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Pesquisa : D08.811.913.696.650.025 [Categoria DeCS]
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  1 / 2706 MEDLINE  
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[PMID]:29293500
[Au] Autor:Márton J; Fodor T; Nagy L; Vida A; Kis G; Brunyánszki A; Antal M; Lüscher B; Bai P
[Ad] Endereço:Department of Medical Chemistry, Faculty of Medicine, University of Debrecen, Debrecen, Hungary.
[Ti] Título:PARP10 (ARTD10) modulates mitochondrial function.
[So] Source:PLoS One;13(1):e0187789, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Poly(ADP-ribose) polymerase (PARP)10 is a PARP family member that performs mono-ADP-ribosylation of target proteins. Recent studies have linked PARP10 to metabolic processes and metabolic regulators that prompted us to assess whether PARP10 influences mitochondrial oxidative metabolism. The depletion of PARP10 by specific shRNAs increased mitochondrial oxidative capacity in cellular models of breast, cervical, colorectal and exocrine pancreas cancer. Upon silencing of PARP10, mitochondrial superoxide production decreased in line with increased expression of antioxidant genes pointing out lower oxidative stress upon PARP10 silencing. Improved mitochondrial oxidative capacity coincided with increased AMPK activation. The silencing of PARP10 in MCF7 and CaCo2 cells decreased the proliferation rate that correlated with increased expression of anti-Warburg enzymes (Foxo1, PGC-1α, IDH2 and fumarase). By analyzing an online database we showed that lower PARP10 expression increases survival in gastric cancer. Furthermore, PARP10 expression decreased upon fasting, a condition that is characterized by increases in mitochondrial biogenesis. Finally, lower PARP10 expression is associated with increased fatty acid oxidation.
[Mh] Termos MeSH primário: Mitocôndrias/fisiologia
Poli(ADP-Ribose) Polimerases/metabolismo
Proteínas Proto-Oncogênicas/metabolismo
[Mh] Termos MeSH secundário: Adenilato Quinase/metabolismo
Animais
Western Blotting
Linhagem Celular
Proliferação Celular/fisiologia
Eletroforese em Gel de Poliacrilamida
Inativação Gênica
Seres Humanos
Masculino
Camundongos Endogâmicos C57BL
Oxirredução
Estresse Oxidativo
Consumo de Oxigênio
Poli(ADP-Ribose) Polimerases/genética
Proteínas Proto-Oncogênicas/genética
Reação em Cadeia da Polimerase em Tempo Real
Reação em Cadeia da Polimerase Via Transcriptase Reversa
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Proto-Oncogene Proteins); EC 2.4.2.30 (PARP10 protein, human); EC 2.4.2.30 (Poly(ADP-ribose) Polymerases); EC 2.7.4.3 (Adenylate Kinase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180103
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0187789


  2 / 2706 MEDLINE  
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[PMID]:29240752
[Au] Autor:Miao Z; Zhang G; Zhang J; Li J; Yang Y
[Ad] Endereço:College of Animal Science and Veterinary Medicine, Shanxi Agricultural University, Shanxi, China.
[Ti] Título:Effect of early dietary energy restriction and phosphorus level on subsequent growth performance, intestinal phosphate transport, and AMPK activity in young broilers.
