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[PMID]:29186181
[Au] Autor:Wormald M; Liao G; Kimos M; Barrow J; Wei H
[Ad] Endereço:Department of Pharmacology and Molecular Sciences, Johns Hopkins University, Baltimore, Maryland, United States of America.
[Ti] Título:Development of a homogenous high-throughput assay for inositol hexakisphosphate kinase 1 activity.
[So] Source:PLoS One;12(11):e0188852, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Inositol pyrophosphates have been implicated in a wide range of cellular processes. Inositol hexakisphosphate kinase 1 catalyzes the pyrophosphorylation of inositol hexakisphosphate into inositol 5-diphospho-1,2,3,4,6-pentakisphosphate which is important in numerous areas of cell physiology such as DNA repair and glucose homeostasis. Furthermore, inositol 5-diphospho-1,2,3,4,6-pentakisphosphate is implicated in the pathology of diabetes and other human diseases. As such there is a demonstrated need in the field for a robust chemical probe to better understand the role of inositol hexakisphosphate kinase 1 and inositol pyrophosphate in physiology and disease. To aid in this effort we developed a homogenous coupled bioluminescence assay for measuring inositol hexakisphosphate kinase 1 activity in a 384-well format (Z' = 0.62±0.05). Using this assay we were able to confirm the activity of a known inositol hexakisphosphate kinase 1 inhibitor N2-(m-trifluorobenzyl), N6-(p-nitrobenzyl)purine. We also screened the Sigma library of pharmacologically active compounds at 10µM concentration and found 24 hits. Two of the most potent compounds were found to have an IC50 less than 5µM. The use of this high-throughput assay will accelerate the field towards the discovery of a potent inositol hexakisphosphate kinase 1 inhibitor.
[Mh] Termos MeSH primário: Fosfotransferases (Aceptor do Grupo Fosfato)/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Eletroforese em Gel de Poliacrilamida
Ensaios de Triagem em Larga Escala
Seres Humanos
Cinética
[Pt] Tipo de publicação:JOURNAL ARTICLE; VALIDATION STUDIES
[Nm] Nome de substância:
8L70Q75FXE (Adenosine Triphosphate); EC 2.7.4.- (Phosphotransferases (Phosphate Group Acceptor)); EC 2.7.4.21 (inositol hexakisphosphate kinase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180101
[Lr] Data última revisão:
180101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171130
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188852


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[PMID]:28450399
[Au] Autor:Franco-Echevarría E; Sanz-Aparicio J; Brearley CA; González-Rubio JM; González B
[Ad] Endereço:From the Departamento de Cristalografía y Biología Estructural, Instituto de Química-Física "Rocasolano," Consejo Superior de Investigaciones Científicas, Serrano 119, 28006 Madrid, Spain and.
[Ti] Título:The crystal structure of mammalian inositol 1,3,4,5,6-pentakisphosphate 2-kinase reveals a new zinc-binding site and key features for protein function.
[So] Source:J Biol Chem;292(25):10534-10548, 2017 06 23.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Inositol 1,3,4,5,6-pentakisphosphate 2-kinases (IP 2-Ks) are part of a family of enzymes in charge of synthesizing inositol hexakisphosphate (IP ) in eukaryotic cells. This protein and its product IP present many roles in cells, participating in mRNA export, embryonic development, and apoptosis. We reported previously that the full-length IP 2-K from is a zinc metallo-enzyme, including two separated lobes (the N- and C-lobes). We have also shown conformational changes in IP 2-K and have identified the residues involved in substrate recognition and catalysis. However, the specific features of mammalian IP 2-Ks remain unknown. To this end, we report here the first structure for a murine IP 2-K in complex with ATP/IP or IP Our structural findings indicated that the general folding in N- and C-lobes is conserved with IP 2-K. A helical scaffold in the C-lobe constitutes the inositol phosphate-binding site, which, along with the participation of the N-lobe, endows high specificity to this protein. However, we also noted large structural differences between the orthologues from these two eukaryotic kingdoms. These differences include a novel zinc-binding site and regions unique to the mammalian IP 2-K, as an unexpected basic patch on the protein surface. In conclusion, our findings have uncovered distinct features of a mammalian IP 2-K and set the stage for investigations into protein-protein or protein-RNA interactions important for IP 2-K function and activity.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/química
Fosfatos de Inositol/química
Fosfotransferases (Aceptor do Grupo Fosfato)/química
[Mh] Termos MeSH secundário: Animais
Arabidopsis/enzimologia
Proteínas de Arabidopsis/química
Sítios de Ligação
Cristalografia por Raios X
Camundongos
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Inositol Phosphates); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.4.- (Phosphotransferases (Phosphate Group Acceptor)); EC 2.7.4.21 (inositol hexakisphosphate kinase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171229
[Lr] Data última revisão:
171229
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.780395


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[PMID]:27776974
[Au] Autor:Shears SB; Baughman BM; Gu C; Nair VS; Wang H
[Ad] Endereço:Laboratory of Signal Transduction, National Institute of Environmental Health Sciences, National Institutes of Health, 101 T.W. Alexander Drive, Research Triangle Park, NC, 27709, USA. Electronic address: shears@niehs.nih.gov.
