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[PMID]:28958473
[Au] Autor:Jia C; Yang H; Dai C; Xu F; Peng S; Zhao Y; Zhao C; Zhao L
[Ad] Endereço:Department of Hepatobiliary-Splenic Surgery, General Surgery, Shengjing Hospital, China Medical University, Shenyang 110004, China.
[Ti] Título:Expression of hypoxia inducible factor-1α and its correlation with phosphoenolpyruvate carboxykinase after portal vein ligation in rats.
[So] Source:Life Sci;190:97-102, 2017 Dec 01.
[Is] ISSN:1879-0631
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:AIMS: Portal vein ligation (PVL) has been used to effectively increase future liver remnant (FLR) in hepatectomy for treatment of liver cancer. However, the underlying molecular mechanisms have not been well characterized. The present study aimed to determine expression of hypoxia inducible factor-1alpha (HIF-1α) in response to PVL and assess the correlation of HIF-1α and phosphoenolpyruvate carboxykinase (PEPCK). MAIN METHODS: Male Sprague-Dawley rats underwent PVL and were sacrificed at different time points (12, 24, 48, 72, and 168h) after surgery. Hepatic HIF-1α expression in the regenerating liver was assessed by Western blot and immunohistochemistry, in parallel; PEPCK levels were quantified by ELISA. KEY FINDINGS: We found that the ligated liver lobes diminished progressively, whereas the unligated lobes underwent compensatory regeneration after 70% ligation of portal vein branches in the PVL group. Hepatic HIF-1α and PEPCK levels in the unligated liver lobes were significantly increased in the PVL group compared to the hepatic artery ligation (HAL) and the sham (SH) operation groups. Pearson's correlation analysis revealed positive correlation between HIF-1α expression and PEPCK levels in the unligated lobes after PVL. Further analysis indicated that higher levels of HIF-1α and PEPCK in response to liver regeneration were paralleled by an increase in the ratio of the mass and volume of unligated lobes to the whole liver. SIGNIFICANCE: HIF-1α was up-regulated and positively correlated with PEPCK during liver regeneration after PVL in rats, suggesting that HIF-1α may modulate hepatic gluconeogenesis through PEPCK, which may ensure the energy supply required for liver regeneration.
[Mh] Termos MeSH primário: Subunidade alfa do Fator 1 Induzível por Hipóxia/genética
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Fígado/metabolismo
Fosfoenolpiruvato Carboxiquinase (GTP)/metabolismo
Regeneração/fisiologia
[Mh] Termos MeSH secundário: Animais
Western Blotting
Ensaio de Imunoadsorção Enzimática
Gluconeogênese/fisiologia
Ligadura
Masculino
Veia Porta
Ratos
Ratos Sprague-Dawley
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hypoxia-Inducible Factor 1, alpha Subunit); 0 (Intracellular Signaling Peptides and Proteins); EC 4.1.1.32 (Phosphoenolpyruvate Carboxykinase (GTP)); EC 4.1.1.32 (phosphoenolpyruvate carboxykinase 1 (soluble) protein, rat)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170930
[St] Status:MEDLINE


  2 / 2085 MEDLINE  
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[PMID]:28835389
[Au] Autor:Ying Z; Zhang H; Su W; Zhou L; Wang F; Li Y; Zhang L; Wang T
[Ad] Endereço:College of Animal Science and Technology, Nanjing Agricultural University, Nanjing, People's Republic of China.
[Ti] Título:Dietary Methionine Restriction Alleviates Hyperglycemia in Pigs with Intrauterine Growth Restriction by Enhancing Hepatic Protein Kinase B Signaling and Glycogen Synthesis.
[So] Source:J Nutr;147(10):1892-1899, 2017 Oct.
