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[PMID]:28742244
[Au] Autor:Porrmann J; Betcheva-Krajcir E; Di Donato N; Kahlert AK; Schallner J; Rump A; Schröck E; Dobritzsch D; Roelofsen J; van Kuilenburg ABP; Tzschach A
[Ad] Endereço:Institut für Klinische Genetik, Technische Universität Dresden, Dresden, Germany.
[Ti] Título:Novel PRPS1 gain-of-function mutation in a patient with congenital hyperuricemia and facial anomalies.
[So] Source:Am J Med Genet A;173(10):2736-2742, 2017 Oct.
[Is] ISSN:1552-4833
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phosphoribosylpyrophosphate synthetase (PRPPS) superactivity (OMIM 300661) is a rare inborn error of purine metabolism that is caused by gain-of-function mutations in the X-chromosomal gene PRPS1 (Xq22.3). Clinical characteristics include congenital hyperuricemia and hyperuricosuria, gouty arthritis, urolithiasis, developmental delay, hypotonia, recurrent infections, short stature, and hearing loss. Only eight families with PRPPS superactivity and PRPS1 gain-of-function mutations have been reported to date. We report on a 7-year-old boy with congenital hyperuricemia, urolithiasis, developmental delay, short stature, hypospadias, and facial dysmorphisms. His mother also suffered from hyperuricemia that was diagnosed at age 13 years. A novel PRPS1 missense mutation (c.573G>C, p.[Leu191Phe]) was detected in the proband and his mother. Enzyme activity analysis confirmed superactivity of PRPP synthetase. Analysis of the crystal structure of human PRPPS suggests that the Leu191Phe mutation affects the architecture of both allosteric sites, thereby preventing the allosteric inhibition of the enzyme. The family reported here broadens the clinical spectrum of PRPPS superactivity and indicates that this rare metabolic disorder might be associated with a recognizable facial gestalt.
[Mh] Termos MeSH primário: Face/anormalidades
Mutação com Ganho de Função
Hiperuricemia/congênito
Hiperuricemia/genética
Ribose-Fosfato Pirofosfoquinase/genética
[Mh] Termos MeSH secundário: Criança
Face/patologia
Seres Humanos
Hiperuricemia/patologia
Masculino
Erros Inatos do Metabolismo da Purina-Pirimidina/genética
Erros Inatos do Metabolismo da Purina-Pirimidina/metabolismo
Ribose-Fosfato Pirofosfoquinase/metabolismo
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.7.6.1 (PRPS1 protein, human); EC 2.7.6.1 (Ribose-Phosphate Pyrophosphokinase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.1002/ajmg.a.38359


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[PMID]:28419153
[Au] Autor:Donini S; Garavaglia S; Ferraris DM; Miggiano R; Mori S; Shibayama K; Rizzi M
[Ad] Endereço:Department of Pharmaceutical Sciences, Università del Piemonte Orientale "A. Avogadro", Largo Donegani 2, Novara, Italy.
[Ti] Título:Biochemical and structural investigations on phosphoribosylpyrophosphate synthetase from Mycobacterium smegmatis.
[So] Source:PLoS One;12(4):e0175815, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mycobacterium smegmatis represents one model for studying the biology of its pathogenic relative Mycobacterium tuberculosis. The structural characterization of a M. tuberculosis ortholog protein can serve as a valid tool for the development of molecules active against the M. tuberculosis target. In this context, we report the biochemical and structural characterization of M. smegmatis phosphoribosylpyrophosphate synthetase (PrsA), the ortholog of M. tuberculosis PrsA, the unique enzyme responsible for the synthesis of phosphoribosylpyrophosphate (PRPP). PRPP is a key metabolite involved in several biosynthetic pathways including those for histidine, tryptophan, nucleotides and decaprenylphosphoryl-arabinose, an essential precursor for the mycobacterial cell wall biosynthesis. Since M. tuberculosis PrsA has been validated as a drug target for the development of antitubercular agents, the data presented here will add to the knowledge of the mycobacterial enzyme and could contribute to the development of M. tuberculosis PrsA inhibitors of potential pharmacological interest.