[Ti] Título:The significance of the 1-kinase/1-phosphatase activities of the PPIP5K family.
[So] Source:Adv Biol Regul;63:98-106, 2017 Jan.
[Is] ISSN:2212-4934
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The inositol pyrophosphates (diphosphoinositol polyphosphates), which include 1-InsP , 5-InsP , and InsP , are highly 'energetic' signaling molecules that play important roles in many cellular processes, particularly with regards to phosphate and bioenergetic homeostasis. Two classes of kinases synthesize the PP-InsPs: IP6Ks and PPIP5Ks. The significance of the IP6Ks - and their 5-InsP product - has been widely reported. However, relatively little is known about the biological significance of the PPIP5Ks. The purpose of this review is to provide an update on developments in our understanding of key features of the PPIP5Ks, which we believe strengthens the hypothesis that their catalytic activities serve important cellular functions. Central to this discussion is the recent discovery that the PPIP5K is a rare example of a single protein that catalyzes a kinase/phosphatase futile cycle.
[Mh] Termos MeSH primário: Hidrolases Anidrido Ácido/metabolismo
Fosfatos de Inositol/metabolismo
Fosfotransferases (Aceptor do Grupo Fosfato)/metabolismo
Ácido Fítico/metabolismo
[Mh] Termos MeSH secundário: Hidrolases Anidrido Ácido/genética
Motivos de Aminoácidos
Metabolismo Energético/genética
Regulação da Expressão Gênica
Seres Humanos
Fosfotransferases (Aceptor do Grupo Fosfato)/química
Fosfotransferases (Aceptor do Grupo Fosfato)/genética
Domínios Proteicos
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Inositol Phosphates); 0 (inositol heptakisphosphate); 7IGF0S7R8I (Phytic Acid); EC 2.7.4.- (Phosphotransferases (Phosphate Group Acceptor)); EC 2.7.4.21 (PPIP5K1 protein, human); EC 3.6.- (Acid Anhydride Hydrolases); EC 3.6.1.- (diphosphoinositol polyphosphate phosphohydrolase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE


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[PMID]:28413866
[Au] Autor:Moriya Y; Nagata E; Fujii N; Satoh T; Ogawa H; Hadano S; Takizawa S
[Ad] Endereço:Department of Neurology, Tokai University school of Medicine, 143 Shimokasuya, Isehara, Kanagawa 259-1193, Japan. moriya-y@is.icc.u-tokai.ac.jp.
[Ti] Título:Inositol Hexakisphosphate Kinase 2 is a Presymptomatic Biomarker for Amyotrophic Lateral Sclerosis.
[So] Source:Tokai J Exp Clin Med;42(1):13-18, 2017 Apr 20.
