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[PMID]: 29432848
[Au] Autor:Yamamoto T; Ugai H; Nakayama-Imaohji H; Tada A; Elahi M; Houchi H; Kuwahara T
[Ad] Address:Department of Pharmacy, Kagawa University Hospital, 1750-1 Miki, Kagawa, 761-0793, Japan.
[Ti] Title:Characterization of a recombinant Bacteroides fragilis sialidase expressed in Escherichia coli.
[So] Source:Anaerobe;50:69-75, 2018 Feb 09.
[Is] ISSN:1095-8274
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:The human gut commensal Bacteroides fragilis produces sialidases that remove a terminal sialic acid from host-derived polysaccharides. Sialidase is considered to be involved in B.fragilis infection pathology. A native B.fragilis sialidase has been purified and characterized, and was shown to be post-translationally modified by glycosylation. However, the biochemical properties of recombinant B.fragilis sialidase expressed in a heterologous host remain uncharacterized. In this study, we examined the enzymatic properties of the 60-kDa sialidase NanH1 of B. fragilis YCH46, which was prepared as a recombinant protein (rNanH1) in Escherichia coli. In E.coli rNanH1 was expressed as inclusion bodies, which were separated from soluble proteins to allow solubilization of insoluble rNanH1 in a buffer containing 8 M urea and renaturation in refolding buffer containing 100 mM CaCl and 50 mM L-arginine. The specific activity of renatured rNanH1 measured using 4-methylumberiferyl-α-D-N-acetyl neuraminic acid as a substrate was 6.16 mol/min/mg. The optimal pH of rNanH1 ranged from 5.0 to 5.5. The specific activity of rNanH1 was enhanced in the presence of calcium ions. rNanH1 preferentially hydrolyzed the sialyl α2,8 linkage and cleaved sialic acids from mucin and serum proteins (e.g., fetuin and transferrin) but not from α1-acid glycoprotein, which is similar to the previously observed biochemical properties for a native sialidase purified from B.fragilis SBT3182. The results and methods described in this study will be useful for preparing and characterizing recombinant proteins for other B.fragilis sialidase isoenzymes.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:Publisher

  2 / 84600 MEDLINE  
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[PMID]: 29451229
[Au] Autor:Patron M; Sprenger HG; Langer T
[Ad] Address:Max Planck Institute for Biology of Aging, Cologne, Germany.
[Ti] Title:m-AAA proteases, mitochondrial calcium homeostasis and neurodegeneration.
[So] Source:Cell Res;28(3):296-306, 2018 Mar.
[Is] ISSN:1748-7838
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:The function of mitochondria depends on ubiquitously expressed and evolutionary conserved m-AAA proteases in the inner membrane. These ATP-dependent peptidases form hexameric complexes built up of homologous subunits. AFG3L2 subunits assemble either into homo-oligomeric isoenzymes or with SPG7 (paraplegin) subunits into hetero-oligomeric proteolytic complexes. Mutations in AFG3L2 are associated with dominant spinocerebellar ataxia (SCA28) characterized by the loss of Purkinje cells, whereas mutations in SPG7 cause a recessive form of hereditary spastic paraplegia (HSP7) with motor neurons of the cortico-spinal tract being predominantly affected. Pleiotropic functions have been assigned to m-AAA proteases, which act as quality control and regulatory enzymes in mitochondria. Loss of m-AAA proteases affects mitochondrial protein synthesis and respiration and leads to mitochondrial fragmentation and deficiencies in the axonal transport of mitochondria. Moreover m-AAA proteases regulate the assembly of the mitochondrial calcium uniporter (MCU) complex. Impaired degradation of the MCU subunit EMRE in AFG3L2-deficient mitochondria results in the formation of deregulated MCU complexes, increased mitochondrial calcium uptake and increased vulnerability of neurons for calcium-induced cell death. A reduction of calcium influx into the cytosol of Purkinje cells rescues ataxia in an AFG3L2-deficient mouse model. In this review, we discuss the relationship between the m-AAA protease and mitochondrial calcium homeostasis and its relevance for neurodegeneration and describe a novel mouse model lacking MCU specifically in Purkinje cells. Our results pledge for a novel view on m-AAA proteases that integrates their pleiotropic functions in mitochondria to explain the pathogenesis of associated neurodegenerative disorders.