[Is] ISSN:1541-6100
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Individuals with intrauterine growth restriction (IUGR) are prone to developing type 2 diabetes mellitus (T2DM). Dietary methionine restriction (MR) improves insulin sensitivity and glucose homeostasis in individuals with normal birth weight (NBW). This study investigated the effects of MR on plasma glucose concentration and hepatic and muscle glucose metabolism in pigs with IUGR. Thirty female NBW and 60 same-sex spontaneous IUGR piglets (Landrace × Yorkshire) were selected. After weaning (day 21), the piglets were fed diets with adequate methionine (NBW-CON and IUGR-CON) or 30% less methionine (IUGR-MR) ( = 6). At day 180, 1 pig with a body weight near the mean of each replication was selected for biochemical analysis. The IUGR-CON group showed 41.6%, 68.6%, and 67.1% higher plasma glucose concentration, hepatic phosphoenolpyruvate carboxykinase activity, and glucose-6-phosphatase activity, respectively, than the NBW-CON group ( < 0.05). Muscle glycogen content and glycogen synthase activity were 36.9% and 38.8% lower, respectively, in the IUGR-CON than the NBW-CON group ( < 0.05), respectively, and there was decreased hepatic and muscle protein kinase B phosphorylation in the IUGR-CON group ( < 0.05). Compared with the IUGR-CON pigs, the IUGR-MR pigs had 28.7% lower plasma glucose concentrations ( < 0.05), which were similar to those of the NBW-CON pigs ( ≥ 0.05). The hepatic glycogen content and glycogen synthase activity of the IUGR-MR pigs were 62.9% and 50.8% higher than those of the IUGR-CON pigs ( < 0.05) and 53.5% and 84.3% higher than the NBW-CON pigs ( < 0.05), respectively. The IUGR-MR pigs' hepatic and muscle protein kinase B phosphorylation was higher than that of the IUGR-CON pigs ( < 0.05) and similar to that of the NBW-CON pigs ( ≥ 0.05). MR attenuates hyperglycemia in IUGR pigs by enhancing hepatic protein kinase B signaling and glycogen synthesis, implying a potential nutritional strategy to prevent type 2 diabetes mellitus in IUGR offspring.
[Mh] Termos MeSH primário: Diabetes Mellitus Tipo 2/metabolismo
Retardo do Crescimento Fetal
Glicogênio/biossíntese
Hiperglicemia/dietoterapia
Fígado/metabolismo
Metionina/administração & dosagem
Proteínas Proto-Oncogênicas c-akt/metabolismo
[Mh] Termos MeSH secundário: Ração Animal
Animais
Animais Recém-Nascidos
Peso ao Nascer
Glicemia/metabolismo
Diabetes Mellitus Tipo 2/prevenção & controle
Dieta
Feminino
Glucose-6-Fosfatase/metabolismo
Glicogênio/metabolismo
Hiperglicemia/metabolismo
Resistência à Insulina
Masculino
Metionina/metabolismo
Metionina/farmacologia
Músculos/metabolismo
Fosfoenolpiruvato Carboxiquinase (GTP)/metabolismo
Fosforilação
Transdução de Sinais
Suínos
Desmame
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Blood Glucose); 9005-79-2 (Glycogen); AE28F7PNPL (Methionine); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 3.1.3.9 (Glucose-6-Phosphatase); EC 4.1.1.32 (Phosphoenolpyruvate Carboxykinase (GTP))
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170825
[St] Status:MEDLINE
[do] DOI:10.3945/jn.117.253427


  3 / 2085 MEDLINE  
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[PMID]:28678435
[Au] Autor:Niaz K; Mabqool F; Khan F; Ismail Hassan F; Baeeri M; Navaei-Nigjeh M; Hassani S; Gholami M; Abdollahi M
[Ad] Endereço:International Campus-Tehran University of Medical Sciences (IC-TUMS), Tehran, Iran.
[Ti] Título:Molecular mechanisms of action of styrene toxicity in blood plasma and liver.
[So] Source:Environ Toxicol;32(10):2256-2266, 2017 Oct.