[Is] ISSN:2185-2243
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Inositol hexakisphosphate kinase 2 (InsP K2), an enzyme that converts inositol hexakisphosphate (InsP ) to diphosphoinositol pentakisphosphate (InsP ), induces cell death. InsP K2 is abundant in the central nervous system, especially anterior horn cells of spinal cord. To identify the role of InsP K2 in amyotrophic lateral sclerosis (ALS), we investigated the expression levels of InsP K2 in transgenic mice expressing mutant superoxide dismutase-1 (SOD1) (mSOD1 Tg mice). METHODS: The specimens of spinal cords were obtained from mSOD1 Tg mice and age-matched wild-type mice. We investigated the expression of InsP K2 at the gene and protein levels of the spinal cord in mSOD1 Tg and wild-type mice. RESULTS: The gene expression levels of InsP K2 in mSOD1 Tg mice was significantly higher than that in wild-type mice before ALS symptoms developed. In immunohistochemistry and western blotting results showed that InsP K2 translocated from the nucleus to the cytoplasm in mSOD1 Tg mice. CONCLUSION: These findings suggest that InsP K2 activates in mSOD1 Tg mice before the onset of ALS. Therefore, InsP K2 might be a presymptomatic biomarker for ALS.
[Mh] Termos MeSH primário: Esclerose Amiotrófica Lateral/diagnóstico
Fosfotransferases (Aceptor do Grupo Fosfato)/análise
Medula Espinal/metabolismo
[Mh] Termos MeSH secundário: Animais
Biomarcadores/análise
Western Blotting
Modelos Animais de Doenças
Diagnóstico Precoce
Expressão Gênica
Imuno-Histoquímica
Camundongos Transgênicos
Mutação
Fosfotransferases (Aceptor do Grupo Fosfato)/genética
Superóxido Dismutase-1/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); EC 1.15.1.1 (Sod1 protein, mouse); EC 1.15.1.1 (Superoxide Dismutase-1); EC 2.7.4.- (Phosphotransferases (Phosphate Group Acceptor)); EC 2.7.4.21 (IP6K1 protein, human)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170428
[Lr] Data última revisão:
170428
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170418
[St] Status:MEDLINE


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[PMID]:28208713
[Au] Autor:Williams EJ; Baines KJ; Berthon BS; Wood LG
[Ad] Endereço:Priority Research Centre for Healthy Lungs, Hunter Medical Research Institute, University of Newcastle, Callaghan NSW 2308, Australia. evan.j.williams@uon.edu.au.
[Ti] Título:Effects of an Encapsulated Fruit and Vegetable Juice Concentrate on Obesity-Induced Systemic Inflammation: A Randomised Controlled Trial.
[So] Source:Nutrients;9(2), 2017 Feb 08.
[Is] ISSN:2072-6643
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Phytochemicals from fruit and vegetables reduce systemic inflammation. This study examined the effects of an encapsulated fruit and vegetable (F&V) juice concentrate on systemic inflammation and other risk factors for chronic disease in overweight and obese adults. A double-blinded, parallel, randomized placebo-controlled trial was conducted in 56 adults aged ≥40 years with a body mass index (BMI) ≥28 kg/m². Before and after eight weeks daily treatment with six capsules of F&V juice concentrate or placebo, peripheral blood gene expression (microarray, quantitative polymerase chain reaction (qPCR)), plasma tumour necrosis factor (TNF)α (enzyme-linked immunosorbent assay (ELISA)), body composition (Dual-energy X-ray absorptiometry (DEXA)) and lipid profiles were assessed. Following consumption of juice concentrate, total cholesterol, low-density lipoprotein (LDL) cholesterol and plasma TNFα decreased and total lean mass increased, while there was no change in the placebo group. In subjects with high systemic inflammation at baseline (serum C-reactive protein (CRP) ≥3.0 mg/mL) who were supplemented with the F&V juice concentrate ( = 16), these effects were greater, with decreased total cholesterol, LDL cholesterol and plasma TNFα and increased total lean mass; plasma CRP was unchanged by the F&V juice concentrate following both analyses. The expression of several genes involved in lipogenesis, the nuclear factor-κB (NF-κB) and 5' adenosine monophosphate-activated protein kinase (AMPK) signalling pathways was altered, including phosphomevalonate kinase (PMVK), zinc finger AN1-type containing 5 (ZFAND5) and calcium binding protein 39 (CAB39), respectively. Therefore, F&V juice concentrate improves the metabolic profile, by reducing systemic inflammation and blood lipid profiles and, thus, may be useful in reducing the risk of obesity-induced chronic disease.