[Mh] Termos MeSH primário: Infecções por Micobactéria não Tuberculosa/microbiologia
Mycobacterium smegmatis/enzimologia
Ribose-Fosfato Pirofosfoquinase/química
Ribose-Fosfato Pirofosfoquinase/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Antibacterianos/farmacologia
Domínio Catalítico
Cristalografia por Raios X
Descoberta de Drogas
Seres Humanos
Modelos Moleculares
Terapia de Alvo Molecular
Infecções por Micobactéria não Tuberculosa/tratamento farmacológico
Mycobacterium smegmatis/química
Mycobacterium smegmatis/efeitos dos fármacos
Mycobacterium smegmatis/metabolismo
Conformação Proteica
Alinhamento de Sequência
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); EC 2.7.6.1 (Ribose-Phosphate Pyrophosphokinase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170505
[Lr] Data última revisão:
170505
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170419
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0175815


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[PMID]:28358323
[Au] Autor:Yu H; Zhang Y; Zhang D; Lu Y; He H; Zheng F; Wang M
[Ad] Endereço:Hainan Key Laboratory for Sustainable Utilization of Tropical Bioresource, Institute of Tropical Agriculture and Forestry, Hainan University, Haikou 570228, China. yuhaiyang@hainu.edu.cn.
[Ti] Título:Identification of a Ribose-Phosphate Pyrophosphokinase that Can Interact In Vivo with the Anaphase Promoting Complex/Cyclosome.
[So] Source:Int J Mol Sci;18(4), 2017 Mar 30.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:5-Phospho-d-ribosyl-1-diphosphate (PRPP) synthase (PRS) catalyzes the biosynthesis of PRPP, which is an important compound of metabolism in most organisms. However, no genes have been cloned, let alone studied for their biological function in rubber tree. In this study, we identify a novel protein (PRS4) that interacts in vivo with rubber tree anaphase promoting complex/cyclosome (APC/C) subunit 10 (HbAPC10) by yeast two-hybrid assays. has been cloned from rubber tree and named as . Blastp search in the genome of showed that HbPRS4 shared the highest similarity with AtPRS4, with 80.71% identity. qRT-PCR was used to determine the expression of in different tissues and under various treatments. was preferentially expressed in the bark. Moreover, the expression level of was significantly induced by the proteasome inhibitor MG132 treatment, suggesting it might be regulated by the ubiquitin/26S proteasome pathway. The amount of transcript was obviously decreased after mechanical wounding and abscisic acid (ABA) treatments, while a slight increase was observed at 24 h after ABA treatment. transcript in the latex was significantly upregulated by ethephon (ET) and methyl jasmonate (MeJA) treatments. These results suggested that HbPRS4 may be a specific substrate of HbAPC10 indirectly regulating natural rubber biosynthesis in rubber tree.
[Mh] Termos MeSH primário: Ciclossomo-Complexo Promotor de Anáfase/metabolismo
Proteínas de Plantas/metabolismo
Ribose-Fosfato Pirofosfoquinase/metabolismo
[Mh] Termos MeSH secundário: Ácido Abscísico/farmacologia
Acetatos/farmacologia
Ciclopentanos/farmacologia
Regulação da Expressão Gênica de Plantas/efeitos dos fármacos
Hevea/genética
Hevea/metabolismo
Leupeptinas/farmacologia
Oxilipinas/farmacologia
Casca de Planta/metabolismo
Proteínas de Plantas/química
Proteínas de Plantas/genética
Ligação Proteica
Ribose-Fosfato Pirofosfoquinase/química
Ribose-Fosfato Pirofosfoquinase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acetates); 0 (Cyclopentanes); 0 (Leupeptins); 0 (Oxylipins); 0 (Plant Proteins); 72S9A8J5GW (Abscisic Acid); 900N171A0F (methyl jasmonate); EC 2.3.2.27 (Anaphase-Promoting Complex-Cyclosome); EC 2.7.6.1 (Ribose-Phosphate Pyrophosphokinase); RF1P63GW3K (benzyloxycarbonylleucyl-leucyl-leucine aldehyde)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170507
[Lr] Data última revisão:
170507
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170331
[St] Status:MEDLINE


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[PMID]:28346452
[Au] Autor:Wang X; Yang K; Xie Q; Wu Q; Mack SC; Shi Y; Kim LJY; Prager BC; Flavahan WA; Liu X; Singer M; Hubert CG; Miller TE; Zhou W; Huang Z; Fang X; Regev A; Suvà ML; Hwang TH; Locasale JW; Bao S; Rich JN
[Ad] Endereço:Department of Stem Cell Biology and Regenerative Medicine, Cleveland Clinic Lerner Research Institute, Cleveland, Ohio, USA.