[Is] ISSN:1522-7278
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Styrene is an aromatic colorless hydrocarbon available in liquid form and highly volatile. In its pure form, it gives a sweet smell. The primary source of exposure in the environment is from plastic materials, rubber industries, packaging materials, insulations, and fiber glass and carpet industry. Natural sources of styrene include: few metabolites in plants which are transferred through food chain. The current study was designed to evaluate styrene toxicity, including: superoxide dismutase (SOD) and protein carbonyl, oxidative stress, glucose-6-phosphatase (G6Pase), glycogen phosphorylase (GP), and phosphoenolpyruvate carboxykinase (PEPCK) activities, adenosine triphosphate (ATP) to adenosine diphosphate (ADP) ratio, and changes in gene expressions such as glutamate dehydrogenase 1 (GLUD1), glucose transporter 2 (GLUT2), and glucokinase (GCK) in the rat liver tissue. For this purpose, styrene was dissolved in corn oil and was administered via gavage, at doses 250, 500, 1000, 1500, 2000, mg/kg/day per mL and control (corn oil) to each rat with one day off in a week, for 42 days. Plasma SOD and protein carbonyl of plasma were significantly up-regulated in 1000, 1500, and 2000 mg/kg/day styrene administrated groups (P < .001). In addition, styrene caused an increase in lipid peroxidation (LPO) and reactive oxygen species (ROS) in the dose-dependent manners in liver tissue (P < .001). Furthermore, the ferrous reducing antioxidant power (FRAP) and total thiol molecules (TTM) in styrene-treated groups were significantly decreased in liver tissue (P < .001) with increasing doses. In treated rats, styrene significantly increased G6Pase activity (P < .001) and down-regulated GP activity (P < .001) as compared to the control group. The PEPCK activity was significantly raised in a dose-dependent manner (P < .001). The ATP/ADP ratio of live cells was significantly raised by increasing the dose (P < .001). There was significantly an up-regulation of GLUD1 and GCK at 2000 mg/kg group (P < .01) and a down-regulation for GLUT2 at the same dose. While in the rest of group, GLUT2 showed up-regulation of relative fold change. By targeting genes such as GLUD1, GLUT2, and GCK, disruption of hepatic gluconeogenesis, glycogenolysis, and insulin secretory functions are obvious. The present study illustrates that induction of oxidative stress followed by changes in G6Pase, GP, and PEPCK activities and the genes responsible for glucose metabolism are the mechanisms of styrene's action in the liver.
[Mh] Termos MeSH primário: Poluentes Ambientais/toxicidade
Fígado/efeitos dos fármacos
Estireno/toxicidade
Superóxido Dismutase/sangue
[Mh] Termos MeSH secundário: Difosfato de Adenosina/metabolismo
Trifosfato de Adenosina/metabolismo
Animais
Regulação da Expressão Gênica
Glucose/metabolismo
Glucose-6-Fosfatase/metabolismo
Glicogênio Fosforilase/metabolismo
Insulina/secreção
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Peroxidação de Lipídeos
Fígado/metabolismo
Masculino
Estresse Oxidativo
Fosfoenolpiruvato Carboxiquinase (GTP)/metabolismo
Carbonilação Proteica
Ratos Wistar
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Environmental Pollutants); 0 (Insulin); 0 (Intracellular Signaling Peptides and Proteins); 0 (Reactive Oxygen Species); 44LJ2U959V (Styrene); 61D2G4IYVH (Adenosine Diphosphate); 8L70Q75FXE (Adenosine Triphosphate); EC 1.15.1.1 (Superoxide Dismutase); EC 2.4.1.- (Glycogen Phosphorylase); EC 3.1.3.9 (Glucose-6-Phosphatase); EC 4.1.1.32 (Phosphoenolpyruvate Carboxykinase (GTP)); EC 4.1.1.32 (phosphoenolpyruvate carboxykinase 1 (soluble) protein, rat); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170706
[St] Status:MEDLINE
[do] DOI:10.1002/tox.22441


  4 / 2085 MEDLINE  
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[PMID]:28644880
[Au] Autor:Latorre P; Varona L; Burgos C; Carrodeguas JA; López-Buesa P
[Ad] Endereço:Departamento de Producción Animal y Ciencia de los Alimentos, Facultad de Veterinaria, Universidad de Zaragoza, Zaragoza, Spain.
[Ti] Título:O-GlcNAcylation mediates the control of cytosolic phosphoenolpyruvate carboxykinase activity via Pgc1α.