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Em] Entry month:1802
[Cu] Class update date: 180309
[Lr] Last revision date:180309
[St] Status:In-Data-Review
[do] DOI:10.1038/cr.2018.17

  3 / 84600 MEDLINE  
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[PMID]: 29513471
[Au] Autor:Maksimov IV; Usupova ZR; Cherepanova EA; Khairulin RM; Vakhitov VA
[Ti] Title:[Inhibition of IAA oxidase activity of wheat anionic peroxidase by chitooligosaccharides].
[So] Source:Prikl Biokhim Mikrobiol;52(5):538-44, 2016 Sep-Oct.
[Is] ISSN:0555-1099
[Cp] Country of publication:Russia (Federation)
[La] Language:rus
[Ab] Abstract:The study demonstrated that chitooligosaccharides with a molecular weight of 510 kDa and a degree of acetylation of 65% exhibited an auxin-like effect in wheat plants and also played an important role in regulating the activity of polysaccharide (chitin)specific anion isoenzymes of peroxidase oxidizing indole acetic acid. Changes in the kinetic parameters of the interaction of the wheat anionic chitin-specific peroxidase with pI ∼3.5 with chitin oligomers in the presence of indoleacetic acid were pH-depended and indicated that chitooligosaccharides significantly impair the ability of the enzyme for oxidation at pH levels of 4.2 and 6.0. It can be assumed that chitooligosaccharides not only induce protective plant systems but also increase the accumulation of auxin in plant tissues, thus adversely affecting a number of components of the plant protective system against pathogens.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180307
[Lr] Last revision date:180307
[St] Status:In-Process

  4 / 84600 MEDLINE  
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[PMID]: 29448869
[Au] Autor:Huguet J; Gaudette F; Michaud V; Turgeon J
[Ad] Address:a CRCHUM, University of Montreal , Montreal , Canada.
[Ti] Title:Development and validation of probe drug cocktails for the characterization of CYP450-mediated metabolism by human heart microsomes.
[So] Source:Xenobiotica;:1-13, 2018 Mar 08.
[Is] ISSN:1366-5928
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:1. The objective of our study was to develop and validate a cocktail approach to allow the simultaneous characterization of various CYP450-mediated oxidations by human heart microsomes for nine probe drug substrates, namely, 7-ethoxyresorufin, bupropion, repaglinide, tolbutamide, bufuralol, chlorzoxazone, ebastine, midazolam and dodecanoic acid. 2. The first validation step was conducted using recombinant human CYP450 isoenzymes by comparing activity measured for each probe drug as a function of (1) buffer used, (2) selectivity towards specific isoenzymes and (3) drug interactions between probes. Activity was all measured by validated LC-MSMS methods. 3. Two cocktails were then constituted with seven of the nine drugs and subjected to kinetic validation. Finally, all probe drugs were incubated with human heart microsomes prepared from ventricular tissues obtained from 12 patients undergoing cardiac transplantation. 4. Validated cocktail #1 including bupropion, chlorzoxazone, ebastine and midazolam was used to characterize CYP2B6-, 2E1-, 2J2- and 3A5-mediated metabolism in human hearts. 5. Cocktail #2 which includes bufuralol, 7-ethoxyresorufin and repaglinide failed the validation step. Substrates in cocktail #2 as well as tolbutamide and dodecanoic acid had to be incubated separately because of their physico-chemical characteristics (solubility and ionization) or drug interactions. 6. Activity in HHM was the highest towards ebastine, chlorzoxazone and tolbutamide.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[St] Status:Publisher
[do] DOI:10.1080/00498254.2018.1438684

  5 / 84600 MEDLINE  
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[PMID]: 29425031
[Au] Autor:Guo T; Dtwyler P; Demina E; Richards MR; Ge P; Zou C; Zheng R; Fougerat A; Pshezhetsky AV; Ernst B; Cairo CW
[Ad] Address:Alberta Glycomics Centre and Department of Chemistry , University of Alberta , Edmonton Alberta T6G 2G2 , Canada.
