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[PMID]:29381398
[Au] Autor:Orywal K; Jelski W; Werel T; Szmitkowski M
[Ad] Endereço:a Department of Biochemical Diagnostics , Medical University , Bialystok , Podlaskie , Poland.
[Ti] Título:The Activity of Class I-IV Alcohol Dehydrogenase Isoenzymes and Aldehyde Dehydrogenase in Bladder Cancer Cells.
[So] Source:Cancer Invest;36(1):66-72, 2018 Jan 02.
[Is] ISSN:1532-4192
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVES: The aim of this study was to determine the differences in the activity of Alcohol Dehydrogenase (ADH) isoenzymes and Aldehyde Dehydrogenase (ALDH) in normal and cancerous bladder cells. METHODS: Class III, IV of ADH and total ADH activity were measured by the photometric method and class I, II ADH and ALDH activity by the fluorometric method. RESULTS: Significantly higher total activity of ADH was found in both, low-grade and high-grade bladder cancer, in comparison to healthy tissues. CONCLUSION: The increased activity of total ADH in bladder cancer cells may be the cause of metabolic disorders in cancer cells, which may intensify carcinogenesis.
[Mh] Termos MeSH primário: Álcool Desidrogenase/metabolismo
Aldeído Desidrogenase/metabolismo
Isoenzimas/metabolismo
Neoplasias da Bexiga Urinária/metabolismo
[Mh] Termos MeSH secundário: Adulto
Idoso
Idoso de 80 Anos ou mais
Carcinogênese/metabolismo
Feminino
Seres Humanos
Masculino
Meia-Idade
Bexiga Urinária/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Isoenzymes); EC 1.1.1.1 (Alcohol Dehydrogenase); EC 1.2.1.3 (Aldehyde Dehydrogenase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180131
[St] Status:MEDLINE
[do] DOI:10.1080/07357907.2017.1422511


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[PMID]:29190729
[Au] Autor:Tan Z; Jia X; Ma F; Feng Y; Lu H; Jin JO; Wu D; Yin L; Liu L; Zhang L
[Ad] Endereço:Shanghai Public Health Clinical Center, Fudan University, Shanghai, China.
[Ti] Título:Increased MMAB level in mitochondria as a novel biomarker of hepatotoxicity induced by Efavirenz.
[So] Source:PLoS One;12(11):e0188366, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Efavirenz (EFV), a non-nucleoside reverse transcriptase inhibitor (NNRTI), has been widely used in the therapy of human immunodeficiency virus (HIV) infection. Some of its toxic effects on hepatic cells have been reported to display features of mitochondrial dysfunction through bioenergetic stress and autophagy, etc. However, alteration of protein levels, especially mitochondrial protein levels, in hepatic cells during treatment of EFV has not been fully investigated. METHODS: We built a cell model of EFV-induced liver toxicity through treating Huh-7 cells with different concentrations of EFV for different time followed by the analysis of cell viability using cell counting kit -8 (CCK8) and reactive oxygen species (ROS) using 2',7'-dichlorodihydrofluorescein diacetate (DCFH-DA) and MitoSox dye. Proteomic profiles in the mitochondria of Huh-7 cells stimulated by EFV were analyzed. Four differentially expressed proteins were quantified by real time RT-PCR. We also detected the expression of mitochondrial precursor Cob(I)yrinic acid a,c-diamide adenosyltransferase (MMAB) by immunohistochemistry analysis in clinical samples. The expression levels of MMAB and ROS were detected in EFV-treated Huh-7 cells with and without shRNA used to knock down MMAB, and in primary hepatocytes (PHC). The effects of other anti-HIV drugs (nevirapine (NVP) and tenofovirdisoproxil (TDF)), and hydrogen peroxide (H2O2) were also tested. Amino acid analysis and fatty aldehyde dehydrogenase (ALDH3A2) expression after MMAB expression knock-down with shRNA was used to investigate the metabolic effect of MMAB in Huh-7 cells. RESULTS: EFV treatment inhibited cell viability and increased ROS production with time- and concentration-dependence. Proteomic study was performed at 2 hours