[So] Source:PLoS One;12(12):e0186828, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We aimed to determine the effect of low dietary energy on intestinal phosphate transport and the possible underlying mechanism to explain the long-term effects of early dietary energy restriction and non-phytate phosphorus (NPP). A 2 × 3 factorial experiment, consisting of 2 energy levels and 3 NPP levels, was conducted. Broiler growth performance, intestinal morphology in 0-21 days and 22-35 days, type IIb sodium-phosphate co-transporter (NaPi-IIb) mRNA expression, adenylate purine concentrations in the duodenum, and phosphorylated adenosine monophosphate-activated protein kinase (AMPK-α) activity in 0-21 days were determined. The following results were obtained. (1) Low dietary energy (LE) induced a high feed conversion ratio (FCR) and significantly decreased body weight gain in young broilers, but LE induced significantly higher compensatory growth in low NPP (LP) groups than in the high or medium NPP groups (HP and MP). (2) LE decreased the villus height (VH) in the intestine, and LE-HP resulted in the lowest crypt depth (CD) and the highest VH:CD ratio in the initial phase. However, in the later period, the LE-LP group showed an increased VH:CD ratio and decreased CD in the intestine. (3) LE increased ATP synthesis and decreased AMP:ATP ratio in the duodenal mucosa of chickens in 0-21 days, and LP diet increased ATP synthesis and adenylate energy charges but decreased AMP production and AMP:ATP ratio. (4) LE led to weaker AMPK phosphorylation, higher mTOR phosphorylation, and higher NaPi-IIb mRNA expression. Thus, LE and LP in the early growth phase had significant compensatory and interactive effect on later growth and intestinal development in broilers. The effect might be relevant to energy status that LE leads to weaker AMPK phosphorylation, causing a lower inhibitory action toward mTOR phosphorylation. This series of events stimulates NaPi-IIb mRNA expression. Our findings provide a theoretical basis and a new perspective on intestinal phosphate transport regulation, with potential applications in broiler production.
[Mh] Termos MeSH primário: Adenilato Quinase/metabolismo
Galinhas/crescimento & desenvolvimento
Ingestão de Energia
Intestinos/metabolismo
Fósforo/administração & dosagem
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/biossíntese
Animais
Transporte Biológico
Galinhas/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Reação em Cadeia da Polimerase Via Transcriptase Reversa
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
27YLU75U4W (Phosphorus); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.4.3 (Adenylate Kinase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171215
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186828


  3 / 2706 MEDLINE  
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[PMID]:29324783
[Au] Autor:Ramesh S; Govindarajulu M; Lynd T; Briggs G; Adamek D; Jones E; Heiner J; Majrashi M; Moore T; Amin R; Suppiramaniam V; Dhanasekaran M
[Ad] Endereço:Department of Drug Discovery and Development, Harrison School of Pharmacy, Auburn University, Auburn, AL, United States of America.
[Ti] Título:SIRT3 activator Honokiol attenuates ß-Amyloid by modulating amyloidogenic pathway.
[So] Source:PLoS One;13(1):e0190350, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Honokiol (poly-phenolic lignan from Magnolia grandiflora) is a Sirtuin-3 (SIRT3) activator which exhibit antioxidant activity and augment mitochondrial functions in several experimental models. Modern evidence suggests the critical role of SIRT3 in the progression of several metabolic and neurodegenerative diseases. Amyloid beta (Aß), the precursor to extracellular senile plaques, accumulates in the brains of patients with Alzheimer's disease (AD) and is related to the development of cognitive impairment and neuronal cell death. Aß is generated from amyloid-ß precursor protein (APP) through sequential cleavages, first by ß-secretase and then by γ-secretase. Drugs modulating this pathway are believed to be one of the most promising strategies for AD treatment. In the present study, we found that Honokiol significantly enhanced SIRT3 expression, reduced reactive oxygen species generation and lipid peroxidation, enhanced antioxidant activities, and mitochondrial function thereby reducing Aß and sAPPß levels in Chinese Hamster Ovarian (CHO) cells (carrying the amyloid precursor protein-APP and Presenilin PS1 mutation). Mechanistic studies revealed that Honokiol affects neither protein levels of APP nor α-secretase activity. In contrast, Honokiol increased the expression of AMPK, CREB, and PGC-1α, thereby inhibiting ß-secretase activity leading to reduced Aß levels. These results suggest that Honokiol is an activator of SIRT3 capable of improving antioxidant activity, mitochondrial energy regulation, while decreasing Aß, thereby indicating it to be a lead compound for AD drug development.
