Isemura M, Sato N, Yamaguchi Y, Aikawa J, Munakata H, Hayashi N, Yosizawa Z, Nakamura T, Kubota A, Arakawa M
J Biol Chem. 1987 Jun 25;262(18):8926-33.
A proteoglycan was isolated from the human placenta by procedures including affinity chromatography with fibronectin immobilized on agarose. The glycosaminoglycan chains were found to be composed of heparan sulfate (86%) and dermatan sulfate (14%). The average molecular weights were estimated to be 1.8 X 10(5) for heparan sulfate and 1.2 X 10(5) for dermatan sulfate. Mouse monoclonal antibodies HS42 and HS47 were prepared against the proteoglycan, and examination of the specificity of these antibodies indicated that they recognized the core protein portion. The binding specificity, as studied by the solid phase enzyme-linked immunoassay with monoclonal antibody HS47, indicated that the proteoglycan bound to solid phase fibronectin and to laminin, but not to collagen types I, II, and IV or gelatin. Competitive immunoassays suggested that the proteoglycan bound weakly to the liquid phase-soluble fibronectin. These studies also indicated that the core protein was involved in the interaction between the proteoglycan and solid phase fibronectin. The ubiquitous distribution of this proteoglycan in the human tissues was demonstrated by the immunohistochemical method and thus suggested its important role in the tissue organization and function.
通过包括用固定在琼脂糖上的纤连蛋白进行亲和层析在内的方法，从人胎盘中分离出一种蛋白聚糖。发现糖胺聚糖链由硫酸乙酰肝素（86%）和硫酸皮肤素（14%）组成。硫酸乙酰肝素的平均分子量估计为1.8×10⁵，硫酸皮肤素的平均分子量估计为1.2×10⁵。制备了针对该蛋白聚糖的小鼠单克隆抗体HS42和HS47，对这些抗体特异性的检测表明它们识别核心蛋白部分。用单克隆抗体HS47通过固相酶联免疫测定法研究的结合特异性表明，该蛋白聚糖与固相纤连蛋白和层粘连蛋白结合，但不与I型、II型和IV型胶原蛋白或明胶结合。竞争性免疫测定表明该蛋白聚糖与液相可溶性纤连蛋白弱结合。这些研究还表明核心蛋白参与了蛋白聚糖与固相纤连蛋白之间的相互作用。通过免疫组织化学方法证明了这种蛋白聚糖在人体组织中的广泛分布，因此表明其在组织组织和功能中起重要作用。
