T cell activation results in physical modification of the mouse CD8 beta chain.

T cell activation results in physical modification of the mouse CD8 beta chain.
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T 细胞激活导致小鼠 CD8 β 链的物理修饰。

DOI:
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发表时间:
1994
影响因子:
4.4
通讯作者:
R. Zamoyska
R. Zamoyska
中科院分区:
医学2区
文献类型:
--
作者:
L. Casabó;C. Mamalaki;D. Kioussis;R. Zamoyska

文献摘要

被引文献

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T淋巴细胞糖蛋白CD8是一类mhc限制性T细胞对Ag反应的重要组成部分。CD8在i类限制性T细胞表面以二硫键异二聚体和两种远亲多肽α和β的更高多聚体表达。在转染研究中以同型二聚体表达的CD8 α多肽,能够复制CD8的粘附和刺激特性,使CD8 β多肽的功能无法确定。在这里,我们证明了CD8 β多肽在T细胞成熟和激活过程中通过可逆地改变其唾液酸含量而发生物理变化。这些变化特异性地发生在CD8 β而不是- α上,表明CD8 β链的主要作用可能是调节,影响CD8复合物的物理结构,并提示一种控制受体/配体相互作用的新机制。
The T lymphocyte glycoprotein, CD8, is an essential component of the response of class I MHC-restricted T cells to Ag. CD8 is expressed on the surface of class I-restricted T cells as disulfide-bonded heterodimers and higher multimers of two distantly related polypeptides, alpha and beta. The CD8 alpha polypeptide, expressed in transfection studies as homodimers, is able to reproduce both the adhesive and stimulatory properties of CD8, leaving the function of the CD8 beta polypeptide unresolved. Herein we demonstrate that the CD8 beta polypeptide changes physically during T cell maturation and activation by reversibly altering its sialic acid content. These changes occur specifically on CD8 beta not -alpha, indicating that the primary role of the CD8 beta chain may be regulatory, influencing the physical structure of the CD8 complex, and suggesting a novel mechanism of controlling receptor/ligand interactions.