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  1 / 315 MEDLINE  
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PMID:28093218
Autor:Bowman A; Dowell FJ; Evans NP; Scottish SPCA
Endereço:Institute of Biodiversity, Animal Health and Comparative Medicine, College of Veterinary and LIFE Sciences, University of Glasgow, Bearsden Rd, Glasgow G61 1QH, United Kingdom. Electronic address: a.bowman.1@research.gla.ac.uk.
Título:'The effect of different genres of music on the stress levels of kennelled dogs'.
Fonte:Physiol Behav; 171:207-215, 2017 Mar 15.
ISSN:1873-507X
País de publicação:United States
Idioma:eng
Resumo:Classical music has been shown to reduce stress in kennelled dogs; however, rapid habituation of dogs to this form of auditory enrichment has also been demonstrated. The current study investigated the physiological and behavioural response of kennelled dogs (n=38) to medium-term (5days) auditory enrichment with five different genres of music including Soft Rock, Motown, Pop, Reggae and Classical, to determine whether increasing the variety of auditory stimulation reduces the level of habituation to auditory enrichment. Dogs were found to spend significantly more time lying and significantly less time standing when music was played, regardless of genre. There was no observable effect of music on barking, however, dogs were significantly (z=2.2, P<0.05) more likely to bark following cessation of auditory enrichment. Heart Rate Variability (HRV) was significantly higher, indicative of decreased stress, when dogs were played Soft Rock and Reggae, with a lesser effect observed when Motown, Pop and Classical genres were played. Relative to the silent period prior to auditory enrichment, urinary cortisol:creatanine (UCCR) values were significantly higher during Soft Rock (t=2.781, P<0.01) and the second silent control period following auditory enrichment (t=2.46, P<0.05). Despite the mixed response to different genres, the physiological and behavioural changes observed remained constant over the 5d of enrichment suggesting that the effect of habituation may be reduced by increasing the variety of auditory enrichment provided.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:EC 3.5.3.- (Ureohydrolases); EC 3.5.3.3 (creatinase); WI4X0X7BPJ (Hydrocortisone)


  2 / 315 MEDLINE  
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PMID:28077628
Autor:Bruender NA; Bandarian V
Endereço:From the Department of Chemistry, University of Utah, Salt Lake City, Utah 84112.
Título:The Creatininase Homolog MftE from Catalyzes a Peptide Cleavage Reaction in the Biosynthesis of a Novel Ribosomally Synthesized Post-translationally Modified Peptide (RiPP).
Fonte:J Biol Chem; 292(10):4371-4381, 2017 Mar 10.
ISSN:1083-351X
País de publicação:United States
Idioma:eng
Resumo:Most ribosomally synthesized and post-translationally modified peptide (RiPP) natural products are processed by tailoring enzymes to create complex natural products that are still recognizably peptide-based. However, some tailoring enzymes dismantle the peptide en route to synthesis of small molecules. A small molecule natural product of as yet unknown structure, mycofactocin, is thought to be synthesized in this way via the gene cluster found in many strains of mycobacteria. This cluster harbors at least six genes, which appear to be conserved across species. We have previously shown that one enzyme from this cluster, MftC, catalyzes the oxidative decarboxylation of the C-terminal Tyr of the substrate peptide MftA in a reaction that requires the MftB protein. Herein we show that encodes a creatininase homolog that catalyzes cleavage of the oxidatively decarboxylated MftA peptide to liberate its final two residues, including the C-terminal decarboxylated Tyr (VY*). Unlike MftC, which requires MftB for function, MftE catalyzes the cleavage reaction in the absence of MftB. The identification of this novel metabolite, VY*, supports the notion that the cluster is involved in generating a small molecule from the MftA peptide. The ability to produce VY* from MftA by reconstitution of the activities of MftB, MftC, and MftE sets the stage for identification of the novel metabolite that results from the proteins encoded by the cluster.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Bacterial Proteins); 0 (Peptide Fragments); EC 3.5.3.- (Ureohydrolases); EC 3.5.3.3 (creatinase)


