Reconstitution of the functional receptors for murine and human interleukin 5.

BETA (programming language) Alpha (finance)
DOI: 10.1084/jem.177.6.1523 Publication Date: 2004-06-24T07:56:10Z
ABSTRACT
The murine interleukin 5 receptor (mIL-5R) is composed of two distinct subunits, alpha and beta. subunit (mIL-5R alpha) specifically binds IL-5 with low affinity. beta beta) does not bind by itself, but forms the high-affinity mIL-5R alpha. has been revealed to be mIL-3R-like protein, AIC2B which shared receptors for IL-3 granulocyte/macrophage colony-stimulating factor. We demonstrated here reconstitution functional human on mouse IL-2-dependent cell line, CTLL-2. CTLL-2 was transfected cDNAs and/or AIC2B. Only transfectant expressing both expressed proliferated in response IL-5. Then hIL-5R KH97 (beta c), homologue Though c did contribute much binding affinity hIL-5R, only These results showed that indispensable signal transduction. further investigated function IL-5-specific transmitting signals. Mutant alpha, lacks its whole cytoplasmic domain, into IL-3-dependent FDC-P1 intrinsically. resulting respond IL-5, though IL-5R, indicating portion also some important role IL-5-mediated
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