in human skin, cornea, amnion, aorta, and tendon. Ultrastructural examination of those tissues indicates antibody binding to collagen fibrils in skin, amnion, aorta, and tendon regardless of the diameter of the fibril. The antibody distribution is unchanged with donor age, site of biopsy, or region of tissue examined. In contrast, antibody applied to adult human cornea localizes to isolated fibrils, which appear randomly throughout the matrix. These studies indicate that type III collagen remains associated with collagen fibrils after removal of the amino and carboxyl propeptides, and suggests that fibrils of skin, tendon, and amnion (and presumably many other tissues that contain both types I and III collagens) are copolymers of at least types I and III collagens.