[Mh] Termos MeSH primário: Sucos de Frutas e Vegetais
Frutas/química
Inflamação/dietoterapia
Obesidade/dietoterapia
Verduras/química
[Mh] Termos MeSH secundário: Proteínas Quinases Ativadas por AMP/genética
Proteínas Quinases Ativadas por AMP/metabolismo
Absorciometria de Fóton
Adulto
Composição Corporal
Índice de Massa Corporal
Proteína C-Reativa/análise
Proteínas de Ligação ao Cálcio/genética
Proteínas de Ligação ao Cálcio/metabolismo
Carotenoides/sangue
HDL-Colesterol/sangue
LDL-Colesterol/sangue
Dieta
Método Duplo-Cego
Feminino
Seres Humanos
Inflamação/sangue
Inflamação/etiologia
Masculino
Meia-Idade
NF-kappa B/genética
NF-kappa B/metabolismo
Obesidade/sangue
Obesidade/complicações
Fosfotransferases (Aceptor do Grupo Fosfato)/genética
Fosfotransferases (Aceptor do Grupo Fosfato)/metabolismo
Proteínas/genética
Proteínas/metabolismo
Fator de Necrose Tumoral alfa/sangue
Circunferência da Cintura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RANDOMIZED CONTROLLED TRIAL
[Nm] Nome de substância:
0 (Calcium-Binding Proteins); 0 (Cholesterol, HDL); 0 (Cholesterol, LDL); 0 (Mo25 protein, human); 0 (NF-kappa B); 0 (Proteins); 0 (Tumor Necrosis Factor-alpha); 0 (ZFAND5 protein, human); 36-88-4 (Carotenoids); 9007-41-4 (C-Reactive Protein); EC 2.7.11.31 (AMP-Activated Protein Kinases); EC 2.7.4.- (Phosphotransferases (Phosphate Group Acceptor)); EC 2.7.4.2 (phosphomevalonate kinase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170218
[St] Status:MEDLINE


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[PMID]:28126903
[Au] Autor:Gu C; Nguyen HN; Hofer A; Jessen HJ; Dai X; Wang H; Shears SB
[Ad] Endereço:From the Laboratory of Signal Transduction, NIEHS, National Institutes of Health, Research Triangle Park, North Carolina, 27709.
[Ti] Título:The Significance of the Bifunctional Kinase/Phosphatase Activities of Diphosphoinositol Pentakisphosphate Kinases (PPIP5Ks) for Coupling Inositol Pyrophosphate Cell Signaling to Cellular Phosphate Homeostasis.
[So] Source:J Biol Chem;292(11):4544-4555, 2017 Mar 17.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Proteins responsible for P homeostasis are critical for all life. In , extracellular [P ] is "sensed" by the inositol-hexakisphosphate kinase (IP6K) that synthesizes the intracellular inositol pyrophosphate 5-diphosphoinositol 1,2,3,4,6-pentakisphosphate (5-InsP ) as follows: during a period of P starvation, there is a decline in cellular [ATP]; the unusually low affinity of IP6Ks for ATP compels 5-InsP levels to fall in parallel (Azevedo, C., and Saiardi, A. (2017) 42, 219-231. Hitherto, such P sensing has not been documented in metazoans. Here, using a human intestinal epithelial cell line (HCT116), we show that levels of both 5-InsP and ATP decrease upon [P ] starvation and subsequently recover during P replenishment. However, a separate inositol pyrophosphate, 1,5-bisdiphosphoinositol 2,3,4,6-tetrakisphosphate (InsP ), reacts more dramatically ( with a wider dynamic range and greater sensitivity). To understand this novel InsP response, we characterized kinetic properties of the bifunctional 5-InsP kinase/InsP phosphatase activities of full-length diphosphoinositol pentakisphosphate kinases (PPIP5Ks). These data fulfil previously published criteria for any bifunctional kinase/phosphatase to exhibit concentration robustness, permitting levels of the kinase product (InsP in this case) to fluctuate independently of varying precursor ( 5-InsP ) pool size. Moreover, we report that InsP phosphatase activities of PPIP5Ks are strongly inhibited by P (40-90% within the 0-1 mm range). For PPIP5K2, P sensing by InsP is amplified by a 2-fold activation of 5-InsP kinase activity by P within the 0-5 mm range. Overall, our data reveal mechanisms that can contribute to specificity in inositol pyrophosphate signaling, regulating InsP turnover independently of 5-InsP , in response to fluctuations in extracellular supply of a key nutrient.