after EFV treatment. After treated Huh-7 cells with EFV (2.5mg/L or 10 mg/L) for 2 h, fifteen differentially expressed protein spots from purified mitochondrion that included four mitochondria proteins were detected in EFV-treated Huh-7 cells compared to controls. Consistent with protein expression levels, mRNA expression levels of mitochondrial protein MMAB were also increased by EFV treatment. In addition, the liver of EFV-treated HIV infected patients showed substantially higher levels of MMAB expression compared to the livers of untreated or protease inhibitor (PI)-treated HIV-infected patients. Furthermore, ROS were found to be decreased in Huh-7 cells treated with shMMAB compared with empty plasmid treated with EFV at the concentration of 2.5 or 10 mg/L. MMAB was increased in EFV-treated Huh-7 cells and primary hepatocytes. However, no change in MMAB expression was detected after treatment of Huh-7 cells and primary hepatocytes with anti-HIV drugs nevirapine (NVP) and tenofovirdisoproxil (TDF), or hydrogen peroxide (H2O2), although ROS was increased in these cells. Finally, knockdown of MMAB by shRNA induced increases in the ß-Alanine (ß-Ala) production levels and decrease in ALDH3A2 expression. CONCLUSIONS: A mitochondrial proteomic study was performed to study the proteins related to EFV-inducted liver toxicity. MMAB might be a target and potential biomarker of hepatotoxicity in EFV-induced liver toxicity.
[Mh] Termos MeSH primário: Alquil e Aril Transferases/metabolismo
Benzoxazinas/toxicidade
Mitocôndrias/enzimologia
Inibidores da Transcriptase Reversa/farmacologia
[Mh] Termos MeSH secundário: Aldeído Desidrogenase/genética
Alquil e Aril Transferases/genética
Western Blotting
Linhagem Celular
Perfilação da Expressão Gênica
Técnicas de Silenciamento de Genes
Seres Humanos
Fígado/efeitos dos fármacos
Fígado/metabolismo
Proteínas Mitocondriais/genética
Estresse Oxidativo
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Transcrição Genética
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzoxazines); 0 (Mitochondrial Proteins); 0 (Reverse Transcriptase Inhibitors); EC 1.2.1.3 (Aldehyde Dehydrogenase); EC 2.5.- (Alkyl and Aryl Transferases); EC 2.5.1.17 (cob(I)alamin adenosyltransferase); JE6H2O27P8 (efavirenz)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171226
[Lr] Data última revisão:
171226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188366


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[PMID]:29241292
[Au] Autor:Swyka RA; Berkowitz DB
[Ad] Endereço:Department of Chemistry, University of Nebraska, Lincoln, Nebraska.
[Ti] Título:The In Situ Enzymatic Screening (ISES) Approach to Reaction Discovery and Catalyst Identification.
[So] Source:Curr Protoc Chem Biol;9(4):285-305, 2017 Dec 14.
[Is] ISSN:2160-4762
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The importance of discovering new chemical transformations and/or optimizing catalytic combinations has led to a flurry of activity in reaction screening. The in situ enzymatic screening (ISES) approach described here utilizes biological tools (enzymes/cofactors) to advance chemistry. The protocol interfaces an organic reaction layer with an adjacent aqueous layer containing reporting enzymes that act upon the organic reaction product, giving rise to a spectroscopic signal. ISES allows the experimentalist to rapidly glean information on the relative rates of a set of parallel organic/organometallic reactions under investigation, without the need to quench the reactions or draw aliquots. In certain cases, the real-time enzymatic readout also provides information on sense and magnitude of enantioselectivity and substrate specificity. This article contains protocols for single-well (relative rate) and double-well (relative rate/enantiomeric excess) ISES, in addition to a colorimetric ISES protocol and a miniaturized double-well procedure. © 2017 by John Wiley & Sons, Inc.