[Ti] Título:Purine synthesis promotes maintenance of brain tumor initiating cells in glioma.
[So] Source:Nat Neurosci;20(5):661-673, 2017 May.
[Is] ISSN:1546-1726
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Brain tumor initiating cells (BTICs), also known as cancer stem cells, hijack high-affinity glucose uptake active normally in neurons to maintain energy demands. Here we link metabolic dysregulation in human BTICs to a nexus between MYC and de novo purine synthesis, mediating glucose-sustained anabolic metabolism. Inhibiting purine synthesis abrogated BTIC growth, self-renewal and in vivo tumor formation by depleting intracellular pools of purine nucleotides, supporting purine synthesis as a potential therapeutic point of fragility. In contrast, differentiated glioma cells were unaffected by the targeting of purine biosynthetic enzymes, suggesting selective dependence of BTICs. MYC coordinated the control of purine synthetic enzymes, supporting its role in metabolic reprogramming. Elevated expression of purine synthetic enzymes correlated with poor prognosis in glioblastoma patients. Collectively, our results suggest that stem-like glioma cells reprogram their metabolism to self-renew and fuel the tumor hierarchy, revealing potential BTIC cancer dependencies amenable to targeted therapy.
[Mh] Termos MeSH primário: Células-Tronco Neoplásicas/metabolismo
Proteínas Proto-Oncogênicas c-myc/metabolismo
Purinas/biossíntese
[Mh] Termos MeSH secundário: Monofosfato de Adenosina/biossíntese
Proliferação Celular/fisiologia
Células Cultivadas
Genômica
Glioma/enzimologia
Glioma/metabolismo
Glicólise/fisiologia
Guanosina Monofosfato/biossíntese
Seres Humanos
Metabolômica
Células-Tronco Neoplásicas/enzimologia
Células-Tronco Neoplásicas/fisiologia
Ribose-Fosfato Pirofosfoquinase/biossíntese
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MYC protein, human); 0 (Proto-Oncogene Proteins c-myc); 0 (Purines); 415SHH325A (Adenosine Monophosphate); 85-32-5 (Guanosine Monophosphate); EC 2.7.6.1 (PRPS1 protein, human); EC 2.7.6.1 (Ribose-Phosphate Pyrophosphokinase); W60KTZ3IZY (purine)
[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:170328
[St] Status:MEDLINE
[do] DOI:10.1038/nn.4537


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[PMID]:28277197
[Au] Autor:Jiang P; Wei WF; Zhong GW; Zhou XG; Qiao WR; Fisher R; Lu L
[Ad] Endereço:1​Jiangsu Key Laboratory for Microbes and Functional Genomics, Jiangsu Engineering and Technology Research Center for Microbiology, College of Life Sciences, Nanjing Normal University, Nanjing 210023, PR China.
[Ti] Título:The function of the three phosphoribosyl pyrophosphate synthetase (Prs) genes in hyphal growth and conidiation in Aspergillus nidulans.
[So] Source:Microbiology;163(2):218-232, 2017 Feb.
