Epitopes of proteoglycans eliciting an anti-proteoglycan response in chronic immune synovitis.

Epitopes of proteoglycans eliciting an anti-proteoglycan response in chronic immune synovitis.
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蛋白多糖表位在慢性免疫滑膜炎中引发抗蛋白多糖反应。

DOI:
10.1073/pnas.84.3.832
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发表时间:
1987
影响因子:
11.1
通讯作者:
Goldberg,VM
Goldberg,VM
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Yoo,JU;Kresina,TF;Malemud,CJ;Goldberg,VM

文献摘要

被引文献

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本研究详细介绍了在实验性慢性IgG诱导的免疫性滑膜炎中对软骨蛋白多糖的免疫应答。在9只免疫性滑膜炎家兔中,观察到与纯化的兔蛋白多糖单体反应的抗体。IgG免疫但无病理学的非滑膜对照动物未显示抗体应答。利用一组对兔蛋白聚糖具有确定特异性的鼠单克隆抗体来表征免疫滑膜炎多克隆抗蛋白聚糖应答的表位特异性。一种鼠单克隆抗体6C 11在所有9只动物中抑制了多克隆抗血清与蛋白聚糖的结合,在6/9只家兔中具有显著(大于40%)抑制作用。进一步的抑制研究,利用DEAE-纤维素分解的蛋白多糖胰蛋白酶肽显示,在硫酸软骨素差的肽的多克隆抗体的蛋白多糖底物的结合的强抑制剂。特别是,含硫酸角质素的胰蛋白酶肽在单位重量基础上具有最大的抑制作用。这些结果表明,在慢性IgG诱导的免疫性滑膜炎,抗蛋白多糖抗体引起的特异性是异质性的,但相对较大的比例主要识别的蛋白多糖分子的一部分,含有核心蛋白和相关的硫酸角质素。
This study details the immune response to cartilage proteoglycan in experimental chronic IgG-induced immune synovitis. Antibodies reactive with purified rabbit proteoglycan monomer were observed in nine of nine rabbits with immune synovitis. IgG-immunized but nonsynovitic control animals with no pathology showed no antibody response. A panel of murine monoclonal antibodies with defined specificity towards rabbit proteoglycan were utilized to characterize the epitope specificity of the immune synovitis polyclonal anti-proteoglycan response. One murine monoclonal antibody, 6C11, inhibited the binding of the polyclonal antisera to proteoglycan in all nine animals with significant (greater than 40%) inhibition in six of nine rabbits. Further inhibition studies utilizing DEAE-cellulose-resolved proteoglycan tryptic peptides revealed that peptides poor in chondroitin sulfate were strong inhibitors of binding of the polyclonal antibodies to the proteoglycan substrate. In particular, keratan sulfate-containing tryptic peptides were most inhibitory on a per weight basis. These results indicate that, in chronic IgG-induced immune synovitis, anti-proteoglycan antibodies elicited are heterogeneous with regard to specificity, but a relatively large proportion predominantly recognized a portion of the proteoglycan molecule containing core protein and associated keratan sulfate.