[Mh] Termos MeSH primário: Álcool Desidrogenase/metabolismo
Aldeído Desidrogenase/metabolismo
Técnicas de Química Combinatória
[Mh] Termos MeSH secundário: Álcool Desidrogenase/química
Aldeído Desidrogenase/química
Catálise
Compostos Organometálicos/química
Compostos Organometálicos/metabolismo
Saccharomyces cerevisiae/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Organometallic Compounds); EC 1.1.1.1 (Alcohol Dehydrogenase); EC 1.2.1.3 (Aldehyde Dehydrogenase)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171225
[Lr] Data última revisão:
171225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171215
[St] Status:MEDLINE
[do] DOI:10.1002/cpch.30


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[PMID]:29053735
[Au] Autor:Zabinyakov N; Bullivant G; Cao F; Fernandez Ojeda M; Jia ZP; Wen XY; Dowling JJ; Salomons GS; Mercimek-Andrews S
[Ad] Endereço:Genetics and Genome Biology Program, Research Institute, The Hospital for Sick Children, Toronto, Canada.
[Ti] Título:Characterization of the first knock-out aldh7a1 zebrafish model for pyridoxine-dependent epilepsy using CRISPR-Cas9 technology.
[So] Source:PLoS One;12(10):e0186645, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pyridoxine dependent epilepsy (PDE) is caused by likely pathogenic variants in ALDH7A1 (PDE-ALDH7A1) and inherited autosomal recessively. Neurotoxic alpha-amino adipic semialdehyde (alpha-AASA), piperideine 6-carboxylate and pipecolic acid accumulate in body fluids. Neonatal or infantile onset seizures refractory to anti-epileptic medications are clinical features. Treatment with pyridoxine, arginine and lysine-restricted diet does not normalize neurodevelopmental outcome or accumulation of neurotoxic metabolites. There is no animal model for high throughput drug screening. For this reason, we developed and characterized the first knock-out aldh7a1 zebrafish model using CRISPR-Cas9 technology. Zebrafish aldh7a1 mutants were generated by using a vector free method of CRISPR-Cas9 mutagenesis. Genotype analysis of aldh7a1 knock-out zebrafish was performed by high resolution melt analysis, direct sequencing and QIAxcel system. Electroencephalogram was performed. Alpha-AASA, piperideine 6-carboxylate and pipecolic acid, were measured by liquid chromatography-tandem mass spectrometry. Our knock-out aldh7a1 zebrafish has homozygous 5 base pair (bp) mutation in ALDH7A1. Knock-out aldh7a1 embryos have spontaneous rapid increase in locomotion and a rapid circling swim behavior earliest 8-day post fertilization (dpf). Electroencephalogram revealed large amplitude spike discharges compared to wild type. Knock-out aldh7a1 embryos have elevated alpha-AASA, piperideine 6-carboxylate and pipecolic acid compared to wild type embryos at 3 dpf. Knock-out aldh7a1 embryos showed no aldh7a1 protein by western blot compared to wild type. Our knock-out aldh7a1 zebrafish is a well characterized model for large-scale drug screening using behavioral and biochemical features and accurately recapitulates the human PDE-ALDH7A1 disease.
[Mh] Termos MeSH primário: Aldeído Desidrogenase/genética
Repetições Palindrômicas Curtas Agrupadas e Regularmente Espaçadas
Epilepsia/induzido quimicamente
Piridoxina/toxicidade
Peixe-Zebra/genética
[Mh] Termos MeSH secundário: Potenciais de Ação
Animais
Comportamento Animal
Eletroencefalografia
Epilepsia/genética
Epilepsia/fisiopatologia
Técnicas de Silenciamento de Genes
Peixe-Zebra/embriologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.2.1.3 (Aldehyde Dehydrogenase); KV2JZ1BI6Z (Pyridoxine)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171021
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186645


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[PMID]:29049740
[Au] Autor:Doherty RE; Sisley K; Hammond DW; Rennie IG; Cross NA
[Ad] Endereço:Academic Unit of Ophthalmology and Orthoptics, Department of Oncology and Metabolism, School of Medicine and Biomedical Sciences, University of Sheffield, Royal Hallamshire Hospital, Sheffield, United Kingdom.