[Is] ISSN:1465-2080
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Phosphoribosyl pyrophosphate synthetase, which is encoded by the Prs gene, catalyses the reaction of ribose-5-phosphate and adenine ribonucleotide triphosphate (ATP) and has central importance in cellular metabolism. However, knowledge about how Prs family members function and contribute to total 5-phosphoribosyl-α-1-pyrophosphate (PRPP) synthetase activity is limited. In this study, we identified that the filamentous fungus Aspergillus nidulans genome contains three PRPP synthase-homologous genes (AnprsA, AnprsB and AnprsC), among which AnprsB and AnprsC but not AnprsA are auxotrophic genes. Transcriptional expression profiles revealed that the mRNA levels of AnprsA, AnprsB and AnprsC are dynamic during germination, hyphal growth and sporulation and that they all showed abundant expression during the vigorous hyphal growth time point. Inhibiting the expression of AnprsB or AnprsC in conditional strains produced more effects on the total PRPP synthetase activity than did inhibiting AnprsA, thus indicating that different AnPrs proteins are unequal in their contributions to Prs enzyme activity. In addition, the constitutive overexpression of AnprsA or AnprsC could significantly rescue the defective phenotype of the AnprsB-absent strain, suggesting that the function of AnprsB is not a specific consequence of this auxotrophic gene but instead comes from the contribution of Prs proteins to PRPP synthetase activity.
[Mh] Termos MeSH primário: Aspergillus nidulans/genética
Aspergillus nidulans/metabolismo
Hifas/crescimento & desenvolvimento
Ribose-Fosfato Pirofosfoquinase/genética
Esporos Fúngicos/crescimento & desenvolvimento
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/química
Aspergillus nidulans/crescimento & desenvolvimento
Deleção de Genes
Técnicas de Inativação de Genes
Hifas/genética
Fosforribosil Pirofosfato/biossíntese
RNA Mensageiro/genética
Ribosemonofosfatos/química
Esporos Fúngicos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); 0 (Ribosemonophosphates); 4B2428FLTO (ribose-5-phosphate); 7540-64-9 (Phosphoribosyl Pyrophosphate); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.6.1 (Ribose-Phosphate Pyrophosphokinase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170310
[St] Status:MEDLINE
[do] DOI:10.1099/mic.0.000427


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[PMID]:28177767
[Au] Autor:He M; Chao L; You YP
[Ad] Endereço:a Department of Breast Surgery, Wuxi Second People's Hospital, Wuxi 214000, China.
[Ti] Título:PRPS1 silencing reverses cisplatin resistance in human breast cancer cells.
[So] Source:Biochem Cell Biol;95(3):385-393, 2017 Jun.
[Is] ISSN:1208-6002
[Cp] País de publicação:Canada
[La] Idioma:eng
[Ab] Resumo:PRPS1 (phosphoribosyl pyrophosphate synthetase 1), which drives the nucleotide biosynthesis pathway, modulates a variety of functions by providing central building blocks and cofactors for cell homeostasis. As tumor cells often display abnormal nucleotide metabolism, dysregulated de-novo nucleotide synthesis has potential impacts in cancers. We now report that PRPS1 is specifically and highly expressed in chemoresistant (CR) cancer cells derived from cisplatin-resistant human breast cancer cell lines SK-BR-3 and MCF-7. The inhibition of PRPS1 activity in CR cells by genetic silencing reduces cell viability and increases apoptosis in vitro, both of which can be further potentiated by cisplatin treatment. Significantly, such down-regulation of PRPS1 in CR cells when administered to nude mice enhanced the survival of those animals, as demonstrated by decreased tumor growth. Knockdown of PRPSI may cause these effects by potently inducing autonomous activation of caspase-3 and inhibiting the proliferation in the engrafted CR tumors. As a result, cisplatin sensitivity in a xenograft model of CR cancer cells can be restored by the down-regulation of PRPS1. Thus, PRPS1 inhibition may afford a therapeutic approach to relapsed patients with breast cancer, resistant to chemotherapy.