[Ti] Title:Selective Inhibitors of Human Neuraminidase 3.
[So] Source:J Med Chem;61(5):1990-2008, 2018 Mar 08.
[Is] ISSN:1520-4804
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Human neuraminidases (NEU) are associated with human diseases including cancer, atherosclerosis, and diabetes. To obtain small molecule inhibitors as research tools for the study of their biological functions, we designed a library of 2-deoxy-2,3-didehydro- N-acetylneuraminic acid (DANA) analogues with modifications at C4 and C9 positions. This library allowed us to discover selective inhibitors targeting the human NEU3 isoenzyme. Our most selective inhibitor for NEU3 has a K of 320 40 nM and a 15-fold selectivity over other human neuraminidase isoenzymes. This inhibitor blocks glycolipid processing by NEU3 in vitro. To improve their pharmacokinetic properties, various esters of the best inhibitors were synthesized and evaluated. Finally, we confirmed that our best compounds exhibited selective inhibition of NEU orthologues from murine brain.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[St] Status:In-Data-Review
[do] DOI:10.1021/acs.jmedchem.7b01574

  6 / 84600 MEDLINE  
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[PMID]: 29422671
[Au] Autor:Li C; Zhang B; Chen B; Ji L; Yu H
[Ad] Address:Department of Biological Sciences, Faculty of Science, National University of Singapore, Singapore, 117543, Singapore.
[Ti] Title:Site-specific phosphorylation of TRANSPARENT TESTA GLABRA1 mediates carbon partitioning in Arabidopsis seeds.
[So] Source:Nat Commun;9(1):571, 2018 02 08.
[Is] ISSN:2041-1723
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Seed development is dependent on nutrients, such as a source of carbon, supplied by the parent plant. It remains largely unknown how these nutrients are distributed to zygotic and maternal tissues to coordinate storage of reserve compounds and development of protective tissues like seed coat. Here we show that phosphorylation of TRANSPARENT TESTA GLABRA1 (TTG1) is regulated by SHAGGY-like kinases 11/12 (SK11/12) and that this mediates carbon flow to fatty acid synthesis and seed coat traits in Arabidopsis seeds. SK11/12 phosphorylate TTG1 at serine 215, thus preventing TTG1 interaction with TRANSPARENT TESTA2. This compromises recruitment of TTG1 to the GLABRA2 locus and downregulates GLABRA2 expression, which enhances biosynthesis of fatty acids in the embryo, but reduces production of mucilage and flavonoid pigments in the seed coat. Therefore, site-specific phosphorylation of TTG1 by SK11/SK12 regulates carbon partitioning between zygotic and maternal sinks in seeds.
