rdf:type |
|
lifeskim:mentions |
umls-concept:C0030685,
umls-concept:C0072034,
umls-concept:C0168405,
umls-concept:C0242275,
umls-concept:C0243125,
umls-concept:C0391871,
umls-concept:C0521119,
umls-concept:C0680255,
umls-concept:C0699900,
umls-concept:C1254042,
umls-concept:C1280500,
umls-concept:C1283071,
umls-concept:C1963578
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pubmed:issue |
40
|
pubmed:dateCreated |
1997-10-22
|
pubmed:abstractText |
The effect of vacuolating toxin (VacA) from Helicobacter pylori on endosomal and lysosomal functions was studied by following procathepsin D maturation and epidermal growth factor (EGF) degradation in HeLa cells exposed to the toxin. VacA inhibited the conversion of procathepsin D (53 kDa) into both the intermediate (47 kDa) and the mature (31 kDa) form. Nonprocessed cathepsin D was partly retained inside cells and partly secreted in the extracellular medium via the constitutive secretion pathway. Intracellular degradation of EGF was also inhibited by VacA with a similar dose-response curve. VacA did not alter endocytosis, cell surface recycling, and retrograde transport from plasma membrane to trans-Golgi network and endoplasmic reticulum, as estimated by using transferrin, diphtheria toxin, and ricin as tracers. Subcellular fractionation of intoxicated cells showed that procathepsin D and nondegraded EGF accumulate in lysosomes. Measurements of intracellular acidification with fluorescein isothiocyanate-dextran revealed a partial neutralization of the lumen of endosomes and lysosomes, sufficient to account for both mistargeting of procathepsin D outside the cell and the decreased activity of lysosomal proteases.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin D,
http://linkedlifedata.com/resource/pubmed/chemical/Diphtheria Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Ricin,
http://linkedlifedata.com/resource/pubmed/chemical/Transferrin,
http://linkedlifedata.com/resource/pubmed/chemical/VacA protein, Helicobacter pylori,
http://linkedlifedata.com/resource/pubmed/chemical/procathepsin D
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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
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
25022-8
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:9312109-Bacterial Proteins,
pubmed-meshheading:9312109-Bacterial Toxins,
pubmed-meshheading:9312109-Cathepsin D,
pubmed-meshheading:9312109-Cell Membrane,
pubmed-meshheading:9312109-Diphtheria Toxin,
pubmed-meshheading:9312109-Endocytosis,
pubmed-meshheading:9312109-Endoplasmic Reticulum,
pubmed-meshheading:9312109-Enzyme Precursors,
pubmed-meshheading:9312109-Epidermal Growth Factor,
pubmed-meshheading:9312109-Golgi Apparatus,
pubmed-meshheading:9312109-HeLa Cells,
pubmed-meshheading:9312109-Helicobacter pylori,
pubmed-meshheading:9312109-Humans,
pubmed-meshheading:9312109-Kinetics,
pubmed-meshheading:9312109-Lysosomes,
pubmed-meshheading:9312109-Protein Processing, Post-Translational,
pubmed-meshheading:9312109-Ricin,
pubmed-meshheading:9312109-Transferrin
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pubmed:year |
1997
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pubmed:articleTitle |
Effect of helicobacter pylori vacuolating toxin on maturation and extracellular release of procathepsin D and on epidermal growth factor degradation.
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pubmed:affiliation |
Centro CNR Biomembrane and Dipartimento di Scienze Biomediche, Universita' di Padova, Via G. Colombo 3, 35121 Padova, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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