[So] Source:PLoS One;12(6):e0179988, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PGC1α is a coactivator of many transcription factors and cytosolic phosphoenolpyruvate carboxykinase (PCK1) is a key enzyme for gluconeogenesis. PGC1α interacts with the transcription factor PPARγ to stimulate PCK1 expression and thus de novo glucose synthesis. These proteins are not only important for central energy metabolism but also for supplying intermediates for other metabolic pathways, including lipidogenesis and protein synthesis and might therefore be important factors in the ethiopathogenesis of metabolic disorders like diabetes but also in other pathologies like cancer. Since polymorphisms in these proteins have been related to some phenotypic traits in animals like pigs and PGC1α G482S polymorphism increases fat deposition in humans, we have investigated the molecular basis of such effects focusing on a commonly studied polymorphism in pig Pgc1α, which changes a cysteine at position 430 (WT) of the protein to a serine (C430S). Biochemical analyses show that Pgc1α WT stimulates higher expression of human PCK1 in HEK293T and HepG2 cells. Paradoxically, Pgc1α WT is less stable than Pgc1α p.C430S in HEK293T cells. However, the study of different post-translational modifications shows a higher O-GlcNAcylation level of Pgc1α p.C430S. This higher O-GlcNAcylation level significantly decreases the interaction between Pgc1α and PPARγ demonstrating the importance of post-translational glycosylation of PGC1α in the regulation of PCK1 activity. This, furthermore, could explain at least in part the observed epistatic effects between PGC1α and PCK1 in pigs.
[Mh] Termos MeSH primário: Coativador 1-alfa do Receptor gama Ativado por Proliferador de Peroxissomo/metabolismo
Fosfoenolpiruvato Carboxiquinase (GTP)/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Epistasia Genética
Glucose/metabolismo
Glicosilação
Células HEK293
Células Hep G2
Seres Humanos
PPAR gama/metabolismo
Coativador 1-alfa do Receptor gama Ativado por Proliferador de Peroxissomo/genética
Fenótipo
Fosfoenolpiruvato Carboxiquinase (GTP)/genética
Processamento de Proteína Pós-Traducional
Estabilidade Proteica
RNA Mensageiro/metabolismo
Homologia de Sequência de Aminoácidos
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (PPAR gamma); 0 (Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha); 0 (RNA, Messenger); EC 4.1.1.32 (Phosphoenolpyruvate Carboxykinase (GTP)); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170624
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0179988


  5 / 2085 MEDLINE  
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[PMID]:28638873
[Au] Autor:Mansour AA; Nassan MA; Saleh OM; Soliman MM
[Ad] Endereço:Medical Biotechnology Department, Faculty of Applied Medical Sciences (Turbah), Taif Univ., KSA.
[Ti] Título:PROTECTIVE EFFECT OF CAMEL MILK AS ANTI-DIABETIC SUPPLEMENT: BIOCHEMICAL, MOLECULAR AND IMMUNOHISTOCHEMICAL STUDY.
[So] Source:Afr J Tradit Complement Altern Med;14(4):108-119, 2017.
[Is] ISSN:2505-0044
[Cp] País de publicação:Nigeria
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Diabetes is a serious disease affects human health. Diabetes in advanced stages is accompanied by general weakness and alteration in fats and carbohydrates metabolism. Recently there are some scientific trends about the usage of camel milk (CM) in the treatment of diabetes and its associated alterations. CM contains vital active particles with insulin like action that cure diabetes and its complications but how these effects occur, still unclear. MATERIALS AND METHODS: Seventy-five adult male rats of the albino type divided into five equal groups. Group 1 served as a negative control (C). Group 2 was supplemented with camel milk (CM). Diabetes was induced in the remaining groups (3, 4 and 5). Group 3 served as positive diabetic control (D). Group 4 served as diabetic and administered metformin (D+MET). Group 5 served as diabetes and supplemented with camel milk (D+CM). Camel milk was supplemented for two consecutive months. Serum glucose, leptin, insulin, liver, kidney, antioxidants, MDA and lipid profiles were assayed. Tissues from liver and adipose tissues were examined using RT-PCR analysis for the changes in mRNA expression of genes of carbohydrates and lipid metabolism. Pancreas and liver were used for immunohistochemical examination using specific antibodies. RESULTS: Camel milk supplementation ameliorated serum biochemical measurements that altered after diabetes induction. CM supplementation up-regulated mRNA expression of , , and genes, while down-regulated the expression of to control mRNA expression level. CM did not affect the expression of gene. On the other hand, metformin failed to reduce the expression of compared to camel milk administered rats. Immunohistochemical findings revealed that CM administration restored the immunostaining reactivity of insulin and GLUT-4 in the pancreas of diabetic rats. CONCLUSION: CM administration is of medical importance and helps physicians in the treatment of diabetes mellitus.
