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首页> 外文期刊>Cytokine >Molecular cloning of the guinea-pig IL-5 receptor alpha and beta subunits and reconstitution of a high affinity receptor.
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Molecular cloning of the guinea-pig IL-5 receptor alpha and beta subunits and reconstitution of a high affinity receptor.

机译：豚鼠IL-5受体α和β亚基的分子克隆和高亲和力受体的重构。

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摘要

The functional IL-5 receptor is a heteromeric complex consisting of an alpha and beta subunit. The cloning, sequencing and expression of guinea-pig IL-5Ralpha and beta subunits is described. The guinea-pig IL-5Ralpha subunit cDNA encodes a protein of M(r)47 kDa, which is 72 and 66% homologous to the human and murine orthologs, respectively. Three guinea-pig IL-5Rbeta subunit cDNA clones were isolated, which differ in the N-terminus and are 56-64% homologous to the human and murine IL-5Rbeta subunits. Expressing human IL-5Ralphabeta and guinea-pig IL-5Ralphabeta(1)in the baculovirus-insect cell system resulted in recombinant receptors which bound hIL-5 with high affinity (K(d)=0.19 and 0.11 nM, respectively). Expressing just gpIL-5Ralpha was not sufficient to demonstrate binding. This contrasts with the human receptor, where hIL-5Ralpha alone can bind hIL-5 with high affinity. gpIL-5Ralphabeta(1)bound both hIL-5 and mIL-5 with comparable affinity (K(i)=0.10 and 0.06 nM), similar to that seen with hIL-5Ralphabeta. Thus, both the heteromeric hIL-5R and gpIL-5Ralphabeta(1)can bind multiple IL-5 orthologs with high affinity whereas the murine IL-5R is selective for the murine ligand. Copyright 2000 Academic Press.
机译：功能性IL-5受体是由α和β亚基组成的异聚复合物。描述了豚鼠IL-5Ralpha和β亚基的克隆，测序和表达。豚鼠IL-5Ralpha亚基cDNA编码一种M（r）47 kDa的蛋白质，该蛋白质分别与人和鼠的直系同源物同源72％和66％。分离了三个豚鼠IL-5Rbeta亚基cDNA克隆，它们在N末端不同，与人和鼠IL-5Rbeta亚基具有56-64％的同源性。在杆状病毒-昆虫细胞系统中表达人IL-5Ralphabeta和豚鼠IL-5Ralphabeta（1）导致重组受体以高亲和力结合hIL-5（分别为K（d）= 0.19和0.11 nM）。仅表达gpIL-5Ralpha不足以证明结合。这与人类受体形成对比，人类受体单独使用hIL-5Ralpha可以高亲和力结合hIL-5。 gpIL-5Ralphabeta（1）以相当的亲和力（K（i）= 0.10和0.06 nM）结合hIL-5和mIL-5，与hIL-5Ralphabeta相似。因此，异源hIL-5R和gpIL-5Ralphabeta（1）都可以高亲和力结合多个IL-5直系同源物，而鼠IL-5R对鼠配体具有选择性。版权所有2000学术出版社。

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