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以非成熟细胞表面糖蛋白形式表达的HLA - G2、- G3和- G4同种型可抑制自然杀伤细胞(NK)和抗原特异性细胞毒性T淋巴细胞(CTL)的细胞溶解作用。

HLA-G2, -G3, and -G4 isoforms expressed as nonmature cell surface glycoproteins inhibit NK and antigen-specific CTL cytolysis.

作者信息

Riteau B, Rouas-Freiss N, Menier C, Paul P, Dausset J, Carosella E D

机构信息

Service de Recherches en Hémato-Immunologie, Commissariat à l'Energie Atomique-Direction des Sciences du Vivant-Department de Recherche Médicale, Institut Universitaire d'Hématologie, Hôpital Saint Louis, and Fondation Jean Dausset, Paris, France.

出版信息

J Immunol. 2001 Apr 15;166(8):5018-26. doi: 10.4049/jimmunol.166.8.5018.

DOI:10.4049/jimmunol.166.8.5018
PMID:11290782
Abstract

HLA-G is a nonclassical MHC class I molecule that plays a major role in maternal-fetal tolerance. Four membrane-bound (HLA-G1 to -G4) and two soluble (HLA-G5, and -G6) proteins are generated by alternative splicing. Only HLA-G1 has been extensively studied in terms of both expression and function. We provide evidence here that HLA-G2, -G3, and -G4 truncated isoforms reach the cell surface of transfected cells, as endoglycosidase H-sensitive glycoproteins, after a 2-h chase period. Moreover, cytotoxicity experiments show that these transfected cells are protected from the lytic activity of both innate (NK cells) and acquired (CTL) effectors. These findings highlight the immunomodulatory role that HLA-G2, -G3, and -G4 proteins will assume during physiologic or pathologic processes in which HLA-G1 expression is altered.

摘要

HLA - G是一种非经典的MHC I类分子,在母胎耐受中起主要作用。通过可变剪接产生四种膜结合蛋白(HLA - G1至 - G4)和两种可溶性蛋白(HLA - G5和 - G6)。就表达和功能而言,只有HLA - G1得到了广泛研究。我们在此提供证据表明,HLA - G2、 - G3和 - G4截短异构体在2小时的追踪期后,作为对内切糖苷酶H敏感的糖蛋白到达转染细胞的细胞表面。此外,细胞毒性实验表明,这些转染细胞免受先天(自然杀伤细胞)和后天(细胞毒性T淋巴细胞)效应细胞的裂解活性影响。这些发现突出了HLA - G2、 - G3和 - G4蛋白在HLA - G1表达改变的生理或病理过程中将发挥的免疫调节作用。

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