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Pesquisa : D08.811.682.662.640 [Categoria DeCS]
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[PMID]:28942439
[Au] Autor:Zareba I; Surazynski A; Chrusciel M; Miltyk W; Doroszko M; Rahman N; Palka J
[Ad] Endereço:Department of Medicinal Chemistry, Medical University of Bialystok, Bialystok, Poland.
[Ti] Título:Functional Consequences of Intracellular Proline Levels Manipulation Affecting PRODH/POX-Dependent Pro-Apoptotic Pathways in a Novel in Vitro Cell Culture Model.
[So] Source:Cell Physiol Biochem;43(2):670-684, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: The effect of impaired intracellular proline availability for proline dehydrogenase/proline oxidase (PRODH/POX)-dependent apoptosis was studied. METHODS: We generated a constitutively knocked-down PRODH/POX MCF-7 breast cancer cell line (MCF-7shPRODH/POX) as a model to analyze the functional consequences of impaired intracellular proline levels. We have used inhibitor of proline utilization in collagen biosynthesis, 2-metoxyestradiol (MOE), inhibitor of prolidase that generate proline, rapamycin (Rap) and glycyl-proline (GlyPro), substrate for prolidase. Collagen and DNA biosynthesis were evaluated by radiometric assays. Cell viability was determined using Nucleo-Counter NC-3000. The activity of prolidase was determined by colorimetric assay. Expression of proteins was assessed by Western blot and immunofluorescence bioimaging. Concentration of proline was analyzed by liquid chromatography with mass spectrometry. RESULTS: PRODH/POX knockdown decreased DNA and collagen biosynthesis, whereas increased prolidase activity and intracellular proline level in MCF-7shPRODH/POX cells. All studied compounds decreased cell viability in MCF-7 and MCF-7shPRODH/POX cells. DNA biosynthesis was similarly inhibited by Rap and MOE in both cell lines, but GlyPro inhibited the process only in MCF-7shPRODH/POX and MOE+GlyPro only in MCF-7 cells. All the compounds inhibited collagen biosynthesis, increased prolidase activity and cytoplasmic proline level in MCF-7shPRODH/POX cells and contributed to the induction of pro-survival mode only in MCF-7shPRODH/POX cells. In contrast, all studied compounds upregulated expression of pro-apoptotic protein only in MCF-7 cells. CONCLUSION: PRODH/POX was confirmed as a driver of apoptosis and proved the eligibility of MCF-7shPRODH/POX cell line as a highly effective model to elucidate the different mechanisms underlying proline utilization or generation in PRODH/POX-dependent pro-apoptotic pathways.
[Mh] Termos MeSH primário: Apoptose
Prolina Oxidase/metabolismo
Prolina/metabolismo
[Mh] Termos MeSH secundário: Neoplasias da Mama/genética
Neoplasias da Mama/metabolismo
Técnicas de Cultura de Células
Proliferação Celular
Sobrevivência Celular
Colágeno/metabolismo
Feminino
Seres Humanos
Células MCF-7
Prolina Oxidase/genética
Interferência de RNA
RNA Interferente Pequeno/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Small Interfering); 9007-34-5 (Collagen); 9DLQ4CIU6V (Proline); EC 1.5.3.- (Proline Oxidase); EC 1.5.5.2 (PRODH protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170925
[St] Status:MEDLINE
[do] DOI:10.1159/000480653


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[PMID]:28712849
[Au] Autor:Liu LK; Becker DF; Tanner JJ
[Ad] Endereço:Department of Biochemistry, University of Missouri, Columbia, MO, 65211, United States.
[Ti] Título:Structure, function, and mechanism of proline utilization A (PutA).
