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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
14
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pubmed:dateCreated |
2001-9-21
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pubmed:abstractText |
Proteome analysis led to the identification and characterization of tumor-associated protein variants by two-dimensional electrophoresis and mass spectrometry. We focused on comparing the influence of genotoxic nitroso compounds N-methyl-N-nitrosourea, diethylnitrosamine and N-nitrosomorpholine and the nongenotoxic peroxisome proliferator Nafenopin as tumor-inducing agents on the protein pattern of rat hepatomas. We found several tumor-associated variants that represent members of the aldo-keto reductase superfamily. Their induction and/or inhibition was specifically related to the carcinogen used for tumor induction. The most prominent tumor-associated protein, rat aldose reductase-like protein-1 (rARLP-1) (69% sequence identity to lens aldose reductase) and three additional types of rARLP-1 were detected in nitroso compound-induced rat hepatomas, while rat aldo-keto reductase protein-c (Rak-c), a novel tumor-associated variant (65% sequence identity with 3alpha-hydroxysteroid dehydrogenase) was discovered in N-methyl-N-nitrosourea-induced hepatomas only. 3Alpha-hydroxysteroid dehydrogenase and delta4-3-ketosteroid-5beta-reductase, both liver-specific enzymes, were reduced in amount in all hepatomas investigated, independent of their mode of induction. We conclude, that detoxification enzymes like 3alpha-hydroxysteroid dehydrogenase (3alpha-HSD) and delta4-3-ketosteroid-5beta-reductase (5beta-Red) might be replaced in hepatomas by tumor-associated proteins that are often present in the embryonal state, like the rARLPs or the Rak-c protein. Their induction appears to reflect an altered constitutive pattern of detoxification enzymes, detoxifying toxic aldehydes being induced by nitroso compounds. In contrast, members of the aldo-keto reductase superfamily have not been found in Nafenopin-induced hepatomas. The pattern of tumor-associated protein variants is apparently characteristic for a given group of initiating carcinogens. The hypothesis is proposed that carcinogens leave specific fingerprints at the proteome level of manifest liver tumors.
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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/AKR1B10 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Aldehyde Reductase,
http://linkedlifedata.com/resource/pubmed/chemical/Carcinogens,
http://linkedlifedata.com/resource/pubmed/chemical/Diethylnitrosamine,
http://linkedlifedata.com/resource/pubmed/chemical/Fetal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Methylnitrosourea,
http://linkedlifedata.com/resource/pubmed/chemical/N-nitrosomorpholine,
http://linkedlifedata.com/resource/pubmed/chemical/Nafenopin,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrosamines,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxisome Proliferators,
http://linkedlifedata.com/resource/pubmed/chemical/Proteome
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0173-0835
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3009-18
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11565795-Aldehyde Reductase,
pubmed-meshheading:11565795-Amino Acid Sequence,
pubmed-meshheading:11565795-Animals,
pubmed-meshheading:11565795-Base Sequence,
pubmed-meshheading:11565795-Carcinogens,
pubmed-meshheading:11565795-Diethylnitrosamine,
pubmed-meshheading:11565795-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:11565795-Fetal Proteins,
pubmed-meshheading:11565795-Gene Expression Profiling,
pubmed-meshheading:11565795-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:11565795-Isoenzymes,
pubmed-meshheading:11565795-Liver Neoplasms, Experimental,
pubmed-meshheading:11565795-Male,
pubmed-meshheading:11565795-Metabolic Detoxication, Drug,
pubmed-meshheading:11565795-Methylnitrosourea,
pubmed-meshheading:11565795-Molecular Sequence Data,
pubmed-meshheading:11565795-Nafenopin,
pubmed-meshheading:11565795-Neoplasm Proteins,
pubmed-meshheading:11565795-Nitrosamines,
pubmed-meshheading:11565795-Organ Specificity,
pubmed-meshheading:11565795-Peroxisome Proliferators,
pubmed-meshheading:11565795-Proteome,
pubmed-meshheading:11565795-Rats,
pubmed-meshheading:11565795-Rats, Wistar,
pubmed-meshheading:11565795-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:11565795-Sequence Alignment,
pubmed-meshheading:11565795-Sequence Homology, Amino Acid,
pubmed-meshheading:11565795-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:11565795-Subtraction Technique
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pubmed:year |
2001
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pubmed:articleTitle |
Proteome analysis of rat hepatomas: carcinogen-dependent tumor-associated protein variants.
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pubmed:affiliation |
Institute of Pathology, University of Munich, Germany.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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