[Mh] Termos MeSH primário: Fosfatos de Inositol/metabolismo
Fosfotransferases (Aceptor do Grupo Fosfato)/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Hidrolases Anidrido Ácido/metabolismo
Trifosfato de Adenosina/metabolismo
Células HCT116
Células HEK293
Homeostase
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Inositol Phosphates); 148077-18-3 (1-diphosphoinositol pentakisphosphate); 55780-80-8 (inositol-1-pyrophosphate); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.4.- (Phosphotransferases (Phosphate Group Acceptor)); EC 2.7.4.21 (PPIP5K1 protein, human); EC 2.7.4.24 (PPIP5K2 protein, human); EC 3.6.- (Acid Anhydride Hydrolases); EC 3.6.1.- (diphosphoinositol polyphosphate phosphohydrolase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170128
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.765743


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[PMID]:28031352
[Au] Autor:Hove-Jensen B; Andersen KR; Kilstrup M; Martinussen J; Switzer RL; Willemoës M
[Ad] Endereço:DTU Systems Biology, Technical University of Denmark, Kongens Lyngby, Denmark hove@mbg.au.dk.
[Ti] Título:Phosphoribosyl Diphosphate (PRPP): Biosynthesis, Enzymology, Utilization, and Metabolic Significance.
[So] Source:Microbiol Mol Biol Rev;81(1), 2017 Mar.
[Is] ISSN:1098-5557
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phosphoribosyl diphosphate (PRPP) is an important intermediate in cellular metabolism. PRPP is synthesized by PRPP synthase, as follows: ribose 5-phosphate + ATP → PRPP + AMP. PRPP is ubiquitously found in living organisms and is used in substitution reactions with the formation of glycosidic bonds. PRPP is utilized in the biosynthesis of purine and pyrimidine nucleotides, the amino acids histidine and tryptophan, the cofactors NAD and tetrahydromethanopterin, arabinosyl monophosphodecaprenol, and certain aminoglycoside antibiotics. The participation of PRPP in each of these metabolic pathways is reviewed. Central to the metabolism of PRPP is PRPP synthase, which has been studied from all kingdoms of life by classical mechanistic procedures. The results of these analyses are unified with recent progress in molecular enzymology and the elucidation of the three-dimensional structures of PRPP synthases from eubacteria, archaea, and humans. The structures and mechanisms of catalysis of the five diphosphoryltransferases are compared, as are those of selected enzymes of diphosphoryl transfer, phosphoryl transfer, and nucleotidyl transfer reactions. PRPP is used as a substrate by a large number phosphoribosyltransferases. The protein structures and reaction mechanisms of these phosphoribosyltransferases vary and demonstrate the versatility of PRPP as an intermediate in cellular physiology. PRPP synthases appear to have originated from a phosphoribosyltransferase during evolution, as demonstrated by phylogenetic analysis. PRPP, furthermore, is an effector molecule of purine and pyrimidine nucleotide biosynthesis, either by binding to PurR or PyrR regulatory proteins or as an allosteric activator of carbamoylphosphate synthetase. Genetic analyses have disclosed a number of mutants altered in the PRPP synthase-specifying genes in humans as well as bacterial species.
[Mh] Termos MeSH primário: Archaea/metabolismo
Bactérias/metabolismo
Metabolismo Energético/fisiologia
Fungos/metabolismo
Peptídeo Sintases/química
Fosforribosil Pirofosfato/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Archaea/enzimologia
Bactérias/enzimologia
Fungos/enzimologia
Seres Humanos
Fosforribosil Pirofosfato/biossíntese
Fosfotransferases (Aceptor do Grupo Fosfato)
Estrutura Secundária de Proteína
Ribosemonofosfatos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Ribosemonophosphates); 4B2428FLTO (ribose-5-phosphate); 7540-64-9 (Phosphoribosyl Pyrophosphate); EC 2.7.4.- (Phosphotransferases (Phosphate Group Acceptor)); EC 6.3.2.- (Peptide Synthases); EC 6.3.2.- (lipoate-protein ligase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161230
[St] Status:MEDLINE


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[PMID]:27941389
[Au] Autor:Cleophas MC; Crisan TO; Joosten LA
[Ad] Endereço:aDepartment of Internal Medicine bRadboud Institute for Molecular Life Sciences, Radboud University Medical Center, Nijmegen, The Netherlands cDepartment of Medical Genetics, Iuliu Hatieganu University of Medicine and Pharmacy, Cluj-Napoca, Romania.