[So] Source:Arch Biochem Biophys;632:142-157, 2017 Oct 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proline has important roles in multiple biological processes such as cellular bioenergetics, cell growth, oxidative and osmotic stress response, protein folding and stability, and redox signaling. The proline catabolic pathway, which forms glutamate, enables organisms to utilize proline as a carbon, nitrogen, and energy source. FAD-dependent proline dehydrogenase (PRODH) and NAD -dependent glutamate semialdehyde dehydrogenase (GSALDH) convert proline to glutamate in two sequential oxidative steps. Depletion of PRODH and GSALDH in humans leads to hyperprolinemia, which is associated with mental disorders such as schizophrenia. Also, some pathogens require proline catabolism for virulence. A unique aspect of proline catabolism is the multifunctional proline utilization A (PutA) enzyme found in Gram-negative bacteria. PutA is a large (>1000 residues) bifunctional enzyme that combines PRODH and GSALDH activities into one polypeptide chain. In addition, some PutAs function as a DNA-binding transcriptional repressor of proline utilization genes. This review describes several attributes of PutA that make it a remarkable flavoenzyme: (1) diversity of oligomeric state and quaternary structure; (2) substrate channeling and enzyme hysteresis; (3) DNA-binding activity and transcriptional repressor function; and (4) flavin redox dependent changes in subcellular location and function in response to proline (functional switching).
[Mh] Termos MeSH primário: 1-Pirrolina-5-Carboxilato Desidrogenase/química
Proteínas de Bactérias/química
Flavoproteínas/química
Bactérias Gram-Negativas/enzimologia
Proteínas de Membrana/química
Prolina Oxidase/química
[Mh] Termos MeSH secundário: 1-Pirrolina-5-Carboxilato Desidrogenase/deficiência
1-Pirrolina-5-Carboxilato Desidrogenase/genética
1-Pirrolina-5-Carboxilato Desidrogenase/metabolismo
Erros Inatos do Metabolismo dos Aminoácidos
Animais
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Flavina-Adenina Dinucleotídeo/química
Flavina-Adenina Dinucleotídeo/genética
Flavina-Adenina Dinucleotídeo/metabolismo
Flavoproteínas/genética
Flavoproteínas/metabolismo
Seres Humanos
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Prolina/química
Prolina/genética
Prolina/metabolismo
Prolina Oxidase/genética
Prolina Oxidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Flavoproteins); 0 (Membrane Proteins); 0 (PutA protein, Bacteria); 146-14-5 (Flavin-Adenine Dinucleotide); 9DLQ4CIU6V (Proline); EC 1.2.1.88 (1-Pyrroline-5-Carboxylate Dehydrogenase); EC 1.5.3.- (Proline Oxidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170718
[St] Status:MEDLINE


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[PMID]:28558236
[Au] Autor:Moxley MA; Zhang L; Christgen S; Tanner JJ; Becker DF
[Ad] Endereço:Department of Biochemistry, Redox Biology Center, University of Nebraska-Lincoln , Lincoln, Nebraska 68588, United States.
[Ti] Título:Identification of a Conserved Histidine As Being Critical for the Catalytic Mechanism and Functional Switching of the Multifunctional Proline Utilization A Protein.
[So] Source:Biochemistry;56(24):3078-3088, 2017 Jun 20.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proline utilization A from Escherichia coli (EcPutA) is a multifunctional flavoenzyme that oxidizes proline to glutamate through proline dehydrogenase (PRODH) and Δ -pyrroline-5-carboxylate dehydrogenase (P5CDH) activities, while also switching roles as a DNA-bound transcriptional repressor and a membrane-bound catabolic enzyme. This phenomenon, termed functional switching, occurs through a redox-mediated mechanism in which flavin reduction triggers a conformational change that increases EcPutA membrane binding affinity. Structural studies have shown that reduction of the FAD cofactor causes the ribityl moiety to undergo a crankshaft motion, indicating that the orientation of the ribityl chain is a key element of PutA functional switching. Here, we test the role of a conserved histidine that bridges from the FAD pyrophosphate to the backbone amide of a conserved leucine residue in the PRODH active site. An EcPutA mutant (H487A) was characterized by steady-state and rapid-reaction kinetics, and cell-based reporter gene experiments. The catalytic activity of H487A is severely diminished (>50-fold) with membrane vesicles as the electron acceptor, and H487A exhibits impaired lipid binding and in vivo transcriptional repressor activity. Rapid-reaction