A NOVEL PROTEOGLYCAN SYNTHESIZED AND SECRETED BY CHONDROCYTES OF THE SUPERFICIAL ZONE OF ARTICULAR-CARTILAGE
A NOVEL PROTEOGLYCAN SYNTHESIZED AND SECRETED BY CHONDROCYTES OF THE SUPERFICIAL ZONE OF ARTICULAR-CARTILAGE
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DOI：
10.1006/abbi.1994.1219
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发表时间：
1994-05-15
影响因子：
3.9
通讯作者：
KUETTNER, KE
中科院分区：
文献类型：
--
作者：
SCHUMACHER, BL;BLOCK, JA;KUETTNER, KE
从牛关节软骨浅层薄片中鉴定出一种新的蛋白多糖(PG)。这种PG是由该区域的软骨细胞选择性地合成和分泌的，但在同一组织中更深层的切片的培养液中尚未发现这种PG。如果有的话，这种PG几乎没有掺入到细胞外基质中。经等量氯化铯密度梯度超速离心、DEAE Sephacel离子交换层析和SepharoseCL-2B凝胶过滤层析，得到部分纯化的PG。它通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳法迁移，表观分子量约为345 kDa。该分子可被木瓜酶、胰酶或链霉蛋白酶降解；然而，在4摄氏度下进行的有限胃酶处理只能将其分子量降至约315 kDa。该分子被硫酸角蛋白和硫酸软骨素取代，这两种物质通过有限的胃酶处理可以很大程度上去除。此外，这种PG，或非常类似的分子，已经在滑液中被证明。这种新型的PG可以作为关节软骨浅层软骨细胞的功能代谢标记物。(C)1994年学术出版社。
A novel proteoglycan (PG) has been identified in culture medium from thin slices of the superficial zone of bovine articular cartilage. This PG is synthesized and secreted selectively by chondrocytes of this zone but has not been demonstrated in culture medium from slices deeper in the same tissue. There is little, if any, incorporation of this PG into the extracellular matrix. The PG has been partially purified by isopycnic CsCl density gradient ultracentrifugation, ion-exchange chromatography on DEAE Sephacel, and gel filtration chromatography on Sepharose CL-2B. It migrates by sodium dodecyl sulfate-polyacrylamide gel electrophoresis with an apparent molecular weight of approximately 345 kDa. The molecule is degraded by papain, trypsin, or pronase; however, limited pepsin treatment performed at 4 degrees C only decreases its molecular weight to approximately 315 kDa. The molecule is substituted with keratan sulfate and chondroitin sulfate, which are largely removed by limited pepsin treatment. In addition, this PG, or a very similar molecule, has been demonstrated in synovial fluid. This novel PG may serve as a functional metabolic marker for chondrocytes of the superficial zone of articular cartilage. (C) 1994 Academic Press, Inc.