[Ti] Título:Factors modulating the inflammatory response in acute gouty arthritis.
[So] Source:Curr Opin Rheumatol;29(2):163-170, 2017 Mar.
[Is] ISSN:1531-6963
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PURPOSE OF REVIEW: Gout is a common debilitating form of arthritis and despite our extensive knowledge on the pathogenesis its prevalence is still rising quickly. In the current review, we provide a concise overview of recent discoveries in factors tuning the inflammatory response to soluble uric acid and monosodium urate crystals. RECENT FINDINGS: It appears that soluble uric acid has a much larger role to play than just being a risk factor for gout. It may have widespread consequences for systemic inflammation and the development of metabolic syndrome. Additionally, a specific gout-related gut microbiome might not only provide us with a new diagnostic tool, but also highlights possible new therapeutic targets. Furthermore, several recent publications further elucidated the roles of mitochondrial dysfunction, production of reactive oxygen species, autophagy, and AMP-dependent protein kinase in monosodium urate-induced NLRP3 inflammasome activation. Finally, neutrophils have been shown to be involved in both the promotion and resolution of gouty inflammation. A new alpha-1-antitrypsin fusion protein may limit the proinflammatory effects of neutrophil-derived serine proteases. SUMMARY: Together, these studies provide us with many new insights in the pathogenesis of gout, important new treatment targets, and a rationale to further study the role of soluble uric acid in inflammatory diseases.
[Mh] Termos MeSH primário: Artrite Gotosa/imunologia
Microbioma Gastrointestinal/imunologia
Hiperuricemia/imunologia
Ácido Úrico/imunologia
[Mh] Termos MeSH secundário: Autofagia/imunologia
Gota/imunologia
Seres Humanos
Inflamassomos/imunologia
Inflamação
Mitocôndrias/imunologia
Proteína 3 que Contém Domínio de Pirina da Família NLR/imunologia
Neutrófilos/imunologia
Estresse Oxidativo
Fosfotransferases (Aceptor do Grupo Fosfato)/imunologia
Espécies Reativas de Oxigênio/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Inflammasomes); 0 (NLR Family, Pyrin Domain-Containing 3 Protein); 0 (Reactive Oxygen Species); 268B43MJ25 (Uric Acid); EC 2.7.4.- (AMP-dependent kinase (ATP-forming)); EC 2.7.4.- (Phosphotransferases (Phosphate Group Acceptor))
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170720
[Lr] Data última revisão:
170720
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161213
[St] Status:MEDLINE
[do] DOI:10.1097/BOR.0000000000000366


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[PMID]:27919691
[Au] Autor:Zhang X; Wu H; Huang B; Li Z; Ye Q
[Ad] Endereço:State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, Shanghai 200237, China.
[Ti] Título:One-pot synthesis of glutathione by a two-enzyme cascade using a thermophilic ATP regeneration system.
[So] Source:J Biotechnol;241:163-169, 2017 Jan 10.