kinetic experiments demonstrate that H487A is 3-fold slower than wild-type EcPutA in a conformational change step following reduction of the FAD cofactor. Furthermore, the reduction potential (E ) of H487A is ∼40 mV more positive than that of wild-type EcPutA, and H487A has an attenuated ability to catalyze the reverse PRODH chemical step of reoxidation by P5C. In this process, significant red semiquinone forms in contrast to the same reaction with wild-type EcPutA, in which facile two-electron reoxidation occurs without the formation of a measurable amount of semiquinone. These results indicate that His487 is critically important for the proline/P5C chemical step, conformational change kinetics, and functional switching in EcPutA.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Biocatálise
Sequência Conservada
Histidina/análise
Histidina/metabolismo
Proteínas de Membrana/química
Proteínas de Membrana/metabolismo
Enzimas Multifuncionais/química
Enzimas Multifuncionais/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Bactérias/genética
Escherichia coli/química
Escherichia coli/genética
Escherichia coli/metabolismo
Cinética
Proteínas de Membrana/genética
Modelos Moleculares
Enzimas Multifuncionais/genética
Prolina Oxidase/química
Prolina Oxidase/genética
Prolina Oxidase/metabolismo
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Membrane Proteins); 0 (Multifunctional Enzymes); 0 (PutA protein, Bacteria); 4QD397987E (Histidine); EC 1.5.3.- (Proline Oxidase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170531
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00046


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[PMID]:28264926
[Au] Autor:Nagano T; Nakashima A; Onishi K; Kawai K; Awai Y; Kinugasa M; Iwasaki T; Kikkawa U; Kamada S
[Ad] Endereço:Division of Signal Pathways, Biosignal Research Center, Kobe University, 1-1 Rokkodai-cho, Nada-ku, Kobe 657-8501, Japan.
[Ti] Título:Proline dehydrogenase promotes senescence through the generation of reactive oxygen species.
[So] Source:J Cell Sci;130(8):1413-1420, 2017 Apr 15.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cellular senescence is a complex stress response characterized by permanent loss of proliferative capacity and is implicated in age-related disorders. Although the transcriptional activity of p53 (encoded by ) is known to be vital for senescence induction, the downstream effector genes critical for senescence remain unsolved. Recently, we have identified the proline dehydrogenase gene ( ) to be upregulated specifically in senescent cells in a p53-dependent manner, and the functional relevance of this to senescence is yet to be defined. Here, we conducted functional analyses to explore the relationship between PRODH and the senescence program. We found that genetic and pharmacological inhibition of PRODH suppressed senescent phenotypes induced by DNA damage. Furthermore, ectopic expression of wild-type PRODH, but not enzymatically inactive forms, induced senescence associated with the increase in reactive oxygen species (ROS) and the accumulation of DNA damage. Treatment with N-acetyl-L-cysteine, a ROS scavenger, prevented senescence induced by PRODH overexpression. These results indicate that PRODH plays a causative role in DNA damage-induced senescence through the enzymatic generation of ROS.
[Mh] Termos MeSH primário: Senescência Celular
Fibroblastos/fisiologia
Prolina Oxidase/metabolismo
Espécies Reativas de Oxigênio/metabolismo
[Mh] Termos MeSH secundário: Acetilcisteína/farmacologia
Linhagem Celular
Senescência Celular/efeitos dos fármacos
Senescência Celular/genética
Dano ao DNA/efeitos dos fármacos
Dano ao DNA/genética
Fibroblastos/efeitos dos fármacos
Furanos/farmacologia
Seres Humanos
Prolina Oxidase/genética
RNA Interferente Pequeno/genética
Transgenes/genética
Proteína Supressora de Tumor p53/genética
Proteína Supressora de Tumor p53/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Furans); 0 (RNA, Small Interfering); 0 (Reactive Oxygen Species); 0 (Tumor Suppressor Protein p53); EC 1.5.3.- (Proline Oxidase); WYQ7N0BPYC (Acetylcysteine); XD95821VF9 (tetrahydrofurfuryl alcohol)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170308
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.196469


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[PMID]:28183913
[Au] Autor:Levin BJ; Huang YY; Peck SC; Wei Y; Martínez-Del Campo A; Marks JA; Franzosa EA; Huttenhower C; Balskus EP
[Ad] Endereço:Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, MA 02138, USA.
