Monoclonal Antibodies Against Two Epitopes in the Human α1(IX) Collagen Chain

Matrix (Stuttgart, Germany) Pub Date : 1993-03-01 DOI:10.1016/S0934-8832(11)80073-9

Matthew Warman , Tomoatsu Kimura , Yasuteru Muragaki , Patrizio Castagnola , Hironori Tamei , Kazushi Iwata , Bjorn R. Olsen

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引用次数: 11

Abstract

Type IX collagen is a component of cartilage and vitreous humor. Its structure and matrix localization suggest it may serve to mediate interactions between fibrillar collagen, proteoglycan and other matrix components. Consequently, abnormalities in type IX collagen may result in chondrodysplasia. In this paper we describe the preparation and use of two monoclonal antibodies which recognize peptide sequences within the human cartilage α1(IX) collagen chain. Antibody 23-5D1 is highly sensitive and highly specific. It permits the immunoblot detection of type IX collagen extracted from milligram amounts of normal and chondrodysplastic cartilage; it also identifies the “short” form of the α1(IX) chain in human vitreous humor. Antibody 37-10H7 is highly specific, but of low sensitivity. It was used to make the new observation that an N-linked oligosaccharide is present in the amino-terminal globular domain of the a1(IX) chain. We anticipate that these antibodies may be valuable tools in the study of human and other mammalian chondrodysplasias.

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抗人α1（IX）胶原链两个表位的单克隆抗体

IX型胶原是软骨和玻璃体的组成部分。其结构和基质定位表明，它可能介导原纤维胶原、蛋白聚糖和其他基质成分之间的相互作用。因此，IX型胶原的异常可能导致软骨发育不良。在本文中，我们描述了两种识别人软骨α1（IX）胶原链内肽序列的单克隆抗体的制备和使用。抗体23-5D1具有高度敏感性和高度特异性。它允许免疫印迹检测从毫克量的正常软骨和软骨发育不良软骨中提取的IX型胶原；它还鉴定了人类玻璃体中α1（IX）链的“短”形式。抗体37-10H7具有高度特异性，但敏感性较低。它被用来进行新的观察，即N-连接的寡糖存在于a1（IX）链的氨基末端球状结构域中。我们预计，这些抗体可能是研究人类和其他哺乳动物软骨发育不良的有价值的工具。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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Matrix (Stuttgart, Germany)

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