  3 / 315 MEDLINE  
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PMID:27846445
Autor:Romero N; Benítez J; Garcia D; González A; Bennun L; García-Robles MA; López V; Wilson LA; Schenk G; Carvajal N; Uribe E
Endereço:Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Biológicas, Universidad de Concepción, Casilla 160-C, Concepción, Chile.
Título:Mammalian agmatinases constitute unusual members in the family of Mn -dependent ureahydrolases.
Fonte:J Inorg Biochem; 166:122-125, 2017 Jan.
ISSN:1873-3344
País de publicação:United States
Idioma:eng
Resumo:Agmatine (1-amino-4-guanidinobutane) plays an important role in a range of metabolic functions, in particular in the brain. Agmatinases (AGMs) are enzymes capable of converting agmatine to the polyamine putrescine and urea. AGMs belong to the family of Mn -dependent ureahydrolases. However, no AGM from a mammalian source has yet been extracted in catalytically active form. While in human AGM the six amino acid ligands that coordinate the two Mn ions in the active site are conserved, four mutations are observed in the murine enzyme. Here, we demonstrate that similar to its human counterpart murine AGM does not appear to have in vitro catalytic activity, independent of the presence of Mn . However, in presence of agmatine both enzymes are very efficient in promoting cell growth of a yeast strain that is deficient in polyamine biosynthesis (Saccharomyces cerevisiae strain TRY104Δspe1). Furthermore, mutations among the putative Mn binding residues had no effect on the ability of murine AGM to promote growth of the yeast culture. It thus appears that mammalian AGMs form a distinct group within the family of ureahydrolases that (i) either fold in a manner distinct from other members in this family, or (ii) require accessory proteins to bind Mn in a mechanism related to that observed for the Ni -dependent urease.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Recombinant Proteins); 42Z2K6ZL8P (Manganese); 70J407ZL5Q (Agmatine); EC 3.5.3.- (Ureohydrolases); EC 3.5.3.11 (agmatinase)


  4 / 315 MEDLINE  
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PMID:27791465
Autor:Kong J; Li Z; Zhang H; Gao XD; Nakanishi H
Endereço:a Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education , School of Biotechnology, Jiangnan University , Wuxi , China.
Título:Production of encapsulated creatinase using yeast spores.
Fonte:Bioengineered; 8(4):411-419, 2017 Jul 04.
ISSN:2165-5987
País de publicação:United States
Idioma:eng
Resumo:Yeast spores can be used as a carrier to produce enzyme capsules. In the present study, this technique was applied to a diagnostic enzyme named creatinase. We found that a secretory form of Pseudomonas putida creatinase could be entrapped in the spore wall, and such spores were used as creatinase capsules. The activity of the encapsulated creatinase was largely improved by mild spore wall defective mutations, such as DIT1 or OSW2 deletions. The advantages of this method include the following: encapsulated and freeze-dried creatinase is produced without preparing the purified enzyme, and it exhibits resistance to environmental stresses, such as high temperature and SDS treatments. Thus, yeast spores could be applied to establish quick and easy clinical diagnostic methods.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Capsules); EC 3.5.3.- (Ureohydrolases); EC 3.5.3.3 (creatinase)


  5 / 315 MEDLINE  
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PMID:27734207
Autor:Kong J; Li Z; Zhang H; Gao XD; Nakanishi H
Endereço:Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, 214122, China.
Título:Consecutive hydrolysis of creatinine using creatininase and creatinase encapsulated in Saccharomyces cerevisiae spores.
Fonte:Biotechnol Lett; 39(2):261-267, 2017 Feb.
ISSN:1573-6776
País de publicação:Netherlands
Idioma:eng
Resumo:OBJECTIVES: To achieve consecutive conversion from creatinine to urea and sarcosine using creatininase and creatinase encapsulated in spores of Saccharomyces cerevisiae. RESULTS: Creatininase encapsulated into the spore wall was produced and its specific activity was 3.4 ± 0.4 U/mg. By deletion of OSW2 gene, which causes a mild spore wall defect, the activity was increased to 10.9 ± 0.5 U/mg. Compared with soluble enzymes, spore-encapsulated creatininase was tolerant to environmental stresses; creatininase encapsulated in osw2∆ spores retained more than 90 % of the activity after treatment by SDS or proteinase K. Creatinase capsules could also be produced through spore encapsulation. The mixture of spores containing either creatininase or creatinase could mediate a two-step reaction to produce urea from creatinine; 5 mg spores produced 19 µmol urea in 10 min. Spores co-expressing creatininase and creatinase could also mediate the reactions more efficiently than the mixture of spores individually expressing each enzyme; the yield in 10 min was 38 µmol. CONCLUSIONS: Yeast spores can hold creatininase and creatinase simultaneously and catalyze the consecutive reactions.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:AYI8EX34EU (Creatinine); EC 3.5.- (Amidohydrolases); EC 3.5.2.10 (creatininase); EC 3.5.3.- (Ureohydrolases); EC 3.5.3.3 (creatinase)