[Ti] Título:A prominent glycyl radical enzyme in human gut microbiomes metabolizes -4-hydroxy-l-proline.
[So] Source:Science;355(6325), 2017 02 10.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The human microbiome encodes vast numbers of uncharacterized enzymes, limiting our functional understanding of this community and its effects on host health and disease. By incorporating information about enzymatic chemistry into quantitative metagenomics, we determined the abundance and distribution of individual members of the glycyl radical enzyme superfamily among the microbiomes of healthy humans. We identified many uncharacterized family members, including a universally distributed enzyme that enables commensal gut microbes and human pathogens to dehydrate -4-hydroxy-l-proline, the product of the most abundant human posttranslational modification. This "chemically guided functional profiling" workflow can therefore use ecological context to facilitate the discovery of enzymes in microbial communities.
[Mh] Termos MeSH primário: Microbioma Gastrointestinal/genética
Trato Gastrointestinal/microbiologia
Hidroxiprolina/metabolismo
Prolina Oxidase/química
Prolina Oxidase/genética
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Anaerobiose
Seres Humanos
Metagenoma
Prolina Oxidase/metabolismo
Propanodiol Desidratase/química
Propanodiol Desidratase/genética
Processamento de Proteína Pós-Traducional
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 1.5.3.- (Proline Oxidase); EC 4.2.1.28 (Propanediol Dehydratase); RMB44WO89X (Hydroxyproline)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170211
[St] Status:MEDLINE


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[PMID]:27761680
[Au] Autor:Sakamoto H; Komatsu T; Yamasaki K; Satomura T; Suye SI
[Ad] Endereço:Tenure-Track Program for Innovation Research, University of Fukui, Fukui, Japan.
[Ti] Título:Design of a multi-enzyme reaction on an electrode surface for an L-glutamate biofuel anode.
[So] Source:Biotechnol Lett;39(2):235-240, 2017 Feb.
[Is] ISSN:1573-6776
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:OBJECTIVES: To design and construct a novel bio-anode electrode based on the oxidation of glutamic acid to produce 2-oxoglutarate, generating two electrons from NADH. RESULTS: Efficient enzyme reaction and electron transfer were observed owing to immobilization of the two enzymes using a mixed self-assembled monolayer. The ratio of the immobilized enzymes was an important factor affecting the efficiency of the system; thus, we quantified the amounts of immobilized enzyme using a quartz crystal microbalance to further evaluate the electrochemical reaction. The electrochemical reaction proceeded efficiently when approximately equimolar amounts of the enzyme were on the electrode. The largest oxidation peak current increase (171 nA) was observed under these conditions. CONCLUSION: Efficient multi-enzyme reaction on the electrode surface has been achieved which is applicable for biofuel cell application.
[Mh] Termos MeSH primário: Biocombustíveis
Eletrodos
Enzimas Imobilizadas/metabolismo
Ácido Glutâmico/metabolismo
[Mh] Termos MeSH secundário: Fontes de Energia Bioelétrica
Carbono/metabolismo
NADH Desidrogenase/metabolismo
Prolina Oxidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biofuels); 0 (Enzymes, Immobilized); 0 (pyrolytic carbon); 3KX376GY7L (Glutamic Acid); 7440-44-0 (Carbon); EC 1.5.3.- (Proline Oxidase); EC 1.6.99.3 (NADH Dehydrogenase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170308
[Lr] Data última revisão:
170308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161021
[St] Status:MEDLINE
[do] DOI:10.1007/s10529-016-2237-6


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[PMID]:27512016
[Au] Autor:Shinde S; Villamor JG; Lin W; Sharma S; Verslues PE
[Ad] Endereço:Institute of Plant and Microbial Biology, Academia Sinica, Taipei 115, Taiwan.
[Ti] Título:Proline Coordination with Fatty Acid Synthesis and Redox Metabolism of Chloroplast and Mitochondria.
[So] Source:Plant Physiol;172(2):1074-1088, 2016 Oct.