[Mh] Termos MeSH primário: Peptídeos beta-Amiloides/metabolismo
Compostos de Bifenilo/farmacologia
Lignanas/farmacologia
Sirtuína 3/efeitos dos fármacos
[Mh] Termos MeSH secundário: Adenilato Quinase/metabolismo
Animais
Células CHO
Cricetulus
Proteína de Ligação ao Elemento de Resposta ao AMP Cíclico/metabolismo
Seres Humanos
Peroxidação de Lipídeos/efeitos dos fármacos
Mitocôndrias/efeitos dos fármacos
Mitocôndrias/metabolismo
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amyloid beta-Peptides); 0 (Biphenyl Compounds); 0 (Cyclic AMP Response Element-Binding Protein); 0 (Lignans); 0 (Reactive Oxygen Species); 11513CCO0N (honokiol); EC 2.7.4.3 (Adenylate Kinase); EC 3.5.1.- (SIRT3 protein, human); EC 3.5.1.- (Sirtuin 3)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180206
[Lr] Data última revisão:
180206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190350


  4 / 2706 MEDLINE  
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[PMID]:28466023
[Au] Autor:Yao F; Zhang M; Chen L
[Ad] Endereço:Department of Pharmacology, College of Basic Medical Sciences, Jilin University, Changchun 130021, China.
[Ti] Título:Adipose Tissue-Specialized Immunologic Features Might Be the Potential Therapeutic Target of Prospective Medicines for Obesity.
[So] Source:J Diabetes Res;2017:4504612, 2017.
[Is] ISSN:2314-6753
[Cp] País de publicação:Egypt
[La] Idioma:eng
[Ab] Resumo:Excessive lipid accumulation in adipose tissue is either the source of obesity or the cause and result of chronic local inflammation, and recent studies indicate that the accumulation may induce many other specialized immunologic features with macrophages and epidemic diseases. We analyze the effective stages of immune cells in adipose tissue, including macrophage recruitment, macrophage polarization, and macrophage-like phenotype preadipocyte possession to find optimal sites as drug targets. Subsequently, some main signaling pathways are summarized in this review, including the AMP-activated protein kinase (AMPK) pathway, the JNK signaling pathway, and a novel one, the Notch signaling pathway. We illustrate all these points in order to determine the general pathogenesis of chronic low-grade local inflammation in adipose tissue and the related signaling pathways. In addition, signal-associated prospective compounds, such as berberine, are summarized and discussed with potential targets in pathogenesis. This might provide some possible thoughts and novel therapies for studying chronic inflammatory diseases, such as insulin resistance and type 2 diabetes mellitus.
[Mh] Termos MeSH primário: Adenilato Quinase/imunologia
Tecido Adiposo/imunologia
Diabetes Mellitus Tipo 2/imunologia
Janus Quinases/imunologia
Macrófagos/imunologia
Obesidade/imunologia
[Mh] Termos MeSH secundário: Adipócitos/imunologia
Animais
Seres Humanos
Inflamação
Terapia de Alvo Molecular
Obesidade/tratamento farmacológico
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
EC 2.7.10.2 (Janus Kinases); EC 2.7.4.3 (Adenylate Kinase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180130
[Lr] Data última revisão:
180130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1155/2017/4504612


  5 / 2706 MEDLINE  
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[PMID]:28890337
[Au] Autor:Ghalei H; Trepreau J; Collins JC; Bhaskaran H; Strunk BS; Karbstein K
[Ad] Endereço:Department of Integrative Structural and Computational Biology, The Scripps Research Institute, Jupiter, FL 33458, USA.
[Ti] Título:The ATPase Fap7 Tests the Ability to Carry Out Translocation-like Conformational Changes and Releases Dim1 during 40S Ribosome Maturation.
