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  1 / 20 MEDLINE  
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[PMID]:28754309
[Au] Autor:Alonso S; Jones RJ; Ghiaur G
[Ad] Endereço:Sidney Kimmel Comprehensive Cancer Center, Department of Oncology, Johns Hopkins University, Baltimore, Maryland.
[Ti] Título:Retinoic acid, CYP26, and drug resistance in the stem cell niche.
[So] Source:Exp Hematol;54:17-25, 2017 Oct.
[Is] ISSN:1873-2399
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The bone marrow niche is essential for hematopoietic stem cells to maintain lifelong blood production by balancing their self-renewal and differentiation. Hematologic malignancies have a similar hierarchical organization to their normal counterparts, with rare populations of cancer stem cells that rely on the microenvironment to survive and propagate their differentiated malignant progenitor cells. Cancer cells alter their microenvironment to create a supportive niche, where they endure chemotherapy, survive as minimal residual disease (MRD), and eventually prevail at relapse. Powerful morphogens, such as retinoids, Wnt/ßcatenin, Notch, and Hedgehog, control stem cell fates across tissues, including normal and malignant hematopoiesis. The molecular conversations between these pathways and the mechanisms that control their activity and create gradients at cellular scale remain a mystery. Here, we discuss accumulating evidence suggesting that cytochrome P450 (CYP26), the primary retinoid-inactivating enzyme, plays a critical role in the integration of two of these molecular programs: the retinoid and Hedgehog pathways. Induction of stromal CYP26 by either one of these pathways limits retinoic acid concentration in the stem cell niche, with profound effects on tissue homeostasis and drug resistance. Bypassing this gatekeeping mechanism holds promise for overcoming drug resistance and improving clinical outcomes in hematological malignancies and cancer in general.
[Mh] Termos MeSH primário: Família 26 do Citocromo P450/genética
Resistência a Medicamentos Antineoplásicos/genética
Regulação Neoplásica da Expressão Gênica
Neoplasias Hematológicas/genética
Recidiva Local de Neoplasia/genética
Tretinoína/metabolismo
[Mh] Termos MeSH secundário: Antineoplásicos/uso terapêutico
Família 26 do Citocromo P450/metabolismo
Resistência a Medicamentos Antineoplásicos/efeitos dos fármacos
Proteínas Hedgehog/genética
Proteínas Hedgehog/metabolismo
Neoplasias Hematológicas/tratamento farmacológico
Neoplasias Hematológicas/metabolismo
Neoplasias Hematológicas/patologia
Células-Tronco Hematopoéticas/efeitos dos fármacos
Células-Tronco Hematopoéticas/metabolismo
Células-Tronco Hematopoéticas/patologia
Seres Humanos
Recidiva Local de Neoplasia/tratamento farmacológico
Recidiva Local de Neoplasia/metabolismo
Recidiva Local de Neoplasia/patologia
Neoplasia Residual
Células-Tronco Neoplásicas/efeitos dos fármacos
Células-Tronco Neoplásicas/metabolismo
Células-Tronco Neoplásicas/patologia
Receptores Notch/genética
Receptores Notch/metabolismo
Transdução de Sinais
Nicho de Células-Tronco/efeitos dos fármacos
Nicho de Células-Tronco/genética
Microambiente Tumoral/efeitos dos fármacos
Microambiente Tumoral/genética
beta Catenina/genética
beta Catenina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Hedgehog Proteins); 0 (Receptors, Notch); 0 (beta Catenin); 5688UTC01R (Tretinoin); EC 1.14.14.1 (Cytochrome P450 Family 26)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170730
[St] Status:MEDLINE


  2 / 20 MEDLINE  
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[PMID]:28715412
[Au] Autor:El Shahawy M; Reibring CG; Neben CL; Hallberg K; Marangoni P; Harfe BD; Klein OD; Linde A; Gritli-Linde A
[Ad] Endereço:Department of Oral Biochemistry, Institute of Odontology, Sahlgrenska Academy at the University of Gothenburg, Göteborg, Sweden.
[Ti] Título:Cell fate specification in the lingual epithelium is controlled by antagonistic activities of Sonic hedgehog and retinoic acid.
