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PMID: 1060063 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Mobility of cholera toxin receptors on rat lymphocyte membranes.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 72 ·No. 10 ·1975-10-00 ·Pages 3844-8

Craig SW, Cuatrecasas P

Abstract

Fluorescein-labeled cholera toxin binds detectably to 40-60% of rat mesenteric lymph node cells and induces a temperature-dependent redistribution (patch and cap formation) of cell surface toxin receptors. The redistribution is inhibited by several "metabolic," "microtubule," and "microfilament" inhibitors, by concanavalin A, and by anticholera toxin IgG. Various studies indicate that cholera toxin is at least bivalent, and that this property may be related to both the induction of receptor redistribution and to the activation of adenylate cyclase. Membrane components which are probably identical to the sialo-glycolipid, GM1 ganglioside, appear to be mobile in the plane of the membrane. The possible role of toxin multivalency and receptor mobility in the mechanism of toxin action is considered.

MeSH Terms
Adenylyl Cyclases/metabolism Animals Antigen-Antibody Reactions Binding Sites Binding, Competitive Cell Membrane/drug effects,metabolism,ultrastructure Enterotoxins/metabolism,pharmacology Gangliosides Lymphocytes/drug effects,metabolism,ultrastructure Microscopy, Fluorescence Protein Binding Rats Receptors, Drug Sepharose Vibrio cholerae/immunology
Chemicals
Enterotoxins Gangliosides Receptors, Drug Sepharose Adenylyl Cyclases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Craig S W
Cuatrecasas P
References (36)
36 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.72.10.3844
Published
1975-10-00
Pages
3844-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC433092
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.72.10.3844 PMC Full Text View journal details
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