[So] Source:Mol Cell;67(6):990-1000.e3, 2017 Sep 21.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Late in their maturation, nascent small (40S) ribosomal subunits bind 60S subunits to produce 80S-like ribosomes. Because of the analogy of this translation-like cycle to actual translation, and because 80S-like ribosomes do not produce any protein, it has been suggested that this represents a quality control mechanism for subunit functionality. Here we use genetic and biochemical experiments to show that the essential ATPase Fap7 promotes formation of the rotated state, a key intermediate in translocation, thereby releasing the essential assembly factor Dim1 from pre-40S subunits. Bypassing this quality control step produces defects in reading frame maintenance. These results show how progress in the maturation cascade is linked to a test for a key functionality of 40S ribosomes: their ability to translocate the mRNAâ‹…tRNA pair. Furthermore, our data demonstrate for the first time that the translation-like cycle is a quality control mechanism that ensures the fidelity of the cellular ribosome pool.
[Mh] Termos MeSH primário: Adenilato Quinase/metabolismo
Mudança da Fase de Leitura do Gene Ribossômico
Metiltransferases/metabolismo
Proteínas Nucleares/metabolismo
Nucleosídeo-Trifosfatase/metabolismo
Subunidades Ribossômicas Menores de Eucariotos/enzimologia
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/enzimologia
[Mh] Termos MeSH secundário: Adenilato Quinase/química
Adenilato Quinase/genética
Genótipo
Metiltransferases/química
Metiltransferases/genética
Modelos Moleculares
Proteínas Nucleares/química
Proteínas Nucleares/genética
Nucleosídeo-Trifosfatase/química
Nucleosídeo-Trifosfatase/genética
Fenótipo
Ligação Proteica
Conformação Proteica
Proteólise
Subunidades Ribossômicas Menores de Eucariotos/química
Subunidades Ribossômicas Menores de Eucariotos/genética
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
Relação Estrutura-Atividade
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nuclear Proteins); 0 (Saccharomyces cerevisiae Proteins); EC 2.1.1.- (DIM1 protein, S cerevisiae); EC 2.1.1.- (Methyltransferases); EC 2.7.4.3 (Adenylate Kinase); EC 2.7.4.3 (FAP7 protein, S cerevisiae); EC 3.6.1.15 (Nucleoside-Triphosphatase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171102
[Lr] Data última revisão:
171102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170912
[St] Status:MEDLINE


  6 / 2706 MEDLINE  
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[PMID]:28767234
[Au] Autor:Onuk E; Badger J; Wang YJ; Bardhan J; Chishti Y; Akcakaya M; Brooks DH; Erdogmus D; Minh DDL; Makowski L
[Ad] Endereço:Radiation Oncology Department, University of California , Los Angeles, California 90095, United States.
[Ti] Título:Effects of Catalytic Action and Ligand Binding on Conformational Ensembles of Adenylate Kinase.
[So] Source:Biochemistry;56(34):4559-4567, 2017 Aug 29.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Crystal structures of adenylate kinase (AdK) from Escherichia coli capture two states: an "open" conformation (apo) obtained in the absence of ligands and a "closed" conformation in which ligands are bound. Other AdK crystal structures suggest intermediate conformations that may lie on the transition pathway between these two states. To characterize the transition from open to closed states in solution, X-ray solution scattering data were collected from AdK in the apo form and with progressively increasing concentrations of five different ligands. Scattering data from apo AdK are consistent with scattering predicted from the crystal structure of AdK in the open conformation. In contrast, data from AdK samples saturated with Ap5A do not agree with that calculated from AdK in the closed conformation. Using cluster analysis of available structures, we selected representative structures in five conformational states: open, partially open, intermediate, partially closed, and closed. We used these structures to estimate the relative abundances of these states for each experimental condition. X-ray solution scattering data obtained from AdK with AMP are dominated by scattering from AdK in the open conformation. For AdK in the presence of high concentrations of ATP and ADP, the conformational ensemble shifts to a mixture of partially open and closed states. Even when AdK is saturated with Ap5A, a significant proportion of AdK remains in a partially open conformation. These results are consistent with an induced-fit model in which the transition of AdK from an open state to a closed state is initiated by ATP binding.