[So] Source:PLoS Genet;13(7):e1006914, 2017 Jul.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The interaction between signaling pathways is a central question in the study of organogenesis. Using the developing murine tongue as a model, we uncovered unknown relationships between Sonic hedgehog (SHH) and retinoic acid (RA) signaling. Genetic loss of SHH signaling leads to enhanced RA activity subsequent to loss of SHH-dependent expression of Cyp26a1 and Cyp26c1. This causes a cell identity switch, prompting the epithelium of the tongue to form heterotopic minor salivary glands and to overproduce oversized taste buds. At developmental stages during which Wnt10b expression normally ceases and Shh becomes confined to taste bud cells, loss of SHH inputs causes the lingual epithelium to undergo an ectopic and anachronic expression of Shh and Wnt10b in the basal layer, specifying de novo taste placode induction. Surprisingly, in the absence of SHH signaling, lingual epithelial cells adopted a Merkel cell fate, but this was not caused by enhanced RA signaling. We show that RA promotes, whereas SHH, acting strictly within the lingual epithelium, inhibits taste placode and lingual gland formation by thwarting RA activity. These findings reveal key functions for SHH and RA in cell fate specification in the lingual epithelium and aid in deciphering the molecular mechanisms that assign cell identity.
[Mh] Termos MeSH primário: Diferenciação Celular/efeitos dos fármacos
Epitélio/efeitos dos fármacos
Proteínas Hedgehog/metabolismo
Tretinoína/farmacologia
[Mh] Termos MeSH secundário: Alelos
Animais
Linhagem Celular
Família 26 do Citocromo P450/genética
Família 26 do Citocromo P450/metabolismo
Células Epiteliais/metabolismo
Epitélio/crescimento & desenvolvimento
Feminino
Proteínas Hedgehog/genética
Masculino
Células de Merkel/efeitos dos fármacos
Células de Merkel/metabolismo
Camundongos
Ácido Retinoico 4 Hidroxilase/genética
Ácido Retinoico 4 Hidroxilase/metabolismo
Transdução de Sinais
Papilas Gustativas/metabolismo
Língua/crescimento & desenvolvimento
Proteínas Wnt/genética
Proteínas Wnt/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hedgehog Proteins); 0 (Shh protein, mouse); 0 (Wnt Proteins); 0 (Wnt10b protein, mouse); 5688UTC01R (Tretinoin); EC 1.14.14.1 (Cyp26a1 protein, mouse); EC 1.14.14.1 (Cyp26c1 protein, mouse); EC 1.14.14.1 (Cytochrome P450 Family 26); EC 1.14.14.1 (Retinoic Acid 4-Hydroxylase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170824
[Lr] Data última revisão:
170824
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170718
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006914


  3 / 20 MEDLINE  
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[PMID]:28103795
[Au] Autor:Carvalho JE; Theodosiou M; Chen J; Chevret P; Alvarez S; De Lera AR; Laudet V; Croce JC; Schubert M
[Ad] Endereço:Sorbonne Universités, UPMC Université Paris 06, CNRS, Laboratoire de Biologie du Développement de Villefranche-sur-Mer, Observatoire Océanologique de Villefranche-sur-Mer, 181 Chemin du Lazaret, 06230, Villefranche-sur-Mer, France.
[Ti] Título:Lineage-specific duplication of amphioxus retinoic acid degrading enzymes (CYP26) resulted in sub-functionalization of patterning and homeostatic roles.
[So] Source:BMC Evol Biol;17(1):24, 2017 Jan 19.