[Mh] Termos MeSH primário: Diabetes Mellitus Tipo 1/dietoterapia
Hipoglicemiantes/metabolismo
Leite/química
Leite/metabolismo
[Mh] Termos MeSH secundário: Animais
Glicemia/metabolismo
Camelus
Diabetes Mellitus Tipo 1/genética
Diabetes Mellitus Tipo 1/metabolismo
Seres Humanos
Insulina/metabolismo
Proteínas Substratos do Receptor de Insulina/genética
Proteínas Substratos do Receptor de Insulina/metabolismo
Peptídeos e Proteínas de Sinalização Intracelular/genética
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Rim/metabolismo
Leptina/metabolismo
Fígado/metabolismo
Masculino
Fosfoenolpiruvato Carboxiquinase (GTP)/genética
Fosfoenolpiruvato Carboxiquinase (GTP)/metabolismo
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Blood Glucose); 0 (Hypoglycemic Agents); 0 (Insulin); 0 (Insulin Receptor Substrate Proteins); 0 (Intracellular Signaling Peptides and Proteins); 0 (Leptin); EC 4.1.1.32 (Phosphoenolpyruvate Carboxykinase (GTP)); EC 4.1.1.32 (phosphoenolpyruvate carboxykinase 1 (soluble) protein, rat)
[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:170623
[St] Status:MEDLINE
[do] DOI:10.21010/ajtcam.v14i4.13


  6 / 2085 MEDLINE  
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[PMID]:28345895
[Au] Autor:Cui DS; Broom A; Mcleod MJ; Meiering EM; Holyoak T
[Ad] Endereço:Department of Biology and ‡Department of Chemistry, University of Waterloo , Waterloo, ON, Canada N2L 3G1.
[Ti] Título:Asymmetric Anchoring Is Required for Efficient Ω-Loop Opening and Closing in Cytosolic Phosphoenolpyruvate Carboxykinase.
[So] Source:Biochemistry;56(15):2106-2115, 2017 Apr 18.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mobile Ω-loops play essential roles in the function of many enzymes. Here we investigated the importance of a residue lying outside of the mobile Ω-loop element in the catalytic function of an H477R variant of cytosolic phosphoenolpyruvate carboxykinase using crystallographic, kinetic, and computational analysis. The crystallographic data suggest that the efficient transition of the Ω-loop to the closed conformation requires stabilization of the N-terminus of the loop through contacts between R461 and E588. In contrast, the C-terminal end of the Ω-loop undergoes changing interactions with the enzyme body through contacts between H477 at the C-terminus of the loop and E591 located on the enzyme body. Potential of mean force calculations demonstrated that altering the anchoring of the C-terminus of the Ω-loop via the H477R substitution results in the destabilization of the closed state of the Ω-loop by 3.4 kcal mol . The kinetic parameters for the enzyme were altered in an asymmetric fashion with the predominant effect being observed in the direction of oxaloacetate synthesis. This is exemplified by a reduction in k for the H477R mutant by an order of magnitude in the direction of OAA synthesis, while in the direction of PEP synthesis, it decreased by a factor of only 2. The data are consistent with a mechanism for loop conformational exchange between open and closed states in which a balance between fixed anchoring of the N-terminus of the Ω-loop and a flexible, unattached C-terminus drives the transition between a disordered (open) state and an ordered (closed) state.
[Mh] Termos MeSH primário: Citosol/enzimologia
Fosfoenolpiruvato Carboxiquinase (GTP)/metabolismo
[Mh] Termos MeSH secundário: Animais
Cristalografia por Raios X
Cinética
Simulação de Dinâmica Molecular
Mutagênese Sítio-Dirigida
Fosfoenolpiruvato Carboxiquinase (GTP)/química
Fosfoenolpiruvato Carboxiquinase (GTP)/genética
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 4.1.1.32 (Phosphoenolpyruvate Carboxykinase (GTP))
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170501
[Lr] Data última revisão:
170501
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170328
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00178


  7 / 2085 MEDLINE  
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[PMID]:28235541
[Au] Autor:Gutteridge RE; Singh CK; Ndiaye MA; Ahmad N
[Ad] Endereço:Department of Dermatology, University of Wisconsin, 1300 University Avenue, Madison, WI 53706, USA.
[Ti] Título:Targeted knockdown of polo-like kinase 1 alters metabolic regulation in melanoma.
[So] Source:Cancer Lett;394:13-21, 2017 May 28.
