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rdf:type |
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lifeskim:mentions |
umls-concept:C0004391,
umls-concept:C0006142,
umls-concept:C0006812,
umls-concept:C0007428,
umls-concept:C0162638,
umls-concept:C0332157,
umls-concept:C0585361,
umls-concept:C0596890,
umls-concept:C1314939,
umls-concept:C1332410,
umls-concept:C1521991,
umls-concept:C1707719
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pubmed:dateCreated |
2005-8-3
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pubmed:abstractText |
The details of molecular switching points between apoptosis and autophagy in tumor cells have still not been fully elucidated. This study focused on the role of cathepsin B and its substrate, BID as molecular links between apoptosis and autophagy in human breast cancer MCF-7 cells exposed to camptothecin. Apoptosis occurred rapidly with a peak in 60 min after drug administration, whereas autophagy developed at a much slower rate with continuous progression during 24 h of cell exposure to the drug. CPT induced very rapid activation of cathepsin B. Inhibition of cathepsins by E64d prevented CPT-induced BAX and BID aggregation on mitochondria and reduced significantly reduced apoptotic cell number. The above effects were accompanied by an increase in autophagosome formation, measured by expression of MAP I LC3. BID knock down resulted in strong suppression of CPT-induced apoptosis and a shift of cell death towards autophagy, manifesting with an increase of Beclin 1 and MAP I LC3 cellular content.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antineoplastic Agents, Phytogenic,
http://linkedlifedata.com/resource/pubmed/chemical/Apoptosis Regulatory Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/BAX protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/BECN1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/BH3 Interacting Domain Death...,
http://linkedlifedata.com/resource/pubmed/chemical/BID protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Camptothecin,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin B,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Proteinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Leucine,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/aloxistatin,
http://linkedlifedata.com/resource/pubmed/chemical/bcl-2-Associated X Protein
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1899-1505
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
56 Suppl 3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
159-79
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pubmed:dateRevised |
2008-5-19
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pubmed:meshHeading |
pubmed-meshheading:16077201-Antineoplastic Agents, Phytogenic,
pubmed-meshheading:16077201-Apoptosis,
pubmed-meshheading:16077201-Apoptosis Regulatory Proteins,
pubmed-meshheading:16077201-Autophagy,
pubmed-meshheading:16077201-BH3 Interacting Domain Death Agonist Protein,
pubmed-meshheading:16077201-Breast Neoplasms,
pubmed-meshheading:16077201-Camptothecin,
pubmed-meshheading:16077201-Cathepsin B,
pubmed-meshheading:16077201-Cell Line, Tumor,
pubmed-meshheading:16077201-Cysteine Proteinase Inhibitors,
pubmed-meshheading:16077201-Enzyme Activation,
pubmed-meshheading:16077201-Female,
pubmed-meshheading:16077201-Humans,
pubmed-meshheading:16077201-Kinetics,
pubmed-meshheading:16077201-Laser Scanning Cytometry,
pubmed-meshheading:16077201-Leucine,
pubmed-meshheading:16077201-Membrane Proteins,
pubmed-meshheading:16077201-Microscopy, Confocal,
pubmed-meshheading:16077201-Microscopy, Electron, Transmission,
pubmed-meshheading:16077201-Microtubule-Associated Proteins,
pubmed-meshheading:16077201-Mitochondria,
pubmed-meshheading:16077201-Signal Transduction,
pubmed-meshheading:16077201-bcl-2-Associated X Protein
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pubmed:year |
2005
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pubmed:articleTitle |
Cathepsins and BID are involved in the molecular switch between apoptosis and autophagy in breast cancer MCF-7 cells exposed to camptothecin.
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pubmed:affiliation |
Department of Physiological Sciences, Faculty of Veterinary Medicine, Warsaw Agricultural University, Warsaw, Poland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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