[Mh] Termos MeSH primário: Difosfato de Adenosina/química
Trifosfato de Adenosina/química
Adenilato Quinase/química
Fosfatos de Dinucleosídeos/química
Proteínas de Escherichia coli/química
Escherichia coli/enzimologia
[Mh] Termos MeSH secundário: Adenilato Quinase/genética
Domínio Catalítico
Cristalografia por Raios X
Escherichia coli/genética
Proteínas de Escherichia coli/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dinucleoside Phosphates); 0 (Escherichia coli Proteins); 50304-44-4 (P(1),P(5)-di(adenosine-5'-)pentaphosphate); 61D2G4IYVH (Adenosine Diphosphate); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.4.3 (Adenylate Kinase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170831
[Lr] Data última revisão:
170831
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170803
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00351


  7 / 2706 MEDLINE  
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[PMID]:28720584
[Au] Autor:Ruby MA; Riedl I; Massart J; Åhlin M; Zierath JR
[Ad] Endereço:Department of Molecular Medicine and Surgery, Section for Integrative Physiology, Karolinska Institutet, Stockholm, Sweden.
[Ti] Título:Protein kinase N2 regulates AMP kinase signaling and insulin responsiveness of glucose metabolism in skeletal muscle.
[So] Source:Am J Physiol Endocrinol Metab;313(4):E483-E491, 2017 Oct 01.
[Is] ISSN:1522-1555
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Insulin resistance is central to the development of type 2 diabetes and related metabolic disorders. Because skeletal muscle is responsible for the majority of whole body insulin-stimulated glucose uptake, regulation of glucose metabolism in this tissue is of particular importance. Although Rho GTPases and many of their affecters influence skeletal muscle metabolism, there is a paucity of information on the protein kinase N (PKN) family of serine/threonine protein kinases. We investigated the impact of PKN2 on insulin signaling and glucose metabolism in primary human skeletal muscle cells in vitro and mouse tibialis anterior muscle in vivo. PKN2 knockdown in vitro decreased insulin-stimulated glucose uptake, incorporation into glycogen, and oxidation. PKN2 siRNA increased 5'-adenosine monophosphate-activated protein kinase (AMPK) signaling while stimulating fatty acid oxidation and incorporation into triglycerides and decreasing protein synthesis. At the transcriptional level, PKN2 knockdown increased expression of PGC-1α and SREBP-1c and their target genes. In mature skeletal muscle, in vivo PKN2 knockdown decreased glucose uptake and increased AMPK phosphorylation. Thus, PKN2 alters key signaling pathways and transcriptional networks to regulate glucose and lipid metabolism. Identification of PKN2 as a novel regulator of insulin and AMPK signaling may provide an avenue for manipulation of skeletal muscle metabolism.
[Mh] Termos MeSH primário: Adenilato Quinase/metabolismo
Glucose/metabolismo
Fibras Musculares Esqueléticas/metabolismo
Músculo Esquelético/metabolismo
Proteína Quinase C/genética
[Mh] Termos MeSH secundário: Animais
Ácidos Graxos/metabolismo
Técnicas de Silenciamento de Genes
Glicogênio/metabolismo
Seres Humanos
Técnicas In Vitro
Resistência à Insulina/genética
Metabolismo dos Lipídeos/genética
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Coativador 1-alfa do Receptor gama Ativado por Proliferador de Peroxissomo/metabolismo
Fosforilação
Biossíntese de Proteínas/genética
Proteína Quinase C/metabolismo
Músculo Quadríceps/citologia
Transdução de Sinais
Proteína de Ligação a Elemento Regulador de Esterol 1/metabolismo
Triglicerídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acids); 0 (Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha); 0 (Sterol Regulatory Element Binding Protein 1); 0 (Triglycerides); 9005-79-2 (Glycogen); EC 2.7.1.- (protein kinase N); EC 2.7.11.13 (Protein Kinase C); EC 2.7.4.3 (Adenylate Kinase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170720
[St] Status:MEDLINE
[do] DOI:10.1152/ajpendo.00147.2017


  8 / 2706 MEDLINE  
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[PMID]:28715469
[Au] Autor:Jayachandran C; Palanisamy Athiyaman B; Sankaranarayanan M
[Ad] Endereço:Centre for Biotechnology, Anna University, Chennai, India.