[Is] ISSN:1471-2148
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: During embryogenesis, tight regulation of retinoic acid (RA) availability is fundamental for normal development. In parallel to RA synthesis, a negative feedback loop controlled by RA catabolizing enzymes of the cytochrome P450 subfamily 26 (CYP26) is crucial. In vertebrates, the functions of the three CYP26 enzymes (CYP26A1, CYP26B1, and CYP26C1) have been well characterized. By contrast, outside vertebrates, little is known about CYP26 complements and their biological roles. In an effort to characterize the evolutionary diversification of RA catabolism, we studied the CYP26 genes of the cephalochordate amphioxus (Branchiostoma lanceolatum), a basal chordate with a vertebrate-like genome that has not undergone the massive, large-scale duplications of vertebrates. RESULTS: In the present study, we found that amphioxus also possess three CYP26 genes (CYP26-1, CYP26-2, and CYP26-3) that are clustered in the genome and originated by lineage-specific duplication. The amphioxus CYP26 cluster thus represents a useful model to assess adaptive evolutionary changes of the RA signaling system following gene duplication. The characterization of amphioxus CYP26 expression, function, and regulation by RA signaling demonstrated that, despite the independent origins of CYP26 duplicates in amphioxus and vertebrates, they convergently assume two main roles during development: RA-dependent patterning and protection against fluctuations of RA levels. Our analysis suggested that in amphioxus RA-dependent patterning is sustained by CYP26-2, while RA homeostasis is mediated by CYP26-1 and CYP26-3. Furthermore, comparisons of the regulatory regions of CYP26 genes of different bilaterian animals indicated that a CYP26-driven negative feedback system was present in the last common ancestor of deuterostomes, but not in that of bilaterians. CONCLUSIONS: Altogether, this work reveals the evolutionary origins of the RA-dependent regulation of CYP26 genes and highlights convergent functions for CYP26 enzymes that originated by independent duplication events, hence establishing a novel selective mechanism for the genomic retention of gene duplicates.
[Mh] Termos MeSH primário: Família 26 do Citocromo P450/metabolismo
Anfioxos/genética
Tretinoína/metabolismo
[Mh] Termos MeSH secundário: Animais
Família 26 do Citocromo P450/genética
Desenvolvimento Embrionário
Evolução Molecular
Duplicação Gênica
Genoma
Anfioxos/enzimologia
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
5688UTC01R (Tretinoin); EC 1.14.14.1 (Cytochrome P450 Family 26)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170121
[St] Status:MEDLINE
[do] DOI:10.1186/s12862-016-0863-1


  4 / 20 MEDLINE  
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[PMID]:27893754
[Au] Autor:Rydeen AB; Waxman JS
[Ad] Endereço:Molecular Cardiovascular Biology Division and Heart Institute, Cincinnati Children's Hospital Medical Center, Cincinnati, Ohio, United States of America.
[Ti] Título:Cyp26 Enzymes Facilitate Second Heart Field Progenitor Addition and Maintenance of Ventricular Integrity.
[So] Source:PLoS Biol;14(11):e2000504, 2016 Nov.
[Is] ISSN:1545-7885
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Although retinoic acid (RA) teratogenicity has been investigated for decades, the mechanisms underlying RA-induced outflow tract (OFT) malformations are not understood. Here, we show zebrafish embryos deficient for Cyp26a1 and Cyp26c1 enzymes, which promote RA degradation, have OFT defects resulting from two mechanisms: first, a failure of second heart field (SHF) progenitors to join the OFT, instead contributing to the pharyngeal arch arteries (PAAs), and second, a loss of first heart field (FHF) ventricular cardiomyocytes due to disrupted cell polarity and extrusion from the heart tube. Molecularly, excess RA signaling negatively regulates fibroblast growth factor 8a (fgf8a) expression and positively regulates matrix metalloproteinase 9 (mmp9) expression. Although restoring Fibroblast growth factor (FGF) signaling can partially rescue SHF addition in Cyp26 deficient embryos, attenuating matrix metalloproteinase (MMP) function can rescue both ventricular SHF addition and FHF integrity. These novel findings indicate a primary effect of RA-induced OFT defects is disruption of the extracellular environment, which compromises both SHF recruitment and FHF ventricular integrity.
[Mh] Termos MeSH primário: Família 26 do Citocromo P450/metabolismo
Ventrículos do Coração/enzimologia
Miocárdio/enzimologia
Peixe-Zebra/embriologia
[Mh] Termos MeSH secundário: Animais
Fatores de Crescimento de Fibroblastos/metabolismo
Metaloproteinases da Matriz/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
62031-54-3 (Fibroblast Growth Factors); EC 1.14.14.1 (Cytochrome P450 Family 26); EC 3.4.24.- (Matrix Metalloproteinases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170524
[Lr] Data última revisão:
170524
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161129
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pbio.2000504


  5 / 20 MEDLINE  
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[PMID]:27861128
[Au] Autor:Montalbano A; Juergensen L; Roeth R; Weiss B; Fukami M; Fricke-Otto S; Binder G; Ogata T; Decker E; Nuernberg G; Hassel D; Rappold GA
[Ad] Endereço:Department of Human Molecular Genetics, Heidelberg University, Heidelberg, Germany.