[Is] ISSN:1872-7980
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:A limited number of studies have indicated an association of the mitotic kinase polo-like kinase 1 (PLK1) and cellular metabolism. Here, employing an inducible RNA interference approach in A375 melanoma cells coupled with a PCR array and multiple validation approaches, we demonstrated that PLK1 alters a number of genes associated with cellular metabolism. PLK1 knockdown resulted in a significant downregulation of IDH1, PDP2 and PCK1 and upregulation of FBP1. Ingenuity Pathway Analysis (IPA) identified that 1) glycolysis and the pentose phosphate pathway are major canonical pathways associated with PLK1, and 2) PLK1 inhibition-modulated genes were largely associated with cellular proliferation, with FBP1 being the key modulator. Further, BI 6727-mediated inhibition of PLK1 caused a decrease in PCK1 and increase in FBP1 in A375 melanoma cell implanted xenografts in vivo. Furthermore, an inverse correlation between PLK1 and FBP1 was found in melanoma cells, with FBP1 expression significantly downregulated in a panel of melanoma cells. In addition, BI 6727 treatment resulted in an upregulation in FBP1 in A375, Hs294T and G361 melanoma cells. Overall, our study suggests that PLK1 may be an important regulator of metabolism maintenance in melanoma cells.
[Mh] Termos MeSH primário: Proteínas de Ciclo Celular/metabolismo
Metabolismo Energético
Técnicas de Silenciamento de Genes
Melanoma/enzimologia
Proteínas Serina-Treonina Quinases/metabolismo
Proteínas Proto-Oncogênicas/metabolismo
Interferência de RNA
Neoplasias Cutâneas/enzimologia
[Mh] Termos MeSH secundário: Animais
Proteínas de Ciclo Celular/genética
Linhagem Celular Tumoral
Proliferação Celular
Regulação para Baixo
Frutose-Bifosfatase/genética
Frutose-Bifosfatase/metabolismo
Regulação Enzimológica da Expressão Gênica
Regulação Neoplásica da Expressão Gênica
Redes Reguladoras de Genes
Células HEK293
Seres Humanos
Peptídeos e Proteínas de Sinalização Intracelular/genética
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Isocitrato Desidrogenase/genética
Isocitrato Desidrogenase/metabolismo
Melanoma/genética
Melanoma/patologia
Camundongos
Fosfoenolpiruvato Carboxiquinase (GTP)/genética
Fosfoenolpiruvato Carboxiquinase (GTP)/metabolismo
Proteínas Serina-Treonina Quinases/genética
Proteínas Proto-Oncogênicas/genética
Piruvato Desidrogenase (Lipoamida)-Fosfatase/genética
Piruvato Desidrogenase (Lipoamida)-Fosfatase/metabolismo
Transdução de Sinais
Neoplasias Cutâneas/genética
Neoplasias Cutâneas/patologia
Transfecção
Carga Tumoral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (Intracellular Signaling Peptides and Proteins); 0 (Proto-Oncogene Proteins); EC 1.1.1.41 (Isocitrate Dehydrogenase); EC 1.1.1.42. (IDH1 protein, human); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (polo-like kinase 1); EC 3.1.3.11 (Fructose-Bisphosphatase); EC 3.1.3.43 (Pyruvate Dehydrogenase (Lipoamide)-Phosphatase); EC 4.1.1.32 (PCK1 protein, human); EC 4.1.1.32 (Phosphoenolpyruvate Carboxykinase (GTP))
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170226
[St] Status:MEDLINE


  8 / 2085 MEDLINE  
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[PMID]:28216384
[Au] Autor:Vieira P; Cameron J; Rahikkala E; Keski-Filppula R; Zhang LH; Santra S; Matthews A; Myllynen P; Nuutinen M; Moilanen JS; Rodenburg RJ; Rolfs A; Uusimaa J; van Karnebeek CD
[Ad] Endereço:PEDEGO Research Unit, University of Oulu, Clinic for Children and Adolescents, Oulu University Hospital, Oulu, Finland. Electronic address: paivi.vieira@fimnet.fi.
[Ti] Título:Novel homozygous PCK1 mutation causing cytosolic phosphoenolpyruvate carboxykinase deficiency presenting as childhood hypoglycemia, an abnormal pattern of urine metabolites and liver dysfunction.
[So] Source:Mol Genet Metab;120(4):337-341, 2017 Apr.