[Ti] Título:Phenotypic Plasticity in Uveal Melanoma Is Not Restricted to a Tumor Subpopulation and Is Unrelated to Cancer Stem Cell Characteristics.
[So] Source:Invest Ophthalmol Vis Sci;58(12):5387-5395, 2017 Oct 01.
[Is] ISSN:1552-5783
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Purpose: Uveal melanoma (UM) is the most common primary intraocular malignancy in adults and approximately half of those diagnosed will die of metastasis. This study investigates whether UM progression is driven by a subpopulation of stem-like cells, termed "cancer stem cells" (CSCs). Methods: Expression of postulated stem cell markers aldehyde dehydrogenase (ALDH), CD44, and CD133 was analyzed in UM cell lines and primary UM short-term cultures (STCs) established from tumor samples. Additionally, the notion of a "cellular hierarchy" within UM was investigated. Finally, the phenomenon of phenotypic plasticity in response to environmental factors was explored. Results: We demonstrate that expression of ALDH, CD44, and CD133 does not select for a subpopulation of stem-like cells in either UM cell lines or UM STCs. Furthermore, there is an absence of a cellular hierarchy in cell lines and all cells in culture are able to drive tumor progression. Last, we show that established UM cell lines and UM STCs are plastic in nature and switch their phenotype in response to environmental stimuli. Conclusions: We hypothesize that this capacity to undergo phenotypic plasticity may be a consequence of neural crest lineage and renders the exploration of the CSC hypothesis extremely challenging in UM.
[Mh] Termos MeSH primário: Plasticidade Celular
Melanoma/patologia
Células-Tronco Neoplásicas/patologia
Neoplasias Uveais/patologia
[Mh] Termos MeSH secundário: Antígeno AC133/metabolismo
Aldeído Desidrogenase/metabolismo
Biomarcadores Tumorais/metabolismo
Linhagem Celular Tumoral
Citometria de Fluxo
Seres Humanos
Receptores de Hialuronatos/metabolismo
Melanoma/metabolismo
Células-Tronco Neoplásicas/metabolismo
Fenótipo
Ensaio Tumoral de Célula-Tronco
Neoplasias Uveais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AC133 Antigen); 0 (Biomarkers, Tumor); 0 (CD44 protein, human); 0 (Hyaluronan Receptors); 0 (PROM1 protein, human); EC 1.2.1.3 (Aldehyde Dehydrogenase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171020
[St] Status:MEDLINE
[do] DOI:10.1167/iovs.17-22272


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[PMID]:29028842
[Au] Autor:Reid P; Wilson P; Li Y; Marcu LG; Staudacher AH; Brown MP; Bezak E
[Ad] Endereço:School of Health Sciences, University of South Australia, Adelaide, Australia.
[Ti] Título:In vitro investigation of head and neck cancer stem cell proportions and their changes following X-ray irradiation as a function of HPV status.
[So] Source:PLoS One;12(10):e0186186, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Some head and neck squamous cell carcinomas (HNSCC) have a distinct aetiology, which depends on the presence of oncogenic human papilloma virus (HPV). Also, HNSCC contains cancer stem cells (CSCs) that have greater radioresistance and capacity to change replication dynamics in response to irradiation compared to non-clonogenic cells. Since there is limited data on CSCs in HNSCC as a function of HPV status, better understanding of their radiobiology may enable improved treatment outcome. METHODS: Baseline and post-irradiation changes in CSC proportions were investigated by flow cytometry in a HPV-negative (UM-SCC-1) and a HPV-positive (UM-SCC-47) HNSCC cell line, using fluorescent staining with CD44/ALDH markers. CSC proportions in both irradiated and unirradiated cultures were compared for the two cell lines at various times post-irradiation. To assess repopulation of CSCs, untreated cultures were depleted of CD44+/ALDH+ cells and re-cultured for 3 weeks before flow cytometry analysis. RESULTS: CSC proportions in untreated cell lines were 0.57% (UM-SCC-1) and 2.87% (UM-SCC-47). Untreated cell lines depleted of CD44+/ALDH+ repopulated this phenotype to a mean of 0.15% (UM-SCC-1) and 6.76% (UM-SCC-47). All UM-SCC-47 generations showed elevated CSC proportions after irradiation, with the most significant increase at 2 days post-irradiation. The highest elevation in UM-SCC-1 CSCs was observed at 1 day post-irradiation in the 2nd generation and at 3 days after irradiation in the 3rd generation. When measured after 10 days, only the 3rd generation of UM-SCC-1 showed elevated CSCs. CONCLUSIONS: CSC proportions in both cell lines were elevated after exposure and varied with time post irradiation. UM-SCC-47 displayed significant plasticity in repopulating the CSC phenotype in depleted cultures, which was not seen in UM-SCC-1.