[Is] ISSN:1532-2548
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proline (Pro) accumulation is one of the most prominent changes in plant metabolism during drought and low water potential; however, the regulation and function of Pro metabolism remain unclear. We used a combination of forward genetic screening based on a Proline Dehydrogenase1 (PDH1) promoter-luciferase reporter (PDH1 :LUC2) and RNA sequencing of the Pro synthesis mutant p5cs1-4 to identify multiple loci affecting Pro accumulation in Arabidopsis (Arabidopsis thaliana). Two mutants having high PDH1 :LUC2 expression and increased Pro accumulation at low water potential were found to be alleles of Cytochrome P450, Family 86, Subfamily A, Polypeptide2 (CYP86A2) and Long Chain Acyl Synthetase2 (LACS2), which catalyze two successive steps in very-long-chain fatty acid (VLCFA) synthesis. Reverse genetic experiments found additional VLCFA and lipid metabolism-related mutants with increased Pro accumulation. Altered cellular redox status is a key factor in the coordination of Pro and VLCFA metabolism. The NADPH oxidase inhibitor diphenyleneiodonium (DPI) induced high levels of Pro accumulation and strongly repressed PDH1 :LUC2 expression. cyp86a2 and lacs2 mutants were hypersensitive to diphenyleneiodonium but could be reverted to wild-type Pro and PDH1 :LUC2 expression by reactive oxygen species scavengers. The coordination of Pro and redox metabolism also was indicated by the altered expression of chloroplast and mitochondria electron transport genes in p5cs1-4 These results show that Pro metabolism is both influenced by and influences cellular redox status via previously unknown coordination with several metabolic pathways. In particular, Pro and VLCFA synthesis share dual roles to help buffer cellular redox status while producing products useful for stress resistance, namely the compatible solute Pro and cuticle lipids.
[Mh] Termos MeSH primário: Arabidopsis/metabolismo
Cloroplastos/metabolismo
Ácidos Graxos/biossíntese
Mitocôndrias/metabolismo
Prolina/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/genética
Proteínas de Arabidopsis/genética
Proteínas de Arabidopsis/metabolismo
Coenzima A Ligases/genética
Coenzima A Ligases/metabolismo
Sistema Enzimático do Citocromo P-450/genética
Sistema Enzimático do Citocromo P-450/metabolismo
Perfilação da Expressão Gênica/métodos
Regulação da Expressão Gênica de Plantas/efeitos dos fármacos
Luciferases/genética
Luciferases/metabolismo
Mutação
Oniocompostos/farmacologia
Oxirredução
Plantas Geneticamente Modificadas
Prolina Oxidase/genética
Regiões Promotoras Genéticas/genética
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Água/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Fatty Acids); 0 (Onium Compounds); 059QF0KO0R (Water); 6HJ411TU98 (diphenyleneiodonium); 9035-51-2 (Cytochrome P-450 Enzyme System); 9DLQ4CIU6V (Proline); EC 1.13.12.- (Luciferases); EC 1.14.99.- (CYP86A8 protein, Arabidopsis); EC 1.5.3.- (PDH1 protein, Arabidopsis); EC 1.5.3.- (Proline Oxidase); EC 6.2.1.- (Coenzyme A Ligases); EC 6.2.1.- (LACS2 protein, Arabidopsis)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160812
[St] Status:MEDLINE


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[PMID]:27303048
[Au] Autor:Cabassa-Hourton C; Schertl P; Bordenave-Jacquemin M; Saadallah K; Guivarc'h A; Lebreton S; Planchais S; Klodmann J; Eubel H; Crilat E; Lefebvre-De Vos D; Ghelis T; Richard L; Abdelly C; Carol P; Braun HP; Savouré A
[Ad] Endereço:Sorbonne Universités, UPMC Univ Paris 06, iEES, UMR 7618, UPMC Paris 06-Sorbonne (UPEC, UPMC, CNRS, IRD, INRA, Paris Diderot), case 237, 4 place Jussieu, F-75252 Paris cedex 05, France.
[Ti] Título:Proteomic and functional analysis of proline dehydrogenase 1 link proline catabolism to mitochondrial electron transport in Arabidopsis thaliana.
