BIOSYNTHESIS OF COLLAGEN AND OTHER MATRIX PROTEINS BY ARTICULAR-CARTILAGE IN EXPERIMENTAL OSTEOARTHROSIS
BIOSYNTHESIS OF COLLAGEN AND OTHER MATRIX PROTEINS BY ARTICULAR-CARTILAGE IN EXPERIMENTAL OSTEOARTHROSIS
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DOI：
10.1042/bj1880823
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发表时间：
1980-01-01
影响因子：
4.1
通讯作者：
MUIR, H
中科院分区：
文献类型：
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作者：
EYRE, DR;MCDEVITT, CA;MUIR, H
骨关节病是由一个既定的手术程序在一个膝关节诱导的狗。通过放射化学标记在体内寻找关节软骨在胶原蛋白和其他蛋白质的生物合成中的变化。在术后2、8和24周，实验关节的所有软骨表面均刺激胶原合成。用[3H]脯氨酸进行系统标记，结果表明：与未手术的膝关节软骨相比，实验软骨每干重的胶原沉积量更多。II型胶原是所有实验软骨样品中放射性标记的产物，其质量范围从未受损到明显纤颤。这是在狗或人类关节的骨关节软骨基质中化学检测到的唯一胶原蛋白。用[3H]赖氨酸标记犬关节，检测新合成软骨胶原中羟基赖氨酸的糖基化。在实验膝关节中，新胶原蛋白的糖基化程度低于对照组。化学分析结果显示，两组组织中总胶原蛋白的糖基化无显著差异。从标记有[3H]脯氨酸的对照软骨中，用4m氯化胍提取了一半以上的蛋白结合氚，而从实验软骨中提取的比例为1/4或更少。在结合条件下，在CsCl中密度梯度离心，提取的氚中有2/3在上部分离。在还原条件下，在十二烷基硫酸钠/聚丙烯酰胺凝胶电泳上，这大部分都是用单个蛋白质带进行的。该蛋白的身份尚不清楚，尽管它在二硫键裂解后的流动性与血清白蛋白相似。
Osteoarthrosis was induced in one knee joint of dogs by an established surgical procedure. Changes in the articular cartilage in the biosynthesis of collagen and other proteins were sought by radiochemical labeling in vivo. Collagen synthesis was stimulated in all cartilage surfaces of the experimental joints at 2, 8 and 24 wk after surgery. Systemic labeling with [3H]proline showed that over 10 .times. more collagen was deposited per dry weight of experimental cartilage compared to control cartilage in the unoperated knee. Type II collagen was the radiolabeled product in all samples of experimental cartilage ranging in quality from undamaged to overtly fibrillated. It was the only collagen detected chemically in the matrix of osteoarthrotic cartilage from dog or human joints. Hydroxylysine glycosylation was examined in the newly synthesized cartilage collagen by labeling dog joints in vivo with [3H]lysine. In experimental knees the new collagen was less glycosylated than in controls. No difference in glycosylation of the total collagen in the tissues was observed by chemical analysis. Over half the protein-bound tritium was extracted by 4 M guanidinium chloride from control cartilage labeled with [3H]proline, compared to 1/4 or less from experimental cartilage. Of the extracted tritium, 2/3 separated in the upper fraction on density-gradient centrifugation in CsCl under associative conditions. Much of this ran with a single protein band on sodium dodecyl sulfate/polyacrylamide-gel electrophoresis under reducing conditions. The identity of this protein was unknown, although it resembled serum albumin in mobility after disulfide bond cleavage.