[Is] ISSN:1873-4863
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:In vitro cascade catalysis using enzyme-based system is becoming a promising biomanufacturing platform for biofuels and biochemicals production. Glutathione is a pivotal non-protein thiol compound and widely applied in food and pharmaceutical industries. In this study, glutathione was synthesized by a bifunctional glutathione synthetase together with a thermophilic ATP regeneration system through a two-enzyme cascade in vitro. Four bifunctional glutathione synthetases from Streptococcus sanguinis, S. gordonii, S. uberis and Bacillus cereus were applied for glutathione synthesis. The bifunctional glutathione synthetase from S. sanguinis was selected and coupled with the polyphosphate kinase from Thermosynechococcus elongatus BP-1 for regenerating ATP to produce glutathione in one pot. In the optimized system, 28.5mM glutathione was produced within 5h due to efficient ATP regeneration from low-cost polyphosphate. The yield based on added l-cysteine reached 81.4% and the productivity of glutathione achieved 5.7mM/h. The one-pot system indicated a potential biotransformation platform for industrial production of glutathione.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Proteínas de Bactérias/metabolismo
Glutationa Sintase/metabolismo
Glutationa/metabolismo
Fosfotransferases (Aceptor do Grupo Fosfato)/metabolismo
Proteínas Recombinantes/metabolismo
[Mh] Termos MeSH secundário: Bacillus cereus/enzimologia
Bacillus cereus/genética
Proteínas de Bactérias/genética
Escherichia coli/genética
Escherichia coli/metabolismo
Glutationa/análise
Glutationa Sintase/genética
Engenharia Metabólica
Fosfotransferases (Aceptor do Grupo Fosfato)/genética
Polifosfatos/metabolismo
Proteínas Recombinantes/genética
Streptococcus/enzimologia
Streptococcus/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Polyphosphates); 0 (Recombinant Proteins); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.4.- (Phosphotransferases (Phosphate Group Acceptor)); EC 2.7.4.1 (polyphosphate kinase); EC 6.3.2.3 (Glutathione Synthase); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170228
[Lr] Data última revisão:
170228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161207
[St] Status:MEDLINE


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[PMID]:27822701
[Au] Autor:Meyer BH; Shams-Eldin H; Albers SV
[Ad] Endereço:Molecular Biology of Archaea, Institute of Biology, University of Freiburg, Schaenzlestrasse 1, 79211, Freiburg, Germany.
[Ti] Título:AglH, a thermophilic UDP-N-acetylglucosamine-1-phosphate:dolichyl phosphate GlcNAc-1-phosphotransferase initiating protein N-glycosylation pathway in Sulfolobus acidocaldarius, is capable of complementing the eukaryal Alg7.
[So] Source:Extremophiles;21(1):121-134, 2017 Jan.
[Is] ISSN:1433-4909
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:AglH, a predicted UDP-GlcNAc-1-phosphate:dolichyl phosphate GlcNAc-1-phosphotransferase, is initiating the protein N-glycosylation pathway in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius. AglH successfully replaced the endogenous GlcNAc-1-phosphotransferase activity of Alg7 in a conditional lethal Saccharomyces cerevisiae strain, in which the first step of the eukaryal protein N-glycosylation process was repressed. This study is one of the few examples of cross-domain complementation demonstrating a conserved polyprenyl phosphate transferase reaction within the eukaryal and archaeal domain like it was demonstrated for Methanococcus voltae (Shams-Eldin et al. 2008). The topology prediction and the alignment of the AglH membrane protein with GlcNAc-1-phosphotransferases from the three domains of life show significant conservation of amino acids within the different proposed cytoplasmic loops. Alanine mutations of selected conserved amino acids in the putative cytoplasmic loops II (D ), IV (F ) and V (F ) demonstrated the importance of these amino acids for cross-domain AlgH activity in in vitro complementation assays in S. cerevisiae. Furthermore, antibiotic treatment interfering directly with the activity of dolichyl phosphate GlcNAc-1-phosphotransferases confirmed the essentiality of N-glycosylation for cell survival.
[Mh] Termos MeSH primário: Proteínas Arqueais/genética
Sulfolobus acidocaldarius/enzimologia
Transferases (Outros Grupos de Fosfato Substituídos)/genética
[Mh] Termos MeSH secundário: Proteínas Arqueais/química
Proteínas Arqueais/metabolismo
Sequência Conservada
Teste de Complementação Genética
Fosfotransferases (Aceptor do Grupo Fosfato)/genética
Domínios Proteicos
Saccharomyces cerevisiae/enzimologia
Saccharomyces cerevisiae/genética
Sulfolobus acidocaldarius/genética
Transferases (Outros Grupos de Fosfato Substituídos)/química
Transferases (Outros Grupos de Fosfato Substituídos)/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); EC 2.7.4.- (Alg7 protein, S cerevisiae); EC 2.7.4.- (Phosphotransferases (Phosphate Group Acceptor)); EC 2.7.8.- (Transferases (Other Substituted Phosphate Groups)); EC 2.7.8.15 (UDPacetylglucosamine-dolichyl-phosphate acetylglucosamine-1-phosphate transferase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM; S
[Da] Data de entrada para processamento:161109
[St] Status:MEDLINE
[do] DOI:10.1007/s00792-016-0890-2



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