Connective tissue activation. XXV. Regulation of proteoglycan synthesis in human synovial cells.
Connective tissue activation. XXV. Regulation of proteoglycan synthesis in human synovial cells.
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结缔组织激活。
DOI：
10.1002/art.1780260411
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发表时间：
1983
影响因子：
--
通讯作者：
Bignall,MC
中科院分区：
文献类型：
--
作者：
Castor,CW;Roberts,DJ;Hossler,PA;Bignall,MC
在这项研究中，几乎所有的硫酸化糖胺聚糖（GAG）的合成和分泌的人滑膜细胞，正常和类风湿性关节炎，被检测到的单体大小的蛋白聚糖的形式。进行的酶水解研究证明硫酸皮肤素是蛋白聚糖中的主要GAG，具有较少量的硫酸软骨素4/6。暴露于β-木糖苷（用作假“核心蛋白”）导致GAG链形成显著增强，表明硫酸化碳水化合物链本身的合成不受速率限制。几种类型的结缔组织激活肽（CTAP）刺激蛋白聚糖的合成和分泌; CTAP-III对增量核心蛋白和糖胺聚糖的刺激幅度相似。由于链的合成是不限速的，它表明，刺激蛋白聚糖的形成所造成的CTAP肽可能主要是通过增加核心蛋白的形成调制。
In this study, virtually all sulfated glycosaminoglycan (GAG) synthesized and secreted by human synovial cells, both normal and rheumatoid, was detected in the form of proteoglycans of monomeric size. Enzyme hydrolysis studies that were performed demonstrated dermatan sulfate to be the dominant GAG in the proteoglycan, with lesser amounts of chondroitin 4/6 sulfate. Exposure to β‐xyloside, used as a false “core protein,” resulted in marked enhancement of GAG chain formation, suggesting that the synthesis of the sulfated carbohydrate chain itself was not rate limiting. Proteoglycan synthesis and secretion were stimulated by several types of connective tissue activating peptides (CTAP); CTAP‐III stimulation of incremental core protein and glycosaminoglycan was shown to be of a similar magnitude. Since chain synthesis was not rate limiting, it is suggested that stimulated proteoglycan formation caused by the CTAP peptides may be primarily modulated through increased formation of core protein.