MAPPING BY MONOCLONAL-ANTIBODY DETECTION OF GLYCOSAMINOGLYCANS IN CONNECTIVE TISSUES
MAPPING BY MONOCLONAL-ANTIBODY DETECTION OF GLYCOSAMINOGLYCANS IN CONNECTIVE TISSUES
复制标题
DOI：
10.1038/307650a0
复制
发表时间：
1984-01-01
期刊：
影响因子：
64.8
通讯作者：
BAKER, JR
中科院分区：
文献类型：
--
作者：
COUCHMAN, JR;CATERSON, B;BAKER, JR
硫酸软骨素蛋白聚糖是广泛存在的结缔组织成分1 - 4，软骨和其他蛋白聚糖的化学分析表明，分子形态涉及糖链硫酸化的程度和位置5，6。这反过来可能会影响糖胺聚糖（GAG）的特性，特别是与其他细胞外基质组分的自缔合和相互作用6，7。与来自不同结缔组织类型的特定分子（如胶原蛋白8、9及其相关糖蛋白10、11）的相互作用可能受到硫酸基团赋予的GAG分子上的特定电荷组织的影响。到目前为止，还不可能鉴定和绘制组织中不同硫酸化的软骨素，但我们现在已经提出了三种单克隆抗体，它们特异性识别未硫酸化、4-硫酸化和6-硫酸化的软骨素和硫酸皮肤素。这为研究硫酸软骨素蛋白多糖的体内分布提供了新的机会。我们证明硫酸软骨素具有显着的结缔组织特异性，并进一步提供证据表明某些蛋白聚糖可能主要仅携带一种类型的硫酸软骨素链。
Chondroitin sulphate proteoglycans are widespread connective tissue components1–4and chemical analysis of cartilage and other proteoglycans has demonstrated molecular speciation involving the degree and position of sulphation of the carbohydrate chains5,6. This may, in turn, affect the properties of the glycpsaminoglycan (GAG), particularly with respect to self-association and interactions with other extracellular matrix components6,7. Interactions with specific molecules from different connective tissue types, such as the collagens8,9and their associated glycoproteins10,11, could be favoured by particular charge organizations on the GAG molecule endowed by the sulphate groups. So far, it has not been possible to identify and map chondroitins of differing sulphation in tissues, but we have now raised three monoclonal antibodies which specifically recognize unsulphated, 4-sulphated and 6-sulphated chondroitin and dermatan sulphate. These provide novel opportunities to study thein vivodistribution of chondroitin sulphate proteoglycans. We demonstrate that chondroitin sulphates exhibit remarkable connective tissue specificity and furthermore provide evidence that some proteoglycans may predominantly carry only one type of chondroitin sulphate chain.