NDLI: Expression and signaling specificity of the IFNAR chain of the type I interferon receptor complex.

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Expression and signaling specificity of the IFNAR chain of the type I interferon receptor complex.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Hollander, D. Mullersman, J. E. Murti, A. Garcia-martinez, V. Wang, C. Russell-harde, D. Basu, L. Betts, M. Pfeffer, L. M. Croze, E. Constantinescu, S. N.
Description	Author Affiliation: Constantinescu SN ( Department of Pathology (576 BMH), University of Tennessee Health Science Center, Memphis 38163, USA.);
Abstract	The IFNAR chain of the type I interferon (IFN) receptor (IFNIR) undergoes rapid ligand-dependent tyrosine phosphorylation and acts as a species-specific transducer for type I IFN action. Using the vaccinia/T7 expression system to amplify IFNAR expression, we found that human HeLa-S3 cells transiently express high levels of cell surface IFNAR chains (approximately 250,000 chains per cell). Metabolic labeling and immunoblot analysis of transfected HeLa cells show that the IFNAR chain is initially detected as 65-kDa and 98-kDa precursors, and then as the 130-kDa mature protein. Due to variation in N-glycosylation, the apparent molecular mass of the mature IFNAR chain varies from 105 to 135 kDa in different cells. IFNIR structure was characterized in various human cell lines by analyzing 125I-labeled IFN cross-linked complexes recognized by various antibodies against IFNIR subunits and JAK protein-tyrosine kinases. Precipitation of cross-linked material from Daudi cells with anti-IFNAR antibodies showed that IFNAR was present in a 240-kDa complex. Precipitation of cross-linked material from U937 cells with anti-TYK2 sera revealed a 240-kDa complex, which apparently did not contain IFNAR and was not present in IFN-resistant HEC1B cells. The tyrosine phosphorylation and down-regulation of the IFNAR chain were induced by type I IFN in several human cell lines of diverse origins but not in HEC1B cells. However, of type I IFNs, IFN-beta uniquely induced the tyrosine phosphorylation of a 105-kDa protein associated with the IFNAR chain in two lymphoblastoid cell lines (Daudi and U266), demonstrating the specificity of transmembrane signaling for IFN-beta and IFN-alpha through the IFNAR chain.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	92
Language	English
Publisher	National Academy of Sciences
Publisher Date	1995-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Interferon Type I Metabolism Receptors, Interferon Signal Transduction Animals Cells, Cultured Down-Regulation Glycosylation Janus Kinase 1 Mice Phosphorylation Protein-Tyrosine Kinases Proteins Receptor, Interferon Alpha-beta Genetics Recombinant Proteins TYK2 Kinase Tyrosine Vaccinia Virus Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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