[Mh] MeSH terms primary: Arabidopsis Proteins/genetics
Arabidopsis/genetics
Carbon/metabolism
Gene Expression Regulation, Plant
Seeds/genetics
[Mh] MeSH terms secundary: Arabidopsis/growth & development
Arabidopsis/metabolism
Arabidopsis Proteins/metabolism
Fatty Acids/biosynthesis
Flavonoids/biosynthesis
Gene Expression Regulation, Developmental
Glycogen Synthase Kinase 3/genetics
Glycogen Synthase Kinase 3/metabolism
Isoenzymes/genetics
Isoenzymes/metabolism
Mutation
Phenotype
Phosphorylation
Plant Mucilage/biosynthesis
Seeds/growth & development
Seeds/metabolism
Transcription Factors/genetics
Transcription Factors/metabolism
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Arabidopsis Proteins); 0 (Fatty Acids); 0 (Flavonoids); 0 (Isoenzymes); 0 (Plant Mucilage); 0 (TTG1 protein, Arabidopsis); 0 (TTG2 protein, Arabidopsis); 0 (Transcription Factors); 7440-44-0 (Carbon); EC 2.7.11.26 (ATSK11 protein, Arabidopsis); EC 2.7.11.26 (Glycogen Synthase Kinase 3)
[Em] Entry month:1803
[Cu] Class update date: 180307
[Lr] Last revision date:180307
[Js] Journal subset:IM
[Da] Date of entry for processing:180210
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-018-03013-5

  7 / 84600 MEDLINE  
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[PMID]: 29422501
[Au] Autor:Collopy LC; Ware TL; Goncalves T; Kongsstovu S; Yang Q; Amelina H; Pinder C; Alenazi A; Moiseeva V; Pearson SR; Armstrong CA; Tomita K
[Ad] Address:Chromosome Maintenance Group, UCL Cancer Institute, University College London, London, WC1E 6DD, UK.
[Ti] Title:LARP7 family proteins have conserved function in telomerase assembly.
[So] Source:Nat Commun;9(1):557, 2018 02 08.
[Is] ISSN:2041-1723
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Understanding the intricacies of telomerase regulation is crucial due to the potential health benefits of modifying its activity. Telomerase is composed of an RNA component and reverse transcriptase. However, additional factors required during biogenesis vary between species. Here we have identified fission yeast Lar7 as a member of the conserved LARP7 family, which includes the Tetrahymena telomerase-binding protein p65 and human LARP7. We show that Lar7 has conserved RNA-recognition motifs, which bind telomerase RNA to protect it from exosomal degradation. In addition, Lar7 is required to stabilise the association of telomerase RNA with the protective complex LSm2-8, and telomerase reverse transcriptase. Lar7 remains a component of the mature telomerase complex and is required for telomerase localisation to the telomere. Collectively, we demonstrate that Lar7 is a crucial player in fission yeast telomerase biogenesis, similarly to p65 in Tetrahymena, and highlight the LARP7 family as a conserved factor in telomere maintenance.
[Mh] MeSH terms primary: Nuclear Proteins/genetics
Phosphoproteins/genetics
Protozoan Proteins/genetics
RNA, Fungal/genetics
RNA-Directed DNA Polymerase/genetics
RNA/genetics
Ribonucleoproteins/genetics
Schizosaccharomyces/genetics
Telomerase/genetics
[Mh] MeSH terms secundary: Amino Acid Motifs
Conserved Sequence
Gene Expression
Humans
Isoenzymes/genetics
Isoenzymes/metabolism
Nuclear Proteins/metabolism
Phosphoproteins/metabolism
Protein Binding
Protozoan Proteins/metabolism
RNA/metabolism
RNA Stability
RNA, Fungal/metabolism
RNA-Directed DNA Polymerase/metabolism
Ribonucleoproteins/metabolism
Schizosaccharomyces/metabolism
Telomerase/metabolism
Telomere/chemistry
Telomere/ultrastructure
Tetrahymena thermophila/genetics
Tetrahymena thermophila/metabolism
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Name of substance:0 (Isoenzymes); 0 (Larp7 protein, human); 0 (Nuclear Proteins); 0 (Pdd1 protein, Tetrahymena); 0 (Phosphoproteins); 0 (Protozoan Proteins); 0 (RNA, Fungal); 0 (Ribonucleoproteins); 0 (Ter1 telomerase subunit, S pombe); 63231-63-0 (RNA); EC 2.7.7.49 (RNA-Directed DNA Polymerase); EC 2.7.7.49 (Telomerase)
[Em] Entry month:1803
[Cu] Class update date: 180307
[Lr] Last revision date:180307
[Js] Journal subset:IM
[Da] Date of entry for processing:180210
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02296-4

  8 / 84600 MEDLINE  
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[PMID]: 29509881
[Au] Autor:Whittington HJ; Ostrowski PJ; McAndrew DJ; Cao F; Shaw A; Eykyn TR; Lake H; Tyler J; Schneider JE; Neubauer S; Zervou S; Lygate CA
[Ad] Address:Division of Cardiovascular Medicine, Radcliffe Department of Medicine, and the BHF Centre of Research Excellence, University of Oxford, Oxford, UK.
