Park L S, Martin U, Garka K, Gliniak B, Di Santo J P, Muller W, Largaespada D A, Copeland N G, Jenkins N A, Farr A G, Ziegler S F, Morrissey P J, Paxton R, Sims J E
Department of Biochemistry, Immunex Corporation, Seattle, Washington 98101, USA.
J Exp Med. 2000 Sep 4;192(5):659-70. doi: 10.1084/jem.192.5.659.
The cellular receptor for murine thymic stromal lymphopoietin (TSLP) was detected in a variety of murine, but not human myelomonocytic cell lines by radioligand binding. cDNA clones encoding the receptor were isolated from a murine T helper cell cDNA library. TSLP receptor (TSLPR) is a member of the hematopoietin receptor family. Transfection of TSLPR cDNA resulted in only low affinity binding. Cotransfection of the interleukin 7 (IL-7)Ralpha chain cDNA resulted in conversion to high affinity binding. TSLP did not activate cells from IL-7Ralpha(-/)- mice, but did activate cells from gammac(-/)- mice. Thus, the functional TSLPR requires the IL-7Ralpha chain, but not the gammac chain for signaling.
通过放射性配体结合法在多种小鼠而非人骨髓单核细胞系中检测到了小鼠胸腺基质淋巴细胞生成素(TSLP)的细胞受体。从鼠辅助性T细胞cDNA文库中分离出了编码该受体的cDNA克隆。TSLP受体(TSLPR)是造血因子受体家族的一员。转染TSLPR cDNA仅产生低亲和力结合。共转染白细胞介素7(IL-7)Rα链cDNA会导致转变为高亲和力结合。TSLP不能激活来自IL-7Rα(-/-)小鼠的细胞,但能激活来自γc(-/-)小鼠的细胞。因此,功能性TSLPR进行信号传导需要IL-7Rα链,但不需要γc链。