Krajícková J, Poláková R, Smetana K, Vytásek R
Institute of Rheumatology, Praha, Czech Republic.
Folia Biol (Praha). 1995;41(1):41-51.
Proteoglycans from annulus fibrosus and nucleus pulposus of human intervertebral disc were investigated by electrophoresis in a composite agarose-polyacrylamide gel and immunohistochemically using various monoclonal antibodies against components of extracellular matrix. There were at least five different populations of proteoglycans in both annulus fibrosus and nucleus pulposus. Proteoglycans represented by individual electrophoretic bands differed from each other in hydrodynamic size but all of them contained epitopes present in keratan sulphate. Chondroitin sulphate could be detected in populations with molecular weight above 200,000 daltons. We could postulate that the cleavage of proteoglycan chains starts at the C-terminal end. This is supported by the finding that the globular region G2 on the protein core was detected in the same populations as keratan sulphate. We could confirm these results using tissue cultures of nucleus pulposus, inner and external part of annulus fibrosus. Of interest is the finding that there is de novo synthesis of globular domain G1 only in structures of intervertebral disc from a 16-year-old male and not in the tissue of a 69-year-old male. This might contribute to an explanation of decreased aggregation of proteoglycans during the aging process.
通过在复合琼脂糖 - 聚丙烯酰胺凝胶中进行电泳以及使用针对细胞外基质成分的各种单克隆抗体进行免疫组织化学分析，对人椎间盘纤维环和髓核中的蛋白聚糖进行了研究。纤维环和髓核中至少存在五种不同的蛋白聚糖群体。由各个电泳条带代表的蛋白聚糖在流体动力学大小上彼此不同，但它们都含有硫酸角质素中存在的表位。在分子量高于200,000道尔顿的群体中可检测到硫酸软骨素。我们可以推测蛋白聚糖链的切割从C末端开始。这一推测得到以下发现的支持：在与硫酸角质素相同的群体中检测到蛋白核心上的球状区域G2。我们使用髓核、纤维环内部和外部的组织培养物证实了这些结果。有趣的是，仅在一名16岁男性的椎间盘结构中发现了球状结构域G1的从头合成，而在一名69岁男性的组织中未发现。这可能有助于解释衰老过程中蛋白聚糖聚集减少的现象。
