人白细胞介素2受体β链（p70）。外周血单个核细胞上的直接鉴定、部分纯化及表达模式
The human interleukin 2 receptor beta chain (p70). Direct identification, partial purification, and patterns of expression on peripheral blood mononuclear cells.
作者信息
Sharon M, Siegel J P, Tosato G, Yodoi J, Gerrard T L, Leonard W J
机构信息
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, Bethesda, Maryland 20892.
出版信息
J Exp Med. 1988 Mar 1;167(3):1265-70. doi: 10.1084/jem.167.3.1265.
Abstract
IL-2 binds to high- and low-affinity receptors on activated T cells. The high-affinity receptor was hypothesized to consist of the noncovalent association between the alpha chain (IL-2-R-alpha, p55) and a beta chain (IL-2-R-beta, p70), whereas the low-affinity receptor consists of p55 without p70. We now directly identify p70 as a 65-77-kD glycoprotein doublet. Preparative quantities of the IL-2/p70 complex have been isolated. Further, we demonstrate that p70 is the principal IL-2 binding protein on both resting CD4+ and CD8+ T cells and that both p70 and p55 can be induced on normal B cells and monocytes.
摘要
白细胞介素-2（IL-2）与活化T细胞上的高亲和力和低亲和力受体结合。据推测，高亲和力受体由α链（IL-2-R-α，p55）和β链（IL-2-R-β，p70）之间的非共价结合组成，而低亲和力受体由不含p70的p55组成。我们现在直接鉴定出p70是一种65 - 77-kD的糖蛋白双峰。已分离出制备量的IL-2/p70复合物。此外，我们证明p70是静息CD4+和CD8+ T细胞上主要的IL-2结合蛋白，并且p70和p55均可在正常B细胞和单核细胞上被诱导产生。
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