[Mh] Termos MeSH primário: Neoplasias da Mama/tratamento farmacológico
Cisplatino/farmacologia
Resistência a Medicamentos Antineoplásicos/genética
RNA Interferente Pequeno/genética
Ribose-Fosfato Pirofosfoquinase/antagonistas & inibidores
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/farmacologia
Apoptose/efeitos dos fármacos
Western Blotting
Neoplasias da Mama/genética
Neoplasias da Mama/patologia
Ciclo Celular/efeitos dos fármacos
Proliferação Celular/efeitos dos fármacos
Feminino
Inativação Gênica
Seres Humanos
Camundongos
Camundongos SCID
RNA Mensageiro/genética
Reação em Cadeia da Polimerase em Tempo Real
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Ribose-Fosfato Pirofosfoquinase/genética
Ribose-Fosfato Pirofosfoquinase/metabolismo
Transdução de Sinais
Células Tumorais Cultivadas
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (RNA, Messenger); 0 (RNA, Small Interfering); EC 2.7.6.1 (PRPS1 protein, human); EC 2.7.6.1 (Ribose-Phosphate Pyrophosphokinase); Q20Q21Q62J (Cisplatin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170815
[Lr] Data última revisão:
170815
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170209
[St] Status:MEDLINE
[do] DOI:10.1139/bcb-2016-0106


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[PMID]:27744273
[Au] Autor:Ugbogu EA; Wang K; Schweizer LM; Schweizer M
[Ad] Endereço:School of Life Sciences, Heriot-Watt University, Edinburgh EH14 4AS, UK.
[Ti] Título:Metabolic gene products have evolved to interact with the cell wall integrity pathway in Saccharomyces cerevisiae.
[So] Source:FEMS Yeast Res;16(8), 2016 Dec.
[Is] ISSN:1567-1364
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Two of the five unlinked genes theoretically capable of encoding 5-phosphoribosyl-1(α)-pyrophosphate (PRPP) synthetase (Prs) in Saccharomyces cerevisiae, PRS1 and PRS5, contain in-frame insertions which separate the cation- and PRPP-binding sites, diagnostic of Prs polypeptides. The impairment of cell wall integrity (CWI) mitogen-activated protein kinase (MAPK) cascade in strains lacking PRS1 and the synthetic lethality associated with loss of PRS1 and PRS5 imply that these insertions are not gratuitous. Coimmunoprecipitation revealed that Prs1 interacts with the CWI MAPK pathway, only when Slt2 has been phosphorylated by Mkk1/2. Three serine residues identified by phosphoproteome analysis (Ficarro et al 2002) are located in one of the insertions of PRS5 thereby defining Prs5 as one of the 11 triply phosphorylated proteins in yeast. Mutation of these phosphosites compromised the transcriptional readout of one endpoint of the CWI pathway, Rlm1, as well as the expression of the gene encoding the stress-activated 1,3 ß-glucan synthase, Fks2, regulated by a second endpoint of the CWI pathway, Swi4/Swi6 (SBF transcription factor). Therefore, the unexpected impairment of the CWI phenotype encountered in yeast strains either mutated or deleted for PRS1 or PRS5 can be explained by disruption of the communication between primary cell metabolism and CWI signalling.
[Mh] Termos MeSH primário: Parede Celular/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Evolução Molecular
Proteínas Quinases Ativadas por Mitógeno/metabolismo
Ribose-Fosfato Pirofosfoquinase/genética
Ribose-Fosfato Pirofosfoquinase/metabolismo
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Saccharomyces cerevisiae Proteins); EC 2.7.11.24 (Mitogen-Activated Protein Kinases); EC 2.7.6.1 (Ribose-Phosphate Pyrophosphokinase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170628
[Lr] Data última revisão:
170628
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161017
[St] Status:MEDLINE


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[PMID]:27517698
[Au] Autor:Bibi T; Perveen S; Aziz I; Bashir Q; Rashid N; Imanaka T; Akhtar M
[Ad] Endereço:School of Biological Sciences, University of the Punjab, Quaid-e-Azam Campus, Lahore, 54590, Pakistan.