[Mh] Termos MeSH primário: Carcinoma de Células Escamosas/patologia
Neoplasias de Cabeça e Pescoço/patologia
Células-Tronco Neoplásicas/patologia
Células-Tronco Neoplásicas/efeitos da radiação
Papillomaviridae/fisiologia
[Mh] Termos MeSH secundário: Aldeído Desidrogenase/metabolismo
Carcinoma de Células Escamosas/metabolismo
Carcinoma de Células Escamosas/radioterapia
Carcinoma de Células Escamosas/virologia
Linhagem Celular Tumoral
Relação Dose-Resposta à Radiação
Neoplasias de Cabeça e Pescoço/metabolismo
Neoplasias de Cabeça e Pescoço/radioterapia
Neoplasias de Cabeça e Pescoço/virologia
Seres Humanos
Receptores de Hialuronatos/metabolismo
Papillomaviridae/efeitos da radiação
Fatores de Tempo
Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hyaluronan Receptors); EC 1.2.1.3 (Aldehyde Dehydrogenase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171014
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186186


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[PMID]:28887587
[Au] Autor:Ruangnam S; Wanchana S; Phoka N; Saeansuk C; Mahatheeranont S; de Hoop SJ; Toojinda T; Vanavichit A; Arikit S
[Ad] Endereço:Faculty of Agriculture at Kamphaeng Saen, Kasetsart University Kamphaeng Saen Campus, Nakhon Pathom, 73140, Thailand.
[Ti] Título:A deletion of the gene encoding amino aldehyde dehydrogenase enhances the "pandan-like" aroma of winter melon (Benincasa hispida) and is a functional marker for the development of the aroma.
[So] Source:Theor Appl Genet;130(12):2557-2565, 2017 Dec.
[Is] ISSN:1432-2242
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:KEY MESSAGE: The gene conferring a "pandan-like" aroma of winter melon was identified. The sequence variation (804-bp deletion) found in the gene was used as the target for functional marker development. Winter melon (Benincasa hispida), a member of the Cucurbitaceae family, is a commonly consumed vegetable in Asian countries that is popular for its nutritional and medicinal value. A "pandan-like" aroma, which is economically important in crops including rice and soybean, is rarely found in most commercial varieties of winter melon, but is present in some landraces. This aroma is a value-added potential trait in breeding winter melon with a higher economic value. In this study, we confirmed that the aroma of winter melon is due to the potent volatile compound 2-acetyl-1-pyrroline (2AP) as previously identified in other plants. Based on an analysis of public transcriptome data, BhAMADH encoding an aminoaldehyde dehydrogenase (AMADH) was identified as a candidate gene conferring aroma of winter melon. A sequence comparison of BhAMADH between the aromatic and non-aromatic accessions revealed an 804-bp deletion encompassing exons 11-13 in the aromatic accession. The deletion caused several premature stop codons and could result in a truncated protein with a length of only 208 amino acids compared with 503 amino acids in the normal protein. A functional marker was successfully developed based on the 804-bp deletion and validated in 237 F progenies. A perfect association of the marker genotypes and aroma phenotypes indicates that BhAMADH is the major gene conferring the aroma. The recently developed functional marker could be efficiently used in breeding programs for the aroma trait in winter melon.
