Intrinsic ligand binding properties of the human and bovine alpha-interferon receptors.
The Type I interferon receptor (IFN-alpha R) interacts with all IFN-alpha s, IFN-beta and IFN-omega, and seems to be a multisubunit receptor. To investigate the role of a cloned receptor subunit (IFN-alpha R1), we have examined the intrinsic ligand binding properties of the bovine and human IFN-alpha R1 polypeptides expressed in Xenopus laevis oocytes. Albeit with different efficiencies, Xenopus oocytes expressing either the human or bovine IFN-alpha R1 polypeptide exhibit significant binding and formation of crosslinked complexes with human IFN-alpha A and IFN-alpha B. Thus, the IFN-alpha R1 polypeptide most likely plays a direct role in ligand binding.
Lim
J K
JK
Department of Molecular Genetics & Microbiology, UDMNJ-Robert Wood Johnson Medical School, Piscataway 08854.
Xiong
J
J
Carrasco
N
N
Langer
J A
JA
D000818:Animals; D002417:Cattle; D006801:Humans; D066298:In Vitro Techniques; D016898:Interferon-alpha / Q000378:metabolism*; D008024:Ligands; D009865:Oocytes; D011940:Receptor Aggregation; D053633:Receptor, Interferon alpha-beta; D017471:Receptors, Interferon / Q000378:metabolism*; D011994:Recombinant Proteins; D014982:Xenopus laevis
D016898:Interferon-alpha; D008024:Ligands; D017471:Receptors, Interferon; D011994:Recombinant Proteins; D053633:Receptor, Interferon alpha-beta