Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2007-8-7
pubmed:abstractText
A correlation between regulation of cell proliferation and polyamine metabolism is described. The latter can enter protein synthesis through the modification of eukaryotic initiation factor 5A (eIF5A) and the formation of the peculiar amino acid hypusine. Specific inhibitors of hypusine formation induce apoptosis that can be potentiated by the combination with cytokines such as interferonalpha (IFNalpha) that itself decreases hypusine synthesis. We have also demonstrated that the concomitant treatment of cancer cells with IFNalpha and the protein synthesis inhibitor fusion protein TGFalpha/Pseudomonas Aeruginosa toxin synergize in inducing cancer cell growth inhibition. Another way used by polyamines to induce apoptosis is the generation of intracellular oxidative stress through the interaction with bovine serum amine oxidase (BSAO). This enzyme used simultaneously to spermine induces apoptosis, necrosis, inhibition of cell proliferation and inhibition of DNA and protein synthesis in several cell types. The enzymatic oxidation products of polyamine, H2O2 and aldehyde(s) cause these effects. We have recently found that the cytotoxicity of anti-cancer agents, either etoposide or docetaxel, in cancer cells is potentiated in the presence of BSAO/Spermine. In conclusion, polyamine metabolites could be useful in the design of new therapeutic strategies.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosylmethionine Decarboxylase, http://linkedlifedata.com/resource/pubmed/chemical/Amine Oxidase (Copper-Containing), http://linkedlifedata.com/resource/pubmed/chemical/Antineoplastic Agents, http://linkedlifedata.com/resource/pubmed/chemical/Caspases, http://linkedlifedata.com/resource/pubmed/chemical/Etoposide, http://linkedlifedata.com/resource/pubmed/chemical/Interferon-alpha, http://linkedlifedata.com/resource/pubmed/chemical/Lysine, http://linkedlifedata.com/resource/pubmed/chemical/Ornithine Decarboxylase, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Initiation Factors, http://linkedlifedata.com/resource/pubmed/chemical/Polyamines, http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Taxoids, http://linkedlifedata.com/resource/pubmed/chemical/docetaxel, http://linkedlifedata.com/resource/pubmed/chemical/eukaryotic translation initiation..., http://linkedlifedata.com/resource/pubmed/chemical/hypusine
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1438-2199
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
273-81
pubmed:dateRevised
2009-7-24
pubmed:meshHeading
pubmed-meshheading:17610128-Adenosylmethionine Decarboxylase, pubmed-meshheading:17610128-Amine Oxidase (Copper-Containing), pubmed-meshheading:17610128-Animals, pubmed-meshheading:17610128-Antineoplastic Agents, pubmed-meshheading:17610128-Caspases, pubmed-meshheading:17610128-Cattle, pubmed-meshheading:17610128-Cell Proliferation, pubmed-meshheading:17610128-Drug Synergism, pubmed-meshheading:17610128-Etoposide, pubmed-meshheading:17610128-Humans, pubmed-meshheading:17610128-Hyperthermia, Induced, pubmed-meshheading:17610128-Interferon-alpha, pubmed-meshheading:17610128-Lysine, pubmed-meshheading:17610128-Ornithine Decarboxylase, pubmed-meshheading:17610128-Oxidation-Reduction, pubmed-meshheading:17610128-Peptide Initiation Factors, pubmed-meshheading:17610128-Polyamines, pubmed-meshheading:17610128-RNA-Binding Proteins, pubmed-meshheading:17610128-Taxoids
pubmed:year
2007
pubmed:articleTitle
Anticancer drugs and hyperthermia enhance cytotoxicity induced by polyamine enzymatic oxidation products.
pubmed:affiliation
Department of Experimental Oncology, Experimental Pharmacology Unit, National Institute of Tumours Fondaz. G. Pascale, Naples, Italy.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't