[Mh] Termos MeSH primário: Aldeído Desidrogenase/genética
Cucurbitaceae/genética
Odorantes
Pirróis/química
Deleção de Sequência
[Mh] Termos MeSH secundário: Produtos Agrícolas/enzimologia
Produtos Agrícolas/genética
Cucurbitaceae/enzimologia
Genes de Plantas
Marcadores Genéticos
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Genetic Markers); 0 (Pyrroles); EC 1.2.1.3 (Aldehyde Dehydrogenase); IGC0W6LY94 (2-acetyl-1-pyrroline)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170910
[St] Status:MEDLINE
[do] DOI:10.1007/s00122-017-2976-3


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[PMID]:28881356
[Au] Autor:Matsumoto A; Arcaroli J; Chen Y; Gasparetto M; Neumeister V; Thompson DC; Singh S; Smith C; Messersmith W; Vasiliou V
[Ad] Endereço:Department of Pharmaceutical Sciences, University of Colorado Denver, Aurora, CO 80045, USA.
[Ti] Título:Aldehyde dehydrogenase 1B1: a novel immunohistological marker for colorectal cancer.
[So] Source:Br J Cancer;117(10):1537-1543, 2017 Nov 07.
[Is] ISSN:1532-1827
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Aldehyde dehydrogenase (ALDH) 1A1 is an immunohistological biomarker of various solid tumours, but has not been successfully proved as a colorectal cancer (CRC) marker. We recently reported that ALDH1B1, which has functional roles in tumourigenesis, may be a better CRC marker than ALDH1A1. METHODS: Human CRC explants and cell lines were analysed to identify candidate CRC markers from eight ALDH isozymes including ALDH1A1 and ALDH1B1. A tissue microarray, including paired specimens of normal and tumour tissues, was subsequently analysed to determine if candidate ALDHs could distinguish CRC from normal tissue. RESULTS: Based on mRNA analysis, ALDH1B1 and ALDH2 were selected as suitable candidates. These were strongly and regularly expressed in tumour tissue and cell lines, including highly tumourigenic cell populations (ALDH CD44 cells), while other ALDHs, including ALDH1A1, showed differential or low expression. No genetic alteration of ALDH1B1 in CRC was suggested by the relationships between mRNA and protein levels/enzymatic activities, and cDNA sequences of CRC cell lines. Tissue microarray findings showed that ALDH1B1, but not ALDH2, could distinguish CRC from normal tissue. Furthermore, ratios of ALDH1B1 to ALDH1A1 or ALDH2 were found to be powerful CRC indicators. CONCLUSIONS: These results suggest that ALDH1B1 is a novel human CRC biomarker.
[Mh] Termos MeSH primário: Aldeído Desidrogenase/análise
Biomarcadores Tumorais/análise
Neoplasias Colorretais/diagnóstico
Neoplasias Colorretais/enzimologia
[Mh] Termos MeSH secundário: Aldeído Desidrogenase/biossíntese
Seres Humanos
Imuno-Histoquímica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); EC 1.2.1.3 (ALDH1B1 protein, human); EC 1.2.1.3 (Aldehyde Dehydrogenase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171117
[Lr] Data última revisão:
171117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170908
[St] Status:MEDLINE
[do] DOI:10.1038/bjc.2017.304


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[PMID]:28870918
[Au] Autor:Orywal K; Jelski W; Werel T; Szmitkowski M
[Ad] Endereço:Department of Biochemical Diagnostics, Medical University of Bialystok, Bialystok, Poland orywalk@umb.edu.pl.
[Ti] Título:The Diagnostic Significance of Serum Alcohol Dehydrogenase Isoenzymes and Aldehyde Dehydrogenase Activity in Prostate Cancer Patients.