  6 / 315 MEDLINE  
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PMID:27497871
Autor:Shao Y; Li C; Zhang W; Xu W; Duan X; Li Y; Qiu Q; Jin C
Endereço:School of Marine Sciences, Ningbo University, Ningbo, 315211, PR China.
Título:Cloning and comparative analysis the proximal promoter activities of arginase and agmatinase genes in Apostichopus japonicus.
Fonte:Dev Comp Immunol; 65:299-308, 2016 12.
ISSN:1879-0089
País de publicação:United States
Idioma:eng
Resumo:Our previous work demonstrated that Apostichopus japonicus arginase and agmatinase from l-arginine metabolism synergistically compete with NOS under pathogens challenge. Here we conducted a study to further investigate the mechanism in the regulation of arginase and agmatinase genes in l-arginine metabolism using EPC cell system. Luciferase analysis and progressive 5' deletion analysis suggested that Ajagmatinase promoter was a very robust promoter for its transcription, and the core region of Ajarginase promoter was located within -277 bp to -157 bp. Besides, their promoter activities were significantly activated by LPS and l-arginine challenge both in a time- and dose-dependent manners in EPC cells. When different truncated reporter vector and expression vector co-transfection experiment revealed transcription factor NF-κB/Rel and STAT5 could significantly inhibited Ajarginase promoter activity, but not Ajagmatinase. Our findings were provided novel insights into the transcriptional regulation of Ajarginase and Ajagmatinase, and selectively change their expressions might prevent pathogens infection.
Tipo de publicação: COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de substância:0 (Lipopolysaccharides); 0 (NF-kappa B); 0 (STAT5 Transcription Factor); 94ZLA3W45F (Arginine); EC 1.13.12.- (Luciferases); EC 3.5.3.- (Ureohydrolases); EC 3.5.3.1 (Arginase); EC 3.5.3.11 (agmatinase)