[Is] ISSN:1096-7206
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Clinical and laboratory data were collected from three Finnish patients including a sibling pair and another unrelated child with unexplained childhood hypoglycemia. Transient elevation of alanine transaminase, lactate and tricarboxylic acid cycle intermediates, especially fumarate, were noticed in urine organic acid analysis. Exome sequencing was performed for the patients and their parents. A novel homozygous PCK1 c.925G>A (p.G309R) mutation was detected in all affected individuals. COS-1 cells transfected with mutant PCK1 transcripts were used to study the pathogenic nature of the detected variant. The COS-1 transfected cells showed the mutant gene to be incapable of producing a normally functioning cytosolic phosphoenolpyruvate carboxykinase (PEPCK) enzyme. This report further delineates the clinical phenotype of isolated cytosolic PEPCK deficiency and offers a metabolic pattern helping to recognize these patients. Cytosolic PEPCK deficiency should be considered in the differential diagnosis of children presenting with hypoglycemia, hepatic dysfunction and elevated tricarboxylic acid intermediates in urinary organic acid analysis.
[Mh] Termos MeSH primário: Erros Inatos do Metabolismo dos Carboidratos/diagnóstico
Hipoglicemia/etiologia
Peptídeos e Proteínas de Sinalização Intracelular/genética
Hepatopatias/diagnóstico
Fígado/fisiopatologia
Mutação de Sentido Incorreto
Fosfoenolpiruvato Carboxiquinase (GTP)/deficiência
Urina/química
[Mh] Termos MeSH secundário: Animais
Células COS
Erros Inatos do Metabolismo dos Carboidratos/fisiopatologia
Cercopithecus aethiops
Criança
Exoma
Feminino
Predisposição Genética para Doença
Homozigoto
Seres Humanos
Hepatopatias/fisiopatologia
Masculino
Linhagem
Fosfoenolpiruvato Carboxiquinase (GTP)/genética
Análise de Sequência de DNA/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Intracellular Signaling Peptides and Proteins); EC 4.1.1.32 (PCK1 protein, human); EC 4.1.1.32 (Phosphoenolpyruvate Carboxykinase (GTP))
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170221
[St] Status:MEDLINE


  9 / 2085 MEDLINE  
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[PMID]:28198082
[Au] Autor:Chen L; Zeng T; Li GQ; Liu R; Tian Y; Li QH; Lu LZ
[Ad] Endereço:Institute of Animal Sciences and Veterinary Medicine, Zhejiang Academy of Agricultural Sciences, Hangzhou, 310021, China.
[Ti] Título:PCK1 expression is correlated with the plasma glucose level in the duck.
[So] Source:Anim Genet;48(3):358-361, 2017 Jun.
[Is] ISSN:1365-2052
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Phosphoenolpyruvate carboxykinase 1 (soluble) (PCK1) is a key gene in gluconeogenesis and glyceroneogenesis. Although its functions have been extensively studied in mice, bats and humans, little is known in ducks. Here, PCK1 functions were studied using a duck domestication model and a 48-h fasting experiment. We found PCK1 expression significantly decreased in two breeds of domestic ducks (Jinyun Pockmark ducks and Cherry Valley ducks) as compared with wild ducks (Anas platyrhynchos). Simultaneously, plasma levels of glucose, triglycerides and free fatty acid in domestic ducks were lower than in wild ducks. When compared with fed ducks, the plasma triglyceride level was observed to be significantly decreased, while the glucose and free fatty acid levels remained constant in 48-h fasting ducks. The expression analysis of gluconeogenic genes revealed that fructose-1,6-bisphosphatase genes (FBP1 and FBP2) and the glucose-6-phosphatase gene (G6PC2) were not changed, whereas PCK1 was significantly upregulated. In addition, the reported regulators of PCK1, including forkhead box A2 (FOXA2) gene and orphan nuclear receptor NR4A family genes (NR4A1, NR4A2 and NR4A3), exhibited similar expression levels between 48-h fasting ducks and fed ducks, suggesting that PCK1 is not regulated by these genes in the duck under fasting conditions. In conclusion, PCK1 expression may affect plasma levels of glucose, triglycerides and free fatty acid during the duck domestication process. This work demonstrates for the first time in duck that PCK1 is a key gene in maintaining plasma glucose homeostasis during fasting and that the upregulated expression of PCK1 may be responsible for constant plasma free fatty acid level by the glyceroneogenesis process.