[So] Source:Anticancer Res;37(9):4961-4965, 2017 09.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIM: The aim of this study was to investigate a potential role of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) as tumor markers for prostate cancer (PCa). MATERIALS AND METHODS: Serum samples were obtained from 52 patients with PCa, 34 patients with benign prostatic hyperplasia (BPH) and 60 healthy subjects. Class III and IV of ADH and total ADH activity were measured by the photometric method. For measurement of class I and II ADH and ALDH activity, the fluorometric method was employed. RESULTS: Significantly higher total activity of ADH, ADH III and ADH IV were found in the sera of both, PCa and BPH patients compared with healthy individuals. The diagnostic sensitivity for ADH III activity was 94.2%, specificity 100%, PPV (positive predictive value) and NPV (negative predictive value) were 100% and 95.2% respectively. Area under receiver-operating characteristics (ROC) curve for ADH III activity was 0.993. CONCLUSION: The results suggest a potential role of ADH III activity as a parameter included in the panel of markers for PCa.
[Mh] Termos MeSH primário: Álcool Desidrogenase/metabolismo
Aldeído Desidrogenase/metabolismo
Biomarcadores Tumorais/metabolismo
Hiperplasia Prostática/diagnóstico
Neoplasias da Próstata/diagnóstico
[Mh] Termos MeSH secundário: Idoso
Idoso de 80 Anos ou mais
Estudos de Casos e Controles
Seguimentos
Seres Humanos
Isoenzimas
Masculino
Meia-Idade
Gradação de Tumores
Estadiamento de Neoplasias
Prognóstico
Hiperplasia Prostática/enzimologia
Neoplasias da Próstata/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Isoenzymes); EC 1.1.1.1 (Alcohol Dehydrogenase); EC 1.2.1.3 (Aldehyde Dehydrogenase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170906
[St] Status:MEDLINE


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[PMID]:28828965
[Au] Autor:Liu Y; Kurita A; Nakashima S; Zhu B; Munemasa S; Nakamura T; Murata Y; Nakamura Y
[Ad] Endereço:a Graduate School of Environmental and Life Science , Okayama University , Okayama , Japan.
[Ti] Título:3,4-Dihydroxyphenylacetic acid is a potential aldehyde dehydrogenase inducer in murine hepatoma Hepa1c1c7 cells.
[So] Source:Biosci Biotechnol Biochem;81(10):1978-1983, 2017 Oct.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:3,4-Dihydroxyphenylacetic acid (DOPAC) is one of the major colonic microflora-produced catabolites of quercetin glycosides, such as quercetin 4'-glucoside derived from onion. Here, we investigated whether DOPAC modulates the aldehyde dehydrogenase (ALDH) activity and protects the cells from the acetaldehyde-induced cytotoxicity in vitro. DOPAC was shown to enhance not only the total ALDH activity, but also the gene expression of ALDH1A1, ALDH2 and ALDH3A1 in a concentration-dependent manner. DOPAC simultaneously stimulated the nuclear translocation of NFE2-related factor 2 and aryl hydrocarbon receptor. The pretreatment of DOPAC completely protected the cells from the acetaldehyde-induced cytotoxicity. The present study suggested that DOPAC acts as a potential ALDH inducer to prevent the alcohol-induced abnormal reaction.
[Mh] Termos MeSH primário: Ácido 3,4-Di-Hidroxifenilacético/farmacologia
Aldeído Desidrogenase/biossíntese
Carcinoma Hepatocelular/patologia
Neoplasias Hepáticas/patologia
[Mh] Termos MeSH secundário: Acetaldeído/toxicidade
Aldeído Desidrogenase/genética
Aldeído Desidrogenase/metabolismo
Animais
Linhagem Celular Tumoral
Relação Dose-Resposta a Droga
Indução Enzimática/efeitos dos fármacos
Regulação Enzimológica da Expressão Gênica/efeitos dos fármacos
Camundongos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
102-32-9 (3,4-Dihydroxyphenylacetic Acid); EC 1.2.1.3 (Aldehyde Dehydrogenase); GO1N1ZPR3B (Acetaldehyde)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170823
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2017.1361809



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