[Ti] Título:Retinoic acid catabolizing enzyme CYP26C1 is a genetic modifier in SHOX deficiency.
[So] Source:EMBO Mol Med;8(12):1455-1469, 2016 12.
[Is] ISSN:1757-4684
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mutations in the homeobox gene SHOX cause SHOX deficiency, a condition with clinical manifestations ranging from short stature without dysmorphic signs to severe mesomelic skeletal dysplasia. In rare cases, individuals with SHOX deficiency are asymptomatic. To elucidate the factors that modify disease severity/penetrance, we studied a three-generation family with SHOX deficiency. The variant p.Phe508Cys of the retinoic acid catabolizing enzyme CYP26C1 co-segregated with the SHOX variant p.Val161Ala in the affected individuals, while the SHOX mutant alone was present in asymptomatic individuals. Two further cases with SHOX deficiency and damaging CYP26C1 variants were identified in a cohort of 68 individuals with LWD The identified CYP26C1 variants affected its catabolic activity, leading to an increased level of retinoic acid. High levels of retinoic acid significantly decrease SHOX expression in human primary chondrocytes and zebrafish embryos. Individual morpholino knockdown of either gene shortens the pectoral fins, whereas depletion of both genes leads to a more severe phenotype. Together, our findings describe CYP26C1 as the first genetic modifier for SHOX deficiency.
[Mh] Termos MeSH primário: Família 26 do Citocromo P450/genética
Predisposição Genética para Doença
Transtornos do Crescimento/genética
Transtornos do Crescimento/patologia
Proteínas de Homeodomínio/genética
Osteocondrodisplasias/genética
Osteocondrodisplasias/patologia
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Animais
Criança
Família 26 do Citocromo P450/metabolismo
Feminino
Perfilação da Expressão Gênica
Variação Genética
Seres Humanos
Masculino
Meia-Idade
Ácido Retinoico 4 Hidroxilase/genética
Ácido Retinoico 4 Hidroxilase/metabolismo
Análise de Sequência de DNA
Índice de Gravidade de Doença
Proteína de Homoeobox de Baixa Estatura
Tretinoína/metabolismo
Adulto Jovem
Peixe-Zebra/anatomia & histologia
Proteínas de Peixe-Zebra/genética
Proteínas de Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Homeodomain Proteins); 0 (SHOX protein, human); 0 (Short Stature Homeobox Protein); 0 (Zebrafish Proteins); 5688UTC01R (Tretinoin); EC 1.14.14.1 (CYP26C1 protein, human); EC 1.14.14.1 (Cyp26c1 protein, zebrafish); EC 1.14.14.1 (Cytochrome P450 Family 26); EC 1.14.14.1 (Retinoic Acid 4-Hydroxylase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE
[do] DOI:10.15252/emmm.201606623


  6 / 20 MEDLINE  
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[PMID]:27830503
[Au] Autor:Kedishvili NY
[Ad] Endereço:Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, 720 20th Street South, 35294, Birmingham, AL, USA. nkedishvili@uab.edu.
[Ti] Título:Retinoic Acid Synthesis and Degradation.
[So] Source:Subcell Biochem;81:127-161, 2016.
[Is] ISSN:0306-0225
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Retinoic acid (RA) was identified as the biologically active form of vitamin A almost 70 years ago and work on its function and mechanism of action is still of major interest both from a scientific and a clinical perspective. The currently accepted model postulates that RA is produced in two sequential oxidative steps: first, retinol is oxidized reversibly to retinaldehyde, and then retinaldehyde is oxidized irreversibly to RA. Excess RA is inactivated by conversion to hydroxylated derivatives. Much is left to learn, especially about retinoid binding proteins and the trafficking of the hydrophobic retinoid substrates between membrane bound and cytosolic enzymes. Here, background on development of the field and an update on recent advances in our understanding of the enzymatic pathways and mechanisms that control the rate of RA production and degradation are presented with a focus on the many questions that remain unanswered.