  7 / 315 MEDLINE  
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PMID:27404284
Autor:Meylan EM; Breuillaud L; Seredenina T; Magistretti PJ; Halfon O; Luthi-Carter R; Cardinaux JR
Endereço:Center for Psychiatric Neuroscience, Department of Psychiatry, University Medical Center, University of Lausanne, Prilly, Switzerland.
Título:Involvement of the agmatinergic system in the depressive-like phenotype of the Crtc1 knockout mouse model of depression.
Fonte:Transl Psychiatry; 6(7):e852, 2016 Jul 12.
ISSN:2158-3188
País de publicação:United States
Idioma:eng
Resumo:Recent studies implicate the arginine-decarboxylation product agmatine in mood regulation. Agmatine has antidepressant properties in rodent models of depression, and agmatinase (Agmat), the agmatine-degrading enzyme, is upregulated in the brains of mood disorder patients. We have previously shown that mice lacking CREB-regulated transcription coactivator 1 (CRTC1) associate behavioral and molecular depressive-like endophenotypes, as well as blunted responses to classical antidepressants. Here, the molecular basis of the behavioral phenotype of Crtc1(-/-) mice was further examined using microarray gene expression profiling that revealed an upregulation of Agmat in the cortex of Crtc1(-/-) mice. Quantitative polymerase chain reaction and western blot analyses confirmed Agmat upregulation in the Crtc1(-/-) prefrontal cortex (PFC) and hippocampus, which were further demonstrated by confocal immunofluorescence microscopy to comprise an increased number of Agmat-expressing cells, notably parvalbumin- and somatostatin-positive interneurons. Acute agmatine and ketamine treatments comparably improved the depressive-like behavior of male and female Crtc1(-/-) mice in the forced swim test, suggesting that exogenous agmatine has a rapid antidepressant effect through the compensation of agmatine deficit because of upregulated Agmat. Agmatine rapidly increased brain-derived neurotrophic factor (BDNF) levels only in the PFC of wild-type (WT) females, and decreased eukaryotic elongation factor 2 (eEF2) phosphorylation in the PFC of male and female WT mice, indicating that agmatine might be a fast-acting antidepressant with N-methyl-D-aspartate (NMDA) receptor antagonist properties. Collectively, these findings implicate Agmat in the depressive-like phenotype of Crtc1(-/-) mice, refine current understanding of the agmatinergic system in the brain and highlight its putative role in major depression.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Brain-Derived Neurotrophic Factor); 0 (Crtc1 protein, mouse); 0 (Eukaryotic Initiation Factor-2); 0 (Excitatory Amino Acid Antagonists); 0 (Transcription Factors); 690G0D6V8H (Ketamine); 70J407ZL5Q (Agmatine); EC 3.5.3.- (Ureohydrolases); EC 3.5.3.11 (agmatinase)


  8 / 315 MEDLINE  
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PMID:27322205
Autor:Jagmann N; Bleicher V; Busche T; Kalinowski J; Philipp B
Endereço:Institut für Molekulare Mikrobiologie und Biotechnologie, Westfälische Wilhelms-Universität (WWU) Münster, Corrensstr. 3, Münster, 48149, Germany.
Título:The guanidinobutyrase GbuA is essential for the alkylquinolone-regulated pyocyanin production during parasitic growth of Pseudomonas aeruginosa in co-culture with Aeromonas hydrophila.
Fonte:Environ Microbiol; 18(10):3550-3564, 2016 Oct.
ISSN:1462-2920
País de publicação:England
Idioma:eng
Resumo:The opportunistic pathogen Pseudomonas aeruginosa controls the production of virulence factors by quorum sensing (QS). Besides cell density, QS in P. aeruginosa is co-regulated by metabolic influences, especially nutrient limitation. Previously, a co-culture model system was established consisting of P. aeruginosa and the chitinolytic bacterium Aeromonas hydrophila, in which parasitic growth of P. aeruginosa is strictly dependent on the QS-controlled production of pyocyanin in response to nutrient limitation (Jagmann et al., ). In this study, the co-culture was employed to identify novel genes involved in the regulation of pyocyanin production. Via transposon mutagenesis, the gene gbuA encoding a guanidinobutyrase was identified, deletion of which led to a loss of pyocyanin production in co-cultures and to a reduced pyocyanin production in single cultures. Addition of the natural substrate of GbuA to the mutant strain enhanced the negative effect on pyocyanin production in single cultures. The gbuA mutant showed a reduced transcription of the pqsABCDE operon and could be complemented by PqsE overexpression and addition of alkylquinolone signal molecules. The strong effect of gbuA deletion on the QS-controlled pyocyanin production in co-cultures showed the value of this approach for the discovery of novel gene functions linking metabolism and QS in P. aeruginosa.
Tipo de publicação: JOURNAL ARTICLE
Nome de substância:0 (Bacterial Proteins); 0 (Quinolones); 9OQM399341 (Pyocyanine); EC 3.5.3.- (Ureohydrolases); EC 3.5.3.7 (guanidinobutyrase)


