Document Detail


Beyond glycoproteins as galectin counterreceptors: tumor-effector T cell growth control via ganglioside GM1 [corrected].
MedLine Citation:
PMID:  22524425     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Glycoprotein glycan chains, by virtue of structure, topology of presentation and connection to signal-inducing units, are functional galectin counterreceptors. As example, cross-linking of the α(5)β(1) integrin by galectin-1 on carcinoma cells leads to G(1) arrest or anoikis. Contact-dependent switching from proliferation to differentiation in cultured neuroblastoma cells (SK-N-MC) also utilizes galectin-1. Activity enhancement of a cell surface sialidase underlies the shift in glycan display to ganglioside GM1. Its pentasaccharide within microdomains becomes the target. Similarly, this recognition pair is upregulated upon T cell activation. Cross-linking of GM1 along with associated α(4)/α(5)β(1) integrins elicits Ca(2+)-influx via TRPC5 channels as the relevant response for T effector cell (T(eff)) suppression. Unlike T(eff) cells from wild-type mice, those from genetically altered mice lacking GM1 are not suppressed by galectin-1 or regulatory T cells. Similarly, in the context of GM1 deficiency in NOD mice, T(eff) cells are associated with resistance to regulatory T cell suppression, which is reversed by applied GM1. The broad array of glycosphingolipid structures suggests the possible existence of several novel counterreceptors targeted to endogenous lectins, with sulfatide-galectin-4 interplay within apical delivery serving as recent example.
Authors:
Robert W Ledeen; Gusheng Wu; Sabine André; David Bleich; Guillemette Huet; Herbert Kaltner; Jürgen Kopitz; Hans-Joachim Gabius
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Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  Annals of the New York Academy of Sciences     Volume:  1253     ISSN:  1749-6632     ISO Abbreviation:  Ann. N. Y. Acad. Sci.     Publication Date:  2012 Apr 
Date Detail:
Created Date:  2012-04-24     Completed Date:  2012-06-28     Revised Date:  2012-08-23    
Medline Journal Info:
Nlm Unique ID:  7506858     Medline TA:  Ann N Y Acad Sci     Country:  United States    
Other Details:
Languages:  eng     Pagination:  206-21     Citation Subset:  IM    
Copyright Information:
© 2012 New York Academy of Sciences.
Affiliation:
Department of Neurology and Neurosciences, New Jersey, Medical School-University of Medicine and Dentistry of New Jersey, Newark, USA. ledeenro@umdnj.edu
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MeSH Terms
Descriptor/Qualifier:
Animals
Anoikis / immunology
Cell Communication / immunology
G(M1) Ganglioside / chemistry,  immunology*
Galectins / chemistry,  immunology*
Glycoproteins / chemistry,  immunology
Humans
Indazoles
Mice
Models, Immunological
Morpholines
Neoplasms / immunology*,  pathology,  therapy*
Propionic Acids
Signal Transduction / immunology
T-Lymphocytes / immunology
Chemical
Reg. No./Substance:
0/Galectins; 0/Glycoproteins; 0/Indazoles; 0/Morpholines; 0/Propionic Acids; 130641-38-2/bindarit; 37758-47-7/G(M1) Ganglioside; 67467-83-8/amorolfine
Comments/Corrections
Erratum In:
Ann N Y Acad Sci. 2012 Jul;1258:191

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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