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人淋巴毒素的大小异质性归因于O-连接糖基化。

Size heterogeneity of human lymphotoxin is due to O-linked glycosylation.

作者信息

Kofler G, Göttfried I, Benjamin D, Tschachler E

机构信息

Department of Dermatology I, University of Vienna Medical School, Austria.

出版信息

Lymphokine Cytokine Res. 1992 Feb;11(1):9-14.

PMID:1576249
Abstract

Lymphotoxin (LT), a cytokine with antiviral and antitumor activities, is produced by activated T- and B-lymphocytes. The molecular weight (MW) of this glycoprotein has been reported to be 24 and 25 kDa for the mature molecule and 18.6 kDa for the recombinant form. Here we report that various human T- and B-cell lines as well as freshly stimulated T and B cells release LT molecules of different sizes, ranging from 23 to 27 kDa by SDS polyacrylamide gele electrophoresis (PAGE) analysis. Although individual cell lines produce LT of characteristic size, no firm association between the different MW forms with either the B or the T cell lineage could be established. The size heterogeneity of LT is due to O-linked glycosylation since only the removal of both N- and O-linked sugar residues but not removal of N-linked sugar residues alone, reduces the size of all forms to around 18.6 kDa, which corresponds to the calculated MW of the recombinant form of human LT.

摘要

淋巴毒素(LT)是一种具有抗病毒和抗肿瘤活性的细胞因子,由活化的T淋巴细胞和B淋巴细胞产生。据报道,这种糖蛋白的成熟分子分子量(MW)为24和25 kDa,重组形式为18.6 kDa。在此我们报道,各种人类T细胞系和B细胞系以及新鲜刺激的T细胞和B细胞释放大小不同的LT分子,通过SDS聚丙烯酰胺凝胶电泳(PAGE)分析,其大小范围为23至27 kDa。尽管单个细胞系产生特征大小的LT,但不同分子量形式与B细胞系或T细胞系之间未发现明确关联。LT的大小异质性是由于O连接糖基化,因为只有同时去除N连接和O连接的糖残基,而不是仅去除N连接的糖残基,才能将所有形式的大小减小到约18.6 kDa,这与重组形式的人类LT的计算分子量相对应。

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