  9 / 315 MEDLINE  
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PMID:27220875
Autor:von Sydow L; Schwenkert S; Meurer J; Funk C; Mamedov F; Schröder WP
Endereço:Department of Chemistry, Umeå University, SE-901 87 Umeå, Sweden.
Título:The PsbY protein of Arabidopsis Photosystem II is important for the redox control of cytochrome b559.
Fonte:Biochim Biophys Acta; 1857(9):1524-33, 2016 09.
ISSN:0006-3002
País de publicação:Netherlands
Idioma:eng
Resumo:Photosystem II is a protein complex embedded in the thylakoid membrane of photosynthetic organisms and performs the light driven water oxidation into electrons and molecular oxygen that initiate the photosynthetic process. This important complex is composed of more than two dozen of intrinsic and peripheral subunits, of those half are low molecular mass proteins. PsbY is one of those low molecular mass proteins; this 4.7-4.9kDa intrinsic protein seems not to bind any cofactors. Based on structural data from cyanobacterial and red algal Photosystem II PsbY is located closely or in direct contact with cytochrome b559. Cytb559 consists of two protein subunits (PsbE and PsbF) ligating a heme-group in-between them. While the exact function of this component in Photosystem II has not yet been clarified, a crucial role for assembly and photo-protection in prokaryotic complexes has been suggested. One unique feature of Cytb559 is its redox-heterogeneity, forming high, medium and low potential, however, neither origin nor mechanism are known. To reveal the function of PsbY within Photosystem II of Arabidopsis we have analysed PsbY knock-out plants and compared them to wild type and to complemented mutant lines. We show that in the absence of PsbY protein Cytb559 is only present in its oxidized, low potential form and plants depleted of PsbY were found to be more susceptible to photoinhibition.
Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de substância:0 (Arabidopsis Proteins); 0 (Cytochrome b Group); 0 (Photosystem II Protein Complex); 9044-61-5 (cytochrome b559); EC 3.5.1.- (PSBY protein, Arabidopsis); EC 3.5.3.- (Ureohydrolases)


  10 / 315 MEDLINE  
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PMID:27032691
Autor:Yina S; Chenghua L; Weiwei Z; Zhenhui W; Zhimeng L
Endereço:School of Marine Sciences, Ningbo University, Ningbo, Zhejiang Province 315211, P. R. China.
Título:The first description of complete invertebrate arginine metabolism pathways implies dose-dependent pathogen regulation in Apostichopus japonicus.
Fonte:Sci Rep; 6:23783, 2016 Apr 01.
ISSN:2045-2322
País de publicação:England
Idioma:eng
Resumo:In this study, three typical members representative of different arginine metabolic pathways were firstly identified from Apostichopus japonicus, including nitric oxide synthase (NOS), arginase, and agmatinase. Spatial expression analysis revealed that the AjNOS transcript presented negative expression patterns relative to those of Ajarginase or Ajagmatinase in most detected tissues. Furthermore, Vibrio splendidus-challenged coelomocytes and intestine, and LPS-exposed primary coelomocytes could significantly induce AjNOS expression, followed by obviously inhibited Arginase and AjAgmatinase transcripts at the most detected time points. Silencing the three members with two specific siRNAs in vivo and in vitro collectively indicated that AjNOS not only compete with Ajarginase but also with Ajagmatinase in arginine metabolism. Interestingly, Ajarginase and Ajagmatinase displayed cooperative expression profiles in arginine utilization. More importantly, live pathogens of V. splendidus and Vibrio parahaemolyticus co-incubated with primary cells also induced NO production and suppressed arginase activity in a time-dependent at an appropriate multiplicity of infection (MOI) of 10, without non-pathogen Escherichia coli. When increasing the pathogen dose (MOI = 100), arginase activity was significantly elevated, and NO production was depressed, with a larger magnitude in V. splendidus co-incubation. The present study expands our understanding of the connection between arginine's metabolic and immune responses in non-model invertebrates.
Tipo de publicação: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de substância:0 (DNA, Complementary); 0 (RNA, Messenger); 0 (RNA, Small Interfering); 31C4KY9ESH (Nitric Oxide); 94ZLA3W45F (Arginine); EC 1.14.13.39 (Nitric Oxide Synthase); EC 3.5.3.- (Ureohydrolases); EC 3.5.3.1 (Arginase); EC 3.5.3.11 (agmatinase)



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