[Ti] Title:Over-expression of mitochondrial creatine kinase in the murine heart improves functional recovery and protects against injury following ischaemia-reperfusion.
[So] Source:Cardiovasc Res;, 2018 Mar 02.
[Is] ISSN:1755-3245
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Aims: Mitochondrial creatine kinase (MtCK) couples ATP production via oxidative phosphorylation to phosphocreatine in the cytosol, which acts as a mobile energy store available for regeneration of ATP at times of high demand. We hypothesised that elevating MtCK would be beneficial in ischaemia-reperfusion (I/R) injury. Methods and Results: Mice were created overexpressing the sarcomeric MtCK gene with αMHC promoter at the Rosa26 locus (MtCK-OE) and compared with wild-type (WT) littermates. MtCK activity was 27% higher than WT, with no change in other CK isoenzymes or creatine levels. Electron microscopy confirmed normal mitochondrial cell density and mitochondrial localisation of transgenic protein. Respiration in isolated mitochondria was unaltered and metabolomic analysis by 1H-NMR suggests that cellular metabolism was not grossly affected by transgene expression. There were no significant differences in cardiac structure or function under baseline conditions by cine-MRI or LV haemodynamics. In Langendorff-perfused hearts subjected to 20min ischaemia and 30 min reperfusion, MtCK-OE exhibited less ischaemic contracture and improved functional recovery (Rate pressure product 58% above WT; P < 0.001). These hearts had reduced myocardial infarct size, which was confirmed in vivo: 554% in WT vs 294% in MtCK-OE; P < 0.0001). Isolated cardiomyocytes from MtCK-OE hearts exhibited delayed opening of the mitochondrial permeability transition pore (mPTP) compared to WT, which was confirmed by reduced mitochondrial swelling in response to calcium. There was no detectable change in the structural integrity of the mitochondrial membrane. Conclusions: Modest elevation of MtCK activity in the heart does not adversely affect cellular metabolism, mitochondrial or in vivo cardiac function, but modifies mPTP opening to protect against I/R injury and improve functional recovery. Our findings support MtCK as a prime therapeutic target in myocardial ischaemia.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180306
[Lr] Last revision date:180306
[St] Status:Publisher
[do] DOI:10.1093/cvr/cvy054

  9 / 84600 MEDLINE  
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[PMID]: 29507144
[Au] Autor:Ingrid K; Nathalie S; Elodie S; Kati M; Cline M; Sandrine B; Jean-Franois GE
[Ad] Address:FLUID Team, Lyon Neurosciences Research Center, INSERM U1028 CRNS UMR 5292, Universit Claude Bernard Lyon-1, Lyon, 69008 France.
[Ti] Title:Glutathione conjugation at the blood-CSF barrier efficiently prevents exposure of the developing brain fluid environment to blood-borne reactive electrophilic substances.
[So] Source:J Neurosci;, 2018 Mar 05.