[Mh] Termos MeSH primário: Tretinoína/metabolismo
[Mh] Termos MeSH secundário: Aldeído Desidrogenase/metabolismo
Animais
Transporte Biológico
Membrana Celular/enzimologia
Família 26 do Citocromo P450/metabolismo
Citosol/enzimologia
Retroalimentação Fisiológica
Previsões
Seres Humanos
Isoenzimas/metabolismo
Camundongos
Microssomos Hepáticos/enzimologia
Oxirredução
Oxirredutases/metabolismo
Ratos
Proteínas Recombinantes/metabolismo
Retinaldeído/metabolismo
Vitamina A/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Isoenzymes); 0 (Recombinant Proteins); 11103-57-4 (Vitamin A); 5688UTC01R (Tretinoin); EC 1.- (Oxidoreductases); EC 1.14.14.1 (Cytochrome P450 Family 26); EC 1.2.1.3 (Aldehyde Dehydrogenase); RR725D715M (Retinaldehyde)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161111
[St] Status:MEDLINE


  7 / 20 MEDLINE  
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[PMID]:27589347
[Au] Autor:Nilsson O; Isoherranen N; Guo MH; Lui JC; Jee YH; Guttmann-Bauman I; Acerini C; Lee W; Allikmets R; Yanovski JA; Dauber A; Baron J
[Ad] Endereço:Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA.
[Ti] Título:Accelerated Skeletal Maturation in Disorders of Retinoic Acid Metabolism: A Case Report and Focused Review of the Literature.
[So] Source:Horm Metab Res;48(11):737-744, 2016 Nov.
[Is] ISSN:1439-4286
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Nutritional excess of vitamin A, a precursor for retinoic acid (RA), causes premature epiphyseal fusion, craniosynostosis, and light-dependent retinopathy. Similarly, homozygous loss-of-function mutations in CYP26B1, one of the major RA-metabolizing enzymes, cause advanced bone age, premature epiphyseal fusion, and craniosynostosis. In this paper, a patient with markedly accelerated skeletal and dental development, retinal scarring, and autism-spectrum disease is presented and the role of retinoic acid in longitudinal bone growth and skeletal maturation is reviewed. Genetic studies were carried out using SNP array and exome sequencing. RA isomers were measured in the patient, family members, and in 18 age-matched healthy children using high-performance liquid chromatography coupled to tandem mass spectrometry. A genomic SNP array identified a novel 8.3 megabase microdeletion on chromosome 10q23.2-23.33. The 79 deleted genes included and , both major RA-metabolizing enzymes. Exome sequencing did not detect any variants that were predicted to be deleterious in the remaining alleles of these genes or other known retinoic acid-metabolizing enzymes. The patient exhibited elevated plasma total RA (16.5 vs. 12.6±1.5 nM, mean±SD, subject vs. controls) and 13- RA (10.7 nM vs. 6.1±1.1). The findings support the hypothesis that elevated RA concentrations accelerate bone and dental maturation in humans. CYP26A1 and C1 haploinsufficiency may contribute to the elevated retinoic acid concentrations and clinical findings of the patient, although this phenotype has not been reported in other patients with similar deletions, suggesting that other unknown genetic or environmental factors may also contribute.
[Mh] Termos MeSH primário: Doenças do Desenvolvimento Ósseo/patologia
Família 26 do Citocromo P450/genética
Ácido Retinoico 4 Hidroxilase/genética
Tretinoína/metabolismo
[Mh] Termos MeSH secundário: Doenças do Desenvolvimento Ósseo/genética
Criança
Cromossomos Humanos Par 10/genética
Regulação Enzimológica da Expressão Gênica
Seres Humanos
Masculino
Fenótipo
Polimorfismo de Nucleotídeo Único/genética
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
5688UTC01R (Tretinoin); EC 1.14.14.1 (CYP26A1 protein, human); EC 1.14.14.1 (CYP26C1 protein, human); EC 1.14.14.1 (Cytochrome P450 Family 26); EC 1.14.14.1 (Retinoic Acid 4-Hydroxylase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160903
[St] Status:MEDLINE


  8 / 20 MEDLINE  
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[PMID]:27569851
[Au] Autor:Kasimanickam VR
[Ad] Endereço:Department of Veterinary Clinical Sciences, College of Veterinary Medicine, Washington State University, Pullman, WA, USA.