[So] Source:Biochem J;473(17):2623-34, 2016 Sep 01.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Proline accumulates in many plant species in response to environmental stresses. Upon relief from stress, proline is rapidly oxidized in mitochondria by proline dehydrogenase (ProDH) and then by pyrroline-5-carboxylate dehydrogenase (P5CDH). Two ProDH genes have been identified in the genome of the model plant Arabidopsis thaliana To gain a better understanding of ProDH1 functions in mitochondria, proteomic analysis was performed. ProDH1 polypeptides were identified in Arabidopsis mitochondria by immunoblotting gels after 2D blue native (BN)-SDS/PAGE, probing them with an anti-ProDH antibody and analysing protein spots by MS. The 2D gels showed that ProDH1 forms part of a low-molecular-mass (70-140 kDa) complex in the mitochondrial membrane. To evaluate the contribution of each isoform to proline oxidation, mitochondria were isolated from wild-type (WT) and prodh1, prodh2, prodh1prodh2 and p5cdh mutants. ProDH activity was high for genotypes in which ProDH, most likely ProDH1, was strongly induced by proline. Respiratory measurements indicate that ProDH1 has a role in oxidizing excess proline and transferring electrons to the respiratory chain.
[Mh] Termos MeSH primário: Arabidopsis/metabolismo
Transporte de Elétrons
Mitocôndrias/metabolismo
Prolina Oxidase/metabolismo
Prolina/metabolismo
Proteoma
[Mh] Termos MeSH secundário: Arabidopsis/enzimologia
Eletroforese em Gel de Poliacrilamida
Espectrometria de Massas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Proteome); 9DLQ4CIU6V (Proline); EC 1.5.3.- (Proline Oxidase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170620
[Lr] Data última revisão:
170620
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160616
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20160314


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[PMID]:27040799
[Au] Autor:Zareba I; Palka J
[Ad] Endereço:Department of Medicinal Chemistry, Medical University of Bialystok, Bialystok, Poland.
[Ti] Título:Prolidase-proline dehydrogenase/proline oxidase-collagen biosynthesis axis as a potential interface of apoptosis/autophagy.
[So] Source:Biofactors;42(4):341-8, 2016 Jul 08.
[Is] ISSN:1872-8081
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Prolidase is a cytosolic imidodipeptidase that specifically splits imidodipeptides with C-terminal proline or hydroxyproline. The enzyme plays an important role in the recycling of proline from imidodipeptides for resynthesis of collagen and other proline-containing proteins. The mechanism of prolidase-dependent regulation of collagen biosynthesis was found at both transcriptional and post-transcriptional level. The increase in the enzyme activity is due to its phosphorylation on serine/threonine residues. Prolidase-dependent transcriptional regulation of collagen biosynthesis was found at the level of NF-κB, known inhibitor of type I collagen gene expression. Proline dehydrogenase/proline oxidase (PRODH/POX) is flavin-dependent enzyme associated with the inner mitochondrial membrane. The enzyme catalyzes conversion of proline into Δ(1) -pyrroline-5-carboxylate (P5C), during which reactive oxygen species (ROS) are produced, inducing intrinsic and extrinsic apoptotic pathways. Alternatively, under low glucose stress, PRODH/POX activation produces ATP for energy supply and survival. Of special interest is that PRODH/POX gene is induced by P53 and peroxisome proliferator-activated gamma receptor (PPARγ). Among down-regulators of PRODH/POX is an oncogenic transcription factor c-MYC and miR-23b*. On the other hand, PRODH/POX suppresses HIF-1α transcriptional activity, the MAPK pathway, cyclooxygenase-2, epidermal growth factor receptor and Wnt/b-catenin signaling. PRODH/POX expression is often down-regulated in various tumors, limiting mitochondrial proline utilization to P5C. It is accompanied by increased cytoplasmic level of proline. Proline availability for PRODH/POX-dependent ATP or ROS generation depends on activity of prolidase and utilization of proline in process of collagen biosynthesis. Therefore, Prolidase-PRODH/POX-Collagen Biosynthesis axis may represent potential interface that regulate apoptosis and survival. © 2016 BioFactors, 42(4):341-348, 2016.
