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胸腺和外周血T细胞Ly-2/3抗原的比较。

Comparison of thymic and peripheral T cell Ly-2/3 antigens.

作者信息

Walker I D, Murray B J, Hogarth P M, Kelso A, McKenzie I F

出版信息

Eur J Immunol. 1984 Oct;14(10):906-10. doi: 10.1002/eji.1830141009.

Abstract

Major structural differences occur between the thymic and peripheral T cell forms of the Ly-2/3 antigen. Thymus Ly-2/3 consists of similar amounts of two types of disulfide-linked heterodimer, alpha beta and alpha' beta (Mr alpha = 38000, Mr alpha' = 35000, Mr beta = 30000). In contrast material from peripheral T cells consists almost exclusively of alpha beta dimers. The alpha chains of thymus and peripheral T cells differ also in isoelectric point with the thymic alpha chain being the more acidic. Based on peptide mapping experiments the alpha and alpha' chains of thymus are likely to be alternatively modified forms of the same polypeptide backbone. Individual T cell clones or T cell tumors propagated in vitro exhibit either a typical thymus or a typical peripheral T cell Ly-2/3 polypeptide pattern indicating that the synthesis of both alpha and alpha' chains can occur in the same cell. The heterogeneity of thymic Ly-2/3 can be considerably reduced by removal of sialic acid residues, and after desialylation the alpha chains of thymus and a cloned cytotoxic T lymphocyte (CTL) line cannot be electrophoretically distinguished. If Ly-2 structures affected the antigen specificity of CTL, a different structural variant would be expected in individual clones. The electrophoretic identity of desialylated thymus and CTL alpha chains suggests that Ly-2 does not exhibit clonal variation in polypeptide structure and, therefore, cannot contribute to antigen specificity.

摘要

Ly-2/3抗原的胸腺T细胞形式和外周T细胞形式之间存在主要的结构差异。胸腺Ly-2/3由两种通过二硫键连接的异二聚体(αβ和α'β)组成,含量相似(α链分子量为38000,α'链分子量为35000,β链分子量为30000)。相比之下,外周T细胞的物质几乎完全由αβ二聚体组成。胸腺T细胞和外周T细胞的α链在等电点上也有所不同,胸腺α链酸性更强。基于肽图谱实验,胸腺的α链和α'链可能是同一多肽骨架的不同修饰形式。在体外培养的单个T细胞克隆或T细胞肿瘤表现出典型的胸腺或典型的外周T细胞Ly-2/3多肽模式,这表明α链和α'链的合成可以在同一细胞中发生。去除唾液酸残基后,胸腺Ly-2/3的异质性可大大降低,去唾液酸化后,胸腺的α链和克隆的细胞毒性T淋巴细胞(CTL)系的α链在电泳上无法区分。如果Ly-2结构影响CTL的抗原特异性,那么在单个克隆中预期会有不同的结构变体。去唾液酸化的胸腺和CTLα链的电泳一致性表明,Ly-2在多肽结构上不表现出克隆变异,因此不能对抗原特异性起作用。

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