High-affinity binding of 125I-labeled mouse interferon to a specific cell surface receptor. IV. Mouse gamma interferon and cholera toxin do not compete for the common receptor site of alpha / beta interferon.

Details

Serval ID
serval:BIB_E28AF4913271
Type
Article: article from journal or magazin.
Collection
Publications
Title
High-affinity binding of 125I-labeled mouse interferon to a specific cell surface receptor. IV. Mouse gamma interferon and cholera toxin do not compete for the common receptor site of alpha / beta interferon.
Journal
Virology
Author(s)
Aguet M., Belardelli F., Blanchard B., Marcucci F., Gresser I.
ISSN
0042-6822 (Print)
ISSN-L
0042-6822
Publication state
Published
Issued date
1982
Volume
117
Number
2
Pages
541-544
Language
english
Abstract
The initial step in interferon action consists of the binding to a specific high-affinity cell surface receptor. Mouse α and β interferon have been shown to share a common receptor. We now present evidence that mouse γ interferon does not compete for this receptor on mouse L 1210 and L 929 cells. Cholera toxin which binds specifically to the membrane monosialoganglioside GM1, and has been shown to inhibit interferon action, does not inhibit the specific binding of labeled mouse α/β interferon to L 1210 or L 929 cells. Conversely, mouse α/β interferon does not inhibit the specific binding of radioactive cholera toxin to L 929 cells. L 1210S cells which have a specific receptor for α/β interferon do not have a specific binding site for cholera toxin. We conclude from these studies that there is no evidence to indicate that cholera toxin and mouse α/β interferon share a common receptor.
Keywords
Animals, Cholera Toxin/metabolism, G(M1) Ganglioside/metabolism, Interferons/metabolism, L Cells (Cell Line)/metabolism, Mice, Receptors, Cell Surface/metabolism, Receptors, Interferon
Pubmed
Web of science
Create date
28/01/2008 11:36
Last modification date
20/08/2019 16:06
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