[Mh] Termos MeSH primário: Apoptose
Autofagia
Colágeno/biossíntese
Dipeptidases/fisiologia
Prolina Oxidase/fisiologia
[Mh] Termos MeSH secundário: Animais
Vias Biossintéticas
Seres Humanos
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
9007-34-5 (Collagen); EC 1.5.3.- (Proline Oxidase); EC 3.4.13.- (Dipeptidases); EC 3.4.13.9 (proline dipeptidase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170123
[Lr] Data última revisão:
170123
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160405
[St] Status:MEDLINE
[do] DOI:10.1002/biof.1283


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[PMID]:26995311
[Au] Autor:Li M; Ashraf U; Tian H; Mo Z; Pan S; Anjum SA; Duan M; Tang X
[Ad] Endereço:Department of Ecology, College of Natural Resources and Environment, South China Agricultural University, Guangzhou, 510642, PR China; Department of Crop Science and Technology, College of Agriculture, South China Agricultural University, Guangzhou, 510642, PR China; Scientific Observing and Experim
[Ti] Título:Manganese-induced regulations in growth, yield formation, quality characters, rice aroma and enzyme involved in 2-acetyl-1-pyrroline biosynthesis in fragrant rice.
[So] Source:Plant Physiol Biochem;103:167-75, 2016 Jun.
[Is] ISSN:1873-2690
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Micro-nutrient application is essential for normal plant growth while a little is known about manganese (Mn)-induced regulations in morpho-physiological attributes, aroma formation and enzyme involved in 2-acetyl-1-pyrroline (2-AP) biosynthesis in aromatic rice. Present study aimed to examine the influence of four levels of Mn i.e., Mn1 (100 mg MnSO4 pot(-1)), Mn2 (150 mg MnSO4 pot(-1)), Mn3 (200 mg MnSO4 pot(-1)), and Mn4 (250 mg MnSO4 pot(-1)) on the growth, yield formation, quality characters, rice aroma and enzyme involved in 2-acetyl-1-pyrroline biosynthesis in two fragrant rice cultivars i.e., Meixiangzhan and Nongxiang 18. Pots without Mn application were served as control (Ck). Each pot contained 15 kg of soil. Effects on agronomic characters, quality attributes, 2-AP contents and enzymes involved in 2-AP biosynthesis have been studied in early and late season rice. Results depicted that Mn improved rice growth, yield and related characters, and some quality attributes significantly. It further up-regulated proline, pyrroline-5-carboxylic acid (P5C) (precursors of 2-AP), soluble proteins and activities of proline dehydrogenase (ProDH), Δ(1) pyrroline-5-carboxylic acid synthetase (P5CS) ornithine aminotransferase (OAT) that led to enhanced 2-AP production in rice grains. Moreover, higher Mn levels resulted in increased grain Mn contents in both rice cultivars. Along with growth and yield improvement, Mn application significantly improved rice aromatic contents. Overall, Nongxiang 18 accumulated more 2-AP contents than Meixiangzhan in both seasons under Mn application. This study further explored the importance of Mn in rice aroma formation and signifies that micro-nutrients can play significant roles in rice aroma synthesis; however, intensive studies at molecular levels are still needed to understand the exact mechanisms of Mn to improve rice aroma formation.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica de Plantas/efeitos dos fármacos
Manganês/farmacologia
Oryza/efeitos dos fármacos
Proteínas de Plantas/metabolismo
Pirróis/metabolismo
[Mh] Termos MeSH secundário: Ornitina-Oxo-Ácido Transaminase/genética
Ornitina-Oxo-Ácido Transaminase/metabolismo
Oryza/enzimologia
Oryza/fisiologia
Proteínas de Plantas/genética
Prolina/metabolismo
Prolina Oxidase/genética
Prolina Oxidase/metabolismo
Sementes/efeitos dos fármacos
Sementes/enzimologia
Sementes/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Plant Proteins); 0 (Pyrroles); 2906-39-0 (delta-1-pyrroline-5-carboxylate); 42Z2K6ZL8P (Manganese); 9DLQ4CIU6V (Proline); EC 1.5.3.- (Proline Oxidase); EC 2.6.1.13 (Ornithine-Oxo-Acid Transaminase); IGC0W6LY94 (2-acetyl-1-pyrroline)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160321
[St] Status:MEDLINE



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