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人类中α-半乳糖基表位的异常表达。自身免疫过程的触发因素?

Abnormal expression of alpha-galactosyl epitopes in man. A trigger for autoimmune processes?

作者信息

Galili U

机构信息

MacMillan-Cargill Hematology Research Laboratory, Cancer Research Institute, San Francisco, California.

出版信息

Lancet. 1989 Aug 12;2(8659):358-61. doi: 10.1016/s0140-6736(89)90539-4.

Abstract

1% of circulating IgG in man is anti-Gal antibody, which interacts specifically with the carbohydrate structure Gal alpha 1----3Gal beta 1----4GlcNAc-R on mammalian glycoconjugates (described throughout as the alpha-galactosyl epitope). This epitope is abundant on cell surface glycoconjugates of non-primate mammals, prosimians, and New World monkeys. It is not found on cells of Old World monkeys, apes, and man because of diminished alpha 1----3 galactosyltransferase enzyme activity. However, the alpha 1----3 galactosyltransferase gene seems to be present within the human genome. A mechanism that increases alpha 1----3 galactosyltransferase activity in human cells could trigger an autoimmune process mediated by anti-Gal binding to the newly synthesised alpha-galactosyl epitopes.

摘要

人类循环免疫球蛋白G(IgG)的1%是抗半乳糖抗体,它能与哺乳动物糖缀合物上的碳水化合物结构Galα1----3Galβ1----4GlcNAc-R(以下简称α-半乳糖基表位)发生特异性相互作用。这种表位在非灵长类哺乳动物、原猴亚目动物和新大陆猴的细胞表面糖缀合物中含量丰富。由于α1----3半乳糖基转移酶活性降低,在旧大陆猴、猿和人类的细胞中未发现该表位。然而,α1----3半乳糖基转移酶基因似乎存在于人类基因组中。一种能提高人类细胞中α1----3半乳糖基转移酶活性的机制,可能会引发由抗半乳糖抗体与新合成的α-半乳糖基表位结合介导的自身免疫过程。

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