[Ti] Título:Cofactor engineering improved CALB production in Pichia pastoris through heterologous expression of NADH oxidase and adenylate kinase.
[So] Source:PLoS One;12(7):e0181370, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The cofactor engineering strategy can relieve the metabolic stress induced by expression of recombinant protein in cellular metabolism related to cofactor and energy reactions. To study the effect of cofactor regeneration on recombinant protein expression, NADH oxidase (noxE) was engineered in P. pastoris expressing lipase B (GSCALB). Expression of noxE in P. pastoris (GSCALBNOX) increased NAD+ levels by 85% with a concomitant reduction in NADH/NAD+ ratio of 67% compared to GSCALB. The change in the redox level positively influenced the methanol uptake rate and made 34% augment in CALB activity. The decline in NADH level (44%) by noxE expression had lowered the adenylate energy charge (AEC) and ATP level in GSCALBNOX. In order to regenerate ATP in GSCALBNOX, adenylate kinase (ADK1) gene from S. cerevisiae S288c was co-expressed. Expression of ADK1 showed a remarkable increase in AEC and co-expression of both the genes synergistically improved CALB activity. This study shows the importance of maintenance of cellular redox homeostasis and adenylate energy charge during recombinant CALB expression in P. pastoris.
[Mh] Termos MeSH primário: Adenilato Quinase/metabolismo
Proteínas Fúngicas/biossíntese
Lipase/biossíntese
Complexos Multienzimáticos/metabolismo
NADH NADPH Oxirredutases/metabolismo
Pichia/genética
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Adenilato Quinase/genética
Aldeído Oxirredutases/metabolismo
Proteínas Fúngicas/genética
Expressão Gênica
Engenharia Genética
Homeostase
Lipase/genética
Metanol/metabolismo
Complexos Multienzimáticos/genética
NAD/metabolismo
NADH NADPH Oxirredutases/genética
Oxirredução
Pichia/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Proteínas Recombinantes/biossíntese
Saccharomyces/enzimologia
Saccharomyces/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Multienzyme Complexes); 0 (Recombinant Proteins); 0U46U6E8UK (NAD); 8L70Q75FXE (Adenosine Triphosphate); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.1.46 (formaldehyde dehydrogenase, glutathione-independent); EC 1.6.- (NADH oxidase); EC 1.6.- (NADH, NADPH Oxidoreductases); EC 2.7.4.3 (Adenylate Kinase); EC 3.1.1.3 (Lipase); EC 3.1.1.3 (lipase B, Candida antarctica); Y4S76JWI15 (Methanol)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170718
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181370


  9 / 2706 MEDLINE  
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[PMID]:28715177
[Au] Autor:DeMott CM; Majumder S; Burz DS; Reverdatto S; Shekhtman A
[Ad] Endereço:Department of Chemistry, State University of New York at Albany , Albany, New York 12222, United States.
[Ti] Título:Ribosome Mediated Quinary Interactions Modulate In-Cell Protein Activities.
[So] Source:Biochemistry;56(32):4117-4126, 2017 Aug 15.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ribosomes are present inside bacterial cells at micromolar concentrations and occupy up to 20% of the cell volume. Under these conditions, even weak quinary interactions between ribosomes and cytosolic proteins can affect protein activity. By using in-cell and in vitro NMR spectroscopy, and biophysical techniques, we show that the enzymes, adenylate kinase and dihydrofolate reductase, and the respective coenzymes, ATP and NADPH, bind to ribosomes with micromolar affinity, and that this interaction suppresses the enzymatic activities of both enzymes. Conversely, thymidylate synthase, which works together with dihydrofolate reductase in the thymidylate synthetic pathway, is activated by ribosomes. We also show that ribosomes impede diffusion of green fluorescent protein in vitro and contribute to the decrease in diffusion in vivo. These results strongly suggest that ribosome-mediated quinary interactions contribute to the differences between in vitro and in vivo protein activities and that ribosomes play a previously under-appreciated nontranslational role in regulating cellular biochemistry.
