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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
2004-4-29
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pubmed:abstractText |
We examined the ability of blood group A-active glycoconjugates to act as receptors for Escherichia coli heat-labile type I enterotoxin (LT-I) in HT-29 cells. These cells contained ~4 times more specific binding sites for LT-I than for cholera toxin (CT). Binding of LT-I could not be blocked by the B subunit of CT (CT-B), indicating the existence of LT-I receptors in addition to the glycosphingolipid GM1. LT-I was able to increase levels of cyclic adenosine monophosphate (AMP), even in the presence of CT-B. Helix pomatia and anti-blood group A antibody caused a dose-dependent inhibition of binding of LT-I to cells and production of cyclic AMP. LT-I recognized several complex blood group A-active glycosphingolipids from cells, and this interaction was also interfered with by H. pomatia. Treatment of cells with D,L-threo-1-phenyl-2-hexadecanoylamino-3-morpholino-1-propanol diminished surface expression of blood group A-active glycosphingolipids and binding of LT-I to non-GM1 receptors. These observations suggest that blood group A-active glycosphingolipids can function as alternative receptors for LT-I in HT-29 cells.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4-propionyloxy-4-phenyl-N-methylpipe...,
http://linkedlifedata.com/resource/pubmed/chemical/ABO Blood-Group System,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Enterotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosphingolipids,
http://linkedlifedata.com/resource/pubmed/chemical/Guanylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Meperidine,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Guanylate Cyclase-Coupled,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Peptide,
http://linkedlifedata.com/resource/pubmed/chemical/enterotoxin receptor,
http://linkedlifedata.com/resource/pubmed/chemical/heat-labile enterotoxin, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0022-1899
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
189
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1556-64
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:15116290-ABO Blood-Group System,
pubmed-meshheading:15116290-Bacterial Toxins,
pubmed-meshheading:15116290-Cyclic AMP,
pubmed-meshheading:15116290-Enterotoxins,
pubmed-meshheading:15116290-Escherichia coli,
pubmed-meshheading:15116290-Escherichia coli Proteins,
pubmed-meshheading:15116290-Glycosphingolipids,
pubmed-meshheading:15116290-Guanylate Cyclase,
pubmed-meshheading:15116290-HT29 Cells,
pubmed-meshheading:15116290-Humans,
pubmed-meshheading:15116290-Ligands,
pubmed-meshheading:15116290-Meperidine,
pubmed-meshheading:15116290-Receptors, Guanylate Cyclase-Coupled,
pubmed-meshheading:15116290-Receptors, Peptide,
pubmed-meshheading:15116290-Signal Transduction
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pubmed:year |
2004
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pubmed:articleTitle |
Ability of blood group A-active glycosphingolipids to act as Escherichia coli heat-labile enterotoxin receptors in HT-29 cells.
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pubmed:affiliation |
Departamento de Quimica Biológica, "Dr. Ranwel Caputto"-Centro de Investigaciones en Química Biológica de Córdoba, Facultad de Ciencias Químicas, Universidad Nacional de Córdoba, Córdoba, Argentina.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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