[Is] ISSN:1529-2401
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Exposure of the developing brain to toxins, drugs, or deleterious endogenous compounds during the perinatal period can trigger alterations in cell division, migration, differentiation, and synaptogenesis, leading to life-long neurological impairment. The brain is protected by cellular barriers acting through multiple mechanisms, some of which are still poorly explored. We used a combination of enzymatic assays, live tissue fluorescence microscopy, and an in vitro cellular model of the blood-CSF barrier to investigate an enzymatic detoxification pathway in the developing male and female rat brain. We show that during the early postnatal period the choroid plexus epithelium forming the blood-CSF barrier and the ependymal cell layer bordering the ventricles harbor a high detoxifying capacity that involves glutathione- -transferases. Using a functional knockdown rat model for choroidal glutathione conjugation, we demonstrate that already in neonates, this metabolic pathway efficiently prevents the penetration of blood-borne reactive compounds into CSF. The versatility of the protective mechanism results from the multiplicity of the glutathione- -transferase isoenzymes, which are differently expressed between the choroidal epithelium and the ependyma. The various isoenzymes display differential substrate specificities, which greatly widens the spectrum of molecules that can be inactivated by this pathway. In conclusion, the blood-CSF barrier and the ependyma are identified as key cellular structures in the CNS to protect the brain fluid environment from different chemical classes of potentially toxic compounds during the postnatal period. This metabolic neuroprotective function of brain interfaces ought to compensate for the liver postnatal immaturity. Brain homeostasis requires a stable and controlled internal environment. Defective brain protection during the perinatal period can lead to life-long neurological impairment. We demonstrate that the choroid plexus forming the blood-CSF barrier is a key player in the protection of the developing brain. Glutathione-dependent enzymatic metabolism in the choroidal epithelium inactivates a broad spectrum of noxious compounds, efficiently preventing their penetration into the CSF. A second line of detoxification is located in the ependyma separating the CSF from brain tissue. Our study reveals a novel facet of the mechanisms by which the brain is protected at a period of high vulnerability, at a time when the astrocytic network is still immature and liver xenobiotic metabolism is limited.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180307
[Lr] Last revision date:180307
[St] Status:Publisher

  10 / 84600 MEDLINE  
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[PMID]: 29505970
[Au] Autor:Takcs Z; Por P; Borbly P; Czkus Z; Szalai G; Tari I
[Ad] Address:Department of Plant Biology, University of Szeged, H-6726 Szeged, Kzp fasor 52., Hungary. Electronic address: takacszoltan8923@gmail.com.
[Ti] Title:H O homeostasis in wild-type and ethylene-insensitive Never ripe tomato in response to salicylic acid treatment in normal photoperiod and in prolonged darkness.
[So] Source:Plant Physiol Biochem;126:74-85, 2018 Mar 02.
[Is] ISSN:1873-2690
[Cp] Country of publication:France
[La] Language:eng
[Ab] Abstract:Ethylene proved to be an important modulator of salicylic acid (SA) signalling pathway. Since SA may regulate both the production and scavenging of hydrogen peroxide (H O ), which show light-dependency, the aim of this study was to compare H O metabolism in the leaves of SA-treated wild-type (WT) tomato (Solanum lycopersicum L. cv. Ailsa Craig) and in ethylene receptor Never-ripe (Nr) mutants grown in normal photoperiod or in prolonged darkness. H O accumulation was higher in the WT than in the mutants in normal photoperiod after 1 mM SA treatment, while Nr leaves contained more H O after light deprivation. The expression of certain superoxide dismutase (SOD) genes and activity of the enzyme followed the same tendency as H O , which was scavenged by different enzymes in the two genotypes. Catalase (CAT, EC 1.11.1.6) activity was inhibited by SA in WT, while the mutants maintained enhanced enzyme activity in the dark. Thus, in WT, CAT inhibition was the major component of the H O accumulation elicited by 1 mM SA in a normal photoperiod, since the expression and/or activity of ascorbate (APX, EC 1.11.1.11) and guaiacol peroxidases (POD, EC 1.11.1.7) were induced in the leaves. The absence of APX and POD activation in mutant plants suggests that the regulation of these enzymes by SA needs functional ethylene signalling. While the block of ethylene perception in Nr mutants was overwritten in the transcription and activity of certain SOD and CAT isoenzymes during prolonged darkness, the low APX and POD activities led to H O accumulation in these tissues.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180305
[Lr] Last revision date:180305
[St] Status:Publisher


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