[Ti] Título:Expression of retinoic acid-metabolizing enzymes, ALDH1A1, ALDH1A2, ALDH1A3, CYP26A1, CYP26B1 and CYP26C1 in canine testis during post-natal development.
[So] Source:Reprod Domest Anim;51(6):901-909, 2016 Dec.
[Is] ISSN:1439-0531
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Mammalian spermatogenesis involves highly regulated temporal and spatial dynamics, carefully controlled by several signalling processes. Retinoic acid (RA) signalling could have a critical role in spermatogenesis by promoting spermatogonia differentiation, adhesion of germ cells to Sertoli cells, and release of mature spermatids. An optimal testicular RA concentration is maintained by retinaldehyde dehydrogenases (ALDHs), which oxidize RA precursors to produce RA, whereas the CYP26 class of enzymes catabolizes (oxidize) RA into inactive metabolites. The objective was to elucidate gene expression of these RA-metabolizing enzymes (ALDH1A1, ALDH1A2, ALDH1A3, CYP26A1, CYP26B1 and CYP26C1) and their protein presence in testes of young, peripubertal and adult dogs. Genes encoding RA-synthesizing isozymes ALDH1A1, ALDH1A2 and ALDH1A3 and RA-catabolizing isomers CYP26A1, CYP26B1 and CYP26C1 were expressed in testis at varying levels during testicular development from birth to adulthood in dogs. Based on detailed analyses of mRNA expression patterns, ALDH1A2 was regarded as a primary RA-synthesizing enzyme and CYP26B1 as a critical RA-hydrolysing enzyme; presumably, these genes have vital roles in maintaining RA homeostasis, which is imperative to spermatogenesis and other testicular functions in post-natal canine testis.
[Mh] Termos MeSH primário: Aldeído Desidrogenase/metabolismo
Família 26 do Citocromo P450/metabolismo
Cães/fisiologia
Regulação da Expressão Gênica no Desenvolvimento/fisiologia
Testículo/crescimento & desenvolvimento
Tretinoína/metabolismo
[Mh] Termos MeSH secundário: Aldeído Desidrogenase/classificação
Aldeído Desidrogenase/genética
Animais
Família 26 do Citocromo P450/genética
Regulação Enzimológica da Expressão Gênica
Masculino
Reação em Cadeia da Polimerase em Tempo Real/veterinária
Maturidade Sexual
Testículo/enzimologia
Testículo/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
5688UTC01R (Tretinoin); EC 1.14.14.1 (Cytochrome P450 Family 26); EC 1.2.1.3 (Aldehyde Dehydrogenase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170406
[Lr] Data última revisão:
170406
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160830
[St] Status:MEDLINE
[do] DOI:10.1111/rda.12756


  9 / 20 MEDLINE  
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[PMID]:26009309
[Au] Autor:Osanai M; Lee GH
[Ad] Endereço:Department of Pathology, Kochi University School of Medicine, Kohasu, Oko-cho, Nankoku, Kochi, 783-8505, Japan. osanaim@kochi-u.ac.jp.
[Ti] Título:Elevated expression of the retinoic acid-metabolizing enzyme CYP26C1 in primary breast carcinomas.
[So] Source:Med Mol Morphol;49(1):22-7, 2016 Mar.
[Is] ISSN:1860-1499
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Retinoic acid (RA)-metabolizing enzyme CYP26A1 has been shown to have increased expression levels in breast cancers and to effectively promote the survival of breast carcinoma cells, implying a potential oncogenic function. However, the expression of CYP26C1, another CYP26 family member, in primary breast carcinoma remains to be clarified. In the present study, we examined the expression of CYP26C1 by immunohistochemistry, using three different types of microarray, and observed strong cytoplasmic staining of CYP26C1 in 73 of the 219 (33.3 %) breast carcinomas. In contrast, CYP26C1 was not expressed in normal ductal and lobular cells in non-neoplastic tissue. Interestingly, increased expression of CYP26C1 was significantly associated with a high Ki-67 labeling index and a grade of tumor. However, CYP26C1 immunoreactivity was not associated with clinicopathological variables, including primary tumor status, lymph node involvement, distant metastasis, and tumor stage. In addition, CYP26C1 positivity was independent of the expression status of the hormone receptors and immunohistochemical surrogates for the intrinsic subtypes of breast cancer. This report is the first to demonstrate elevated expression of CYP26C1 in primary breast carcinomas. Based on the RA-catabolizing activity of CYP26C1, our data suggest that CYP26C1 expression may contribute to neoplasia in the breast.