[Ti] Título:Pcal_1127, a highly stable and efficient ribose-5-phosphate pyrophosphokinase from Pyrobaculum calidifontis.
[So] Source:Extremophiles;20(6):821-830, 2016 Nov.
[Is] ISSN:1433-4909
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Analysis of the genome sequence of Pyrobaculum calidifontis revealed the presence of an open reading frame Pcal_1127 annotated as ribose-5-phosphate pyrophosphokinase. To examine the properties of Pcal_1127 the coding gene was cloned, expressed in Escherichia coli, and the purified gene product was characterized. Pcal_1127 exhibited higher activity when ATP was replaced by dATP as pyrophosphate donor. Phosphate and EDTA activated the enzyme activity and equivalent amount of activity was detected with ATP and dATP in their presence. Recombinant Pcal_1127 could utilize all the four nucleotides as pyrophosphate donors with a marked preference for ATP. Optimum temperature and pH for the enzyme activity were 55 °C and 10.5, respectively. A unique feature of Pcal_1127 was its stability against temperature as well as denaturants. Pcal_1127 exhibited more than 95 % residual activity after heating for 4 h at 90 °C and a half-life of 15 min in the boiling water. The enzyme activity was not affected by the presence of 8 M urea or 4 M guanidinium chloride. Pcal_1127 was a highly efficient enzyme with a catalytic efficiency of 5183 mM s . These features make Pcal_1127, a novel and unique ribose-5-phosphate pyrophosphokinase.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Temperatura Alta
Pyrobaculum/enzimologia
Ribose-Fosfato Pirofosfoquinase/genética
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Estabilidade Enzimática
Pyrobaculum/genética
Ribose-Fosfato Pirofosfoquinase/química
Ribose-Fosfato Pirofosfoquinase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.6.1 (Ribose-Phosphate Pyrophosphokinase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM; S
[Da] Data de entrada para processamento:160813
[St] Status:MEDLINE


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[PMID]:27370097
[Au] Autor:Li HG; Hou PY; Zhang X; He Y; Zhang J; Wang SQ; Anderson S; Zhang YW; Wu XH
[Ad] Endereço:Tianjin Key Laboratory on Technologies Enabling Development of Clinical, Therapeutics and Diagnostics, College of Pharmacy, Tianjin Medical University, Tianjin 300070, China.
[Ti] Título:Hypouricemic effect of allopurinol are improved by Pallidifloside D based on the uric acid metabolism enzymes PRPS, HGPRT and PRPPAT.
[So] Source:Fitoterapia;113:1-5, 2016 Sep.
[Is] ISSN:1873-6971
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Allopurinol is a commonly used medication to treat hyperuricemia and its complications. Pallidifloside D, a saponin glycoside constituent from the total saponins of Smilax riparia, had been proved to enhanced hypouricemic effect of allopurinol based on uric acid metabolism enzyme XOD. In this study, we evaluated whether Pallidifloside D (5mg/kg) enhanced hypouricemic effect of allopurinol (5mg/kg) related to others uric acid metabolism enzymes such as PRPS, HGPRT and PRPPAT. We found that, compared with allopurinol alone, the combination of allopurinol and Pallidifloside D significantly up-regulated HGPRT mRNA expression and down-regulated the mRNA expression of PRPS and PRPPAT in PC12 cells (all P<0.01). These results strongly suggest that hypouricemic effect of allopurinol are improved by Pallidifloside D via numerous mechanisms and our data may have a potential value in clinical practice in the treatment of gout and other hyperuricemic conditions.