[Mh] Termos MeSH primário: Adenilato Quinase/metabolismo
Proteínas de Escherichia coli/metabolismo
Escherichia coli/metabolismo
Ressonância Magnética Nuclear Biomolecular/métodos
Ribossomos/metabolismo
Tetra-Hidrofolato Desidrogenase/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/genética
Trifosfato de Adenosina/metabolismo
Adenilato Quinase/genética
Coenzimas/genética
Coenzimas/metabolismo
Escherichia coli/genética
Proteínas de Escherichia coli/genética
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
NADP/genética
NADP/metabolismo
Ribossomos/genética
Tetra-Hidrofolato Desidrogenase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coenzymes); 0 (Escherichia coli Proteins); 147336-22-9 (Green Fluorescent Proteins); 53-59-8 (NADP); 8L70Q75FXE (Adenosine Triphosphate); EC 1.5.1.3 (Tetrahydrofolate Dehydrogenase); EC 2.7.4.3 (Adenylate Kinase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170718
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00613


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[PMID]:28654658
[Au] Autor:Yan H; Ajuwon KM
[Ad] Endereço:Department of Animal Sciences, Purdue University, West Lafayette, Indiana, United States of America.
[Ti] Título:Butyrate modifies intestinal barrier function in IPEC-J2 cells through a selective upregulation of tight junction proteins and activation of the Akt signaling pathway.
[So] Source:PLoS One;12(6):e0179586, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The intestinal epithelial barrier, composed of epithelial cells, tight junction proteins and intestinal secretions, prevents passage of luminal substances and antigens through the paracellular space. Dysfunction of the intestinal barrier integrity induced by toxins and pathogens is associated with a variety of gastrointestinal disorders and diseases. Although butyrate is known to enhance intestinal health, its role in the protection of intestinal barrier function is poorly characterized. Therefore, we investigated the effect of butyrate on intestinal epithelial integrity and tight junction permeability in a model of LPS-induced inflammation in IPEC-J2 cells. Butyrate dose-dependently reduced LPS impairment of intestinal barrier integrity and tight junction permeability, measured by trans-epithelial electrical resistance (TEER) and paracellular uptake of fluorescein isothiocyanate-dextran (FITC-dextran). Additionally, butyrate increased both mRNA expression and protein abundance of claudins-3 and 4, and influenced intracellular ATP concentration in a dose-dependent manner. Furthermore, butyrate prevented the downregulation of Akt and 4E-BP1 phosphorylation by LPS, indicating that butyrate might enhance tight junction protein abundance through mechanisms that included activation of Akt/mTOR mediated protein synthesis. The regulation of AMPK activity and intracellular ATP level by butyrate indicates that butyrate might regulate energy status of the cell, perhaps by serving as a nutrient substrate for ATP synthesis, to support intestinal epithelial barrier tight junction protein abundance. Our findings suggest that butyrate might protect epithelial cells from LPS-induced impairment of barrier integrity through an increase in the synthesis of tight junction proteins, and perhaps regulation of energy homeostasis.
[Mh] Termos MeSH primário: Ácido Butírico/farmacologia
Mucosa Intestinal/efeitos dos fármacos
Proteínas Proto-Oncogênicas c-akt/metabolismo
Transdução de Sinais/efeitos dos fármacos
Proteínas de Junções Íntimas/metabolismo
Regulação para Cima/efeitos dos fármacos
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Adenilato Quinase/metabolismo
Animais
Linhagem Celular
Citocinas/metabolismo
Relação Dose-Resposta a Droga
Mucosa Intestinal/metabolismo
Permeabilidade
Fosforilação/efeitos dos fármacos
Suínos
Junções Íntimas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); 0 (Tight Junction Proteins); 107-92-6 (Butyric Acid); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 2.7.4.3 (Adenylate Kinase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170628
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0179586



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