rdf:type |
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lifeskim:mentions |
|
pubmed:issue |
40
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pubmed:dateCreated |
1997-10-22
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pubmed:abstractText |
Intoxication of mammalian cells with the vacuolating toxin (VacA) released by Helicobacter pylori causes the formation of large acidic vacuoles containing the vacuolar ATPase proton pump and Rab7, a late endosome marker. Here, we describe a novel subcellular fractionation procedure, and we show that nanomolar concentrations of VacA induce a clear redistribution of lysosomal membrane glycoproteins among endocytic compartments. This redistribution is an early event in the process of cellular intoxication by VacA and precedes the formation of macroscopic vacuoles. The absence of the cation independent mannose 6-P receptor and the presence of Rab7 and of lysosomal membrane proteins in the newly formed compartment suggest that the vacuolating toxin induces the accumulation of a post-endosomal hybrid compartment presenting both late endosomal and lysosomal features.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Biological Markers,
http://linkedlifedata.com/resource/pubmed/chemical/Cytotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proton-Translocating ATPases,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, IGF Type 2,
http://linkedlifedata.com/resource/pubmed/chemical/VacA protein, Helicobacter pylori,
http://linkedlifedata.com/resource/pubmed/chemical/Vacuolar Proton-Translocating...,
http://linkedlifedata.com/resource/pubmed/chemical/rab GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/rab7 protein
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
25339-44
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9312153-Animals,
pubmed-meshheading:9312153-Bacterial Proteins,
pubmed-meshheading:9312153-Biological Markers,
pubmed-meshheading:9312153-Cell Fractionation,
pubmed-meshheading:9312153-Cell Line,
pubmed-meshheading:9312153-Centrifugation, Density Gradient,
pubmed-meshheading:9312153-Cricetinae,
pubmed-meshheading:9312153-Cytotoxins,
pubmed-meshheading:9312153-Endosomes,
pubmed-meshheading:9312153-GTP-Binding Proteins,
pubmed-meshheading:9312153-Helicobacter pylori,
pubmed-meshheading:9312153-Kidney,
pubmed-meshheading:9312153-Lysosomes,
pubmed-meshheading:9312153-Membrane Glycoproteins,
pubmed-meshheading:9312153-Proton-Translocating ATPases,
pubmed-meshheading:9312153-Receptor, IGF Type 2,
pubmed-meshheading:9312153-Vacuolar Proton-Translocating ATPases,
pubmed-meshheading:9312153-Vacuoles,
pubmed-meshheading:9312153-rab GTP-Binding Proteins
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pubmed:year |
1997
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pubmed:articleTitle |
Vacuoles induced by Helicobacter pylori toxin contain both late endosomal and lysosomal markers.
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pubmed:affiliation |
Centro CNR Biomembrane and Dipartimento di Scienze Biomediche, Università di Padova, 35100 Padova, Italy. toxin@civ.bio.unipd.it
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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