[Mh] Termos MeSH primário: Neoplasias da Mama/metabolismo
Família 26 do Citocromo P450/metabolismo
[Mh] Termos MeSH secundário: Neoplasias da Mama/patologia
Feminino
Seres Humanos
Imuno-Histoquímica/métodos
Receptor ErbB-2/metabolismo
Análise Serial de Tecidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 1.14.14.1 (CYP26C1 protein, human); EC 1.14.14.1 (Cytochrome P450 Family 26); EC 2.7.10.1 (ERBB2 protein, human); EC 2.7.10.1 (Receptor, ErbB-2)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150527
[St] Status:MEDLINE
[do] DOI:10.1007/s00795-015-0110-7


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[PMID]:25966166
[Au] Autor:Xi J; Yue J; Yang Z
[Ad] Endereço:Department of Pharmacy, Wuhan University of Science and Technology School of Medicine, Hubei, China.
[Ti] Título:Expression profiles of retinoic acid synthetases ALDH1As and metabolic enzymes CYP26s in adult and embryonic zebrafish (Danio rerio).
[So] Source:Genet Mol Res;14(2):3948-56, 2015 Apr 27.
[Is] ISSN:1676-5680
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:Retinoic acid (RA) plays a crucial role in cellular proliferation, differentiation, and apoptosis. The physiological activity of RA begins early in development and continues throughout an organism's life. RA distribution is tightly controlled by the RA synthetases ALDH1As and the metabolic enzymes CYP26s. We analyzed the expressions of ALDH1As and CYP26s in whole embryos during zebrafish (Danio rerio) development and in adult zebrafish organs, by quantitative reverse transcriptase polymerase chain reaction analysis. All the ALDH1A and CYP26 genes exhibited similar pulse expression patterns, with peak expressions at different developmental stages. ALDH1A2 exhibited an earlier and sharper expression peak [12 hours post-fertilization (hpf)] than ALDH1A3 (24 hpf). CYP26A1 transcription peaked earlier (8 hpf) than CYP26B1 and CYP26C1 (12 hpf), while CYP26C1 expression dropped to basal levels later (48 hpf) than that of CYP26A1 and CYP26B1 (18 hpf). ALDH1A2 and CYP26A1 exhibited the highest mRNA peak level and seem to be the dominant isoenzymes in their families during zebrafish development. Expression patterns of ALDH1As and CYP26s in most adult zebrafish tissues were similar to those in humans. Nevertheless, three CYP26s were more vigorously expressed in the zebrafish brain than in human organs, whereas much weaker ALDH1A and CYP26 transcription was found in the zebrafish liver and intestine. This suggests that RA metabolic rates differ between zebrafish and humans or that other enzymes are responsible for RA homeostasis in the zebrafish liver and intestine. All the ALDH1A and CYP26 genes exhibited distinct expression patterns during zebrafish development and in adult zebrafish tissues.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica no Desenvolvimento
Tretinoína/metabolismo
Proteínas de Peixe-Zebra/genética
Peixe-Zebra/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Família 26 do Citocromo P450/genética
Feminino
Seres Humanos
Isoenzimas/genética
Masculino
Dados de Sequência Molecular
RNA Mensageiro/genética
Retinal Desidrogenase/genética
Alinhamento de Sequência
Peixe-Zebra/embriologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Isoenzymes); 0 (RNA, Messenger); 0 (Zebrafish Proteins); 5688UTC01R (Tretinoin); EC 1.14.14.1 (Cytochrome P450 Family 26); EC 1.2.1.- (aldehyde dehydrogenase 1); EC 1.2.1.36 (Retinal Dehydrogenase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170417
[Lr] Data última revisão:
170417
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150513
[St] Status:MEDLINE
[do] DOI:10.4238/2015.April.27.9



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