[Mh] Termos MeSH primário: Glicemia/genética
Patos/genética
Gluconeogênese/genética
Fosfoenolpiruvato Carboxiquinase (GTP)/genética
[Mh] Termos MeSH secundário: Animais
Animais Domésticos
Animais Selvagens
Cruzamento
Ácidos Graxos não Esterificados/sangue
Homeostase
Masculino
Triglicerídeos/sangue
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Blood Glucose); 0 (Fatty Acids, Nonesterified); 0 (Triglycerides); EC 4.1.1.32 (Phosphoenolpyruvate Carboxykinase (GTP))
[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:170216
[St] Status:MEDLINE
[do] DOI:10.1111/age.12540


  10 / 2085 MEDLINE  
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[PMID]:27785616
[Au] Autor:Semakova J; Hyrossová P; Méndez-Lucas A; Cutz E; Bermudez J; Burgess S; Alcántara S; Perales JC
[Ad] Endereço:Department of Physiological Sciences, Faculty of Medicine, University of Barcelona, L'Hospitalet del Llobregat, Barcelona, Spain.
[Ti] Título:PEPCK-C reexpression in the liver counters neonatal hypoglycemia in Pck1 mice, unmasking role in non-gluconeogenic tissues.
[So] Source:J Physiol Biochem;73(1):89-98, 2017 Feb.
[Is] ISSN:1877-8755
[Cp] País de publicação:Spain
[La] Idioma:eng
[Ab] Resumo:Whole body cytosolic phosphoenolpyruvate carboxykinase knockout (PEPCK-C KO) mice die early after birth with profound hypoglycemia therefore masking the role of PEPCK-C in adult, non-gluconeogenic tissues where it is expressed. To investigate whether PEPCK-C deletion in the liver was critically responsible for the hypoglycemic phenotype, we reexpress this enzyme in the liver of PEPCK-C KO pups by early postnatal administration of PEPCK-C-expressing adenovirus. This maneuver was sufficient to partially rescue hypoglycemia and allow the pups to survive and identifies the liver as a critical organ, and hypoglycemia as the critical pathomechanism, leading to early postnatal death in the whole-body PEPCK-C knockout mice. Pathology assessment of survivors also suggest a possible role for PEPCK-C in lung maturation and muscle metabolism.
[Mh] Termos MeSH primário: Erros Inatos do Metabolismo dos Carboidratos/veterinária
Hipoglicemia/prevenção & controle
Hepatopatias/veterinária
Fígado/enzimologia
Pulmão/metabolismo
Músculo Esquelético/metabolismo
Fosfoenolpiruvato Carboxiquinase (GTP)/deficiência
Fosfoenolpiruvato Carboxiquinase (GTP)/metabolismo
[Mh] Termos MeSH secundário: Animais
Animais Recém-Nascidos
Encéfalo/enzimologia
Encéfalo/metabolismo
Encéfalo/patologia
Erros Inatos do Metabolismo dos Carboidratos/enzimologia
Erros Inatos do Metabolismo dos Carboidratos/fisiopatologia
Erros Inatos do Metabolismo dos Carboidratos/terapia
Cruzamentos Genéticos
Técnicas de Transferência de Genes
Gluconeogênese
Heterozigoto
Hipoglicemia/etiologia
Hipoglicemia/metabolismo
Hipoglicemia/patologia
Gotículas Lipídicas/metabolismo
Gotículas Lipídicas/patologia
Metabolismo dos Lipídeos
Lipidoses/etiologia
Fígado/metabolismo
Fígado/patologia
Hepatopatias/enzimologia
Hepatopatias/fisiopatologia
Hepatopatias/terapia
Pulmão/enzimologia
Pulmão/patologia
Camundongos Endogâmicos C57BL
Camundongos Knockout
Músculo Esquelético/enzimologia
Músculo Esquelético/patologia
Neurônios/enzimologia
Neurônios/metabolismo
Neurônios/patologia
Fosfoenolpiruvato Carboxiquinase (GTP)/genética
Fosfoenolpiruvato Carboxiquinase (GTP)/uso terapêutico
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Proteins); EC 4.1.1.32 (Phosphoenolpyruvate Carboxykinase (GTP))
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161028
[St] Status:MEDLINE
[do] DOI:10.1007/s13105-016-0528-y



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