[Mh] Termos MeSH primário: Alopurinol/farmacologia
Hiperuricemia/tratamento farmacológico
Hipoxantina Fosforribosiltransferase/metabolismo
Ribose-Fosfato Pirofosfoquinase/metabolismo
Saponinas/farmacologia
Transaminases/metabolismo
[Mh] Termos MeSH secundário: Animais
Sinergismo Farmacológico
Regulação da Expressão Gênica/efeitos dos fármacos
Masculino
Camundongos
Células PC12
RNA Mensageiro/metabolismo
Ratos
Smilax/química
Ácido Úrico/sangue
Ácido Úrico/urina
Xantina Oxidase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); 0 (Saponins); 0 (pallidifloside D); 268B43MJ25 (Uric Acid); 63CZ7GJN5I (Allopurinol); EC 1.17.3.2 (Xanthine Oxidase); EC 2.4.2.8 (Hypoxanthine Phosphoribosyltransferase); EC 2.6.1.- (Transaminases); EC 2.6.1.- (phosphoribosyl pyrophosphate aminotransferase); EC 2.7.6.1 (Ribose-Phosphate Pyrophosphokinase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170131
[Lr] Data última revisão:
170131
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160703
[St] Status:MEDLINE


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[PMID]:27343059
[Au] Autor:Li C; Yan Z; Cao X; Zhang X; Yang L
[Ad] Endereço:Department of Neurosurgery, The Second Hospital of Hebei Medical University, Shijiazhuang, China.
[Ti] Título:Phosphoribosylpyrophosphate Synthetase 1 Knockdown Suppresses Tumor Formation of Glioma CD133+ Cells Through Upregulating Cell Apoptosis.
[So] Source:J Mol Neurosci;60(2):145-56, 2016 Oct.
[Is] ISSN:1559-1166
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Relapse is the main cause of mortality in patients with glioblastoma multiforme (GBM). Treatment options involve surgical resection followed by a combination of radiotheraphy and chemotherapy with temozolomide. Several genes and genetic pathways have been identified to contribute to therapeutic resistance, giving rise to recurrence of the malignancy. In the last decades, glioma stem cells (GSCs) with the capacity of self-renewal have been demonstrated to maintain tumor propagation and treatment resistance. Here, we isolated CD133-positive (CD133+) and CD133-negative (CD133-) cells from glioblastoma U98G and U87MG cell lines. The role of phosphoribosylpyrophosphate synthetase 1 (PRPS1), which catalyzes the first step of the synthesis of nucleotide, in proliferation and apoptosis was investigated. We found that PRPS1 had a remarkable effect on cell proliferation and sphere formation in both CD133+ and CD133- cells. Compared to CD133- cells, CD133+ cells exhibited more significant results in cell apoptosis assay. CD133+ T98G and U87MG cells were used in xenograft mouse model of tumor formation. Interestingly, the mice implanted with PRPS1 knockdown T98G or U87MG stem cells exhibited prolonged survival time and reduced tumor volume. By immunostaining caspase-3 in tumor tissues of these mice, we demonstrated that the apoptotic activities in tumor cells were positively correlated to the survival time but negatively correlated to PRPS1 expression. Our results indicate that PRPS1 plays an important role in proliferation and apoptosis in GSCs and provide new clues for potential PRPS1-targeted therapy in GBM treatment.
[Mh] Termos MeSH primário: Apoptose
Neoplasias Encefálicas/metabolismo
Glioma/metabolismo
Ribose-Fosfato Pirofosfoquinase/genética
[Mh] Termos MeSH secundário: Antígeno AC133/genética
Antígeno AC133/metabolismo
Animais
Neoplasias Encefálicas/patologia
Linhagem Celular Tumoral
Glioma/patologia
Seres Humanos
Masculino
Camundongos
Camundongos Endogâmicos BALB C
Ribose-Fosfato Pirofosfoquinase/metabolismo
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AC133 Antigen); EC 2.7.6.1 (PRPS1 protein, mouse); EC 2.7.6.1 (Ribose-Phosphate Pyrophosphokinase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160626
[St] Status:MEDLINE
[do] DOI:10.1007/s12031-016-0783-y



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