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Search on : Lactoperoxidase [Words]
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[PMID]: 29408362
[Au] Autor:Nauseef WM
[Ad] Address:Inflammation Program and Department of Internal Medicine, Roy J. and Lucille A. Carver College of Medicine University of Iowa, Veterans Administration Medical Center, Iowa City, IA 52240, USA; Veterans Administration Medical Center, Iowa City, IA 52240, USA; 2501 Crosspark Road D168- MTF, Coralville, IA 52241, USA. Electronic address: william-nauseef@uiowa.edu.
[Ti] Title:Biosynthesis of human myeloperoxidase.
[So] Source:Arch Biochem Biophys;642:1-9, 2018 Mar 15.
[Is] ISSN:1096-0384
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Members of Chordata peroxidase subfamily [1] expressed in mammals, including myeloperoxidase (MPO), eosinophil peroxidase (EPO), lactoperoxidase (LPO), and thyroid peroxidase (TPO), express conserved motifs around the heme prosthetic group essential for their activity, a calcium-binding site, and at least two covalent bonds linking the heme group to the protein backbone. Although most studies of the biosynthesis of these peroxidases have focused on MPO, many of the features described occur during biosynthesis of other members of the protein subfamily. Whereas MPO biosynthesis includes events typical for proteins generated in the secretory pathway, the importance and consequences of heme insertion are events uniquely associated with peroxidases. This Review summarizes decades of work elucidating specific steps in the biosynthetic pathway of human MPO. Discussion includes cotranslational glycosylation and subsequent modifications of the N-linked carbohydrate sidechains, contributions by molecular chaperones in the endoplasmic reticulum, cleavage of the propeptide from proMPO, and proteolytic processing of protomers and dimerization to yield mature MPO. Parallels between the biosynthesis of MPO and TPO as well as the impact of inherited mutations in the MPO gene on normal biosynthesis will be summarized. Lastly, specific gaps in our knowledge revealed by this review of our current understanding will be highlighted.
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Em] Entry month:1802
[Cu] Class update date: 180310
[Lr] Last revision date:180310
[St] Status:In-Data-Review

  2 / 2610 MEDLINE  
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[PMID]: 29462588
[Au] Autor:Nicolussi A; Auer M; Sevcnikar B; Paumann-Page M; Pfanzagl V; Zámocký M; Hofbauer S; Furtmüller PG; Obinger C
[Ad] Address:Department of Chemistry, Division of Biochemistry, Protein Biochemistry, VIBT - Vienna Institute of BioTechnology, University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
[Ti] Title:Posttranslational modification of heme in peroxidases - Impact on structure and catalysis.
[So] Source:Arch Biochem Biophys;643:14-23, 2018 Feb 17.
[Is] ISSN:1096-0384
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Four heme peroxidase superfamilies arose independently in evolution. Only in the peroxidase-cyclooxygenase superfamily the prosthetic group is posttranslationally modified (PTM). As a consequence these peroxidases can form one, two or three covalent bonds between heme substituents and the protein. This may include ester bonds between heme 1- and 5-methyl groups and glutamate and aspartate residues as well as a sulfonium ion link between the heme 2-vinyl substituent and a methionine. Here the phylogeny and physiological roles of representatives of this superfamily, their occurrence in all kingdoms of life, the relevant sequence motifs for definite identification and the available crystal structures are presented. We demonstrate the autocatalytic posttranslational maturation process and the impact of the covalent links on spectral and redox properties as well as on catalysis, including Compound I formation and reduction by one- and two-electron donors. Finally, we discuss the evolutionary advantage of these PTMs with respect to the proposed physiological functions of the metalloenzymes that range from antimicrobial defence in innate immunity to extracellular matrix formation and hormone biosynthesis.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[St] Status:Publisher

  3 / 2610 MEDLINE  
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[PMID]: 29516514
[Au] Autor:Herrero ER; Boon N; Bernaerts K; Slomka V; Verspecht T; Quirynen M; Teughels W
[Ad] Address:Department of Oral Health Sciences, KU Leuven, Leuven, Belgium.
[Ti] Title:Clinical concentrations of peroxidases cause dysbiosis in in vitro oral biofilms.
[So] Source:J Periodontal Res;, 2018 Mar 08.
[Is] ISSN:1600-0765
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:BACKGROUND AND OBJECTIVE: Little is known about the initiation of dysbiosis in oral biofilms, a topic of prime importance for understanding the etiology of, and preventing, periodontitis. The aim of this study was to evaluate the effect of different concentrations of crevicular and salivary peroxidase and catalase on dysbiosis in multispecies biofilms in vitro. MATERIAL AND METHODS: The spotting technique was used to identify the effect of different concentrations of myeloperoxidase, lactoperoxidase, erythrocyte catalase, and horseradish peroxidase in salivary and crevicular fluid on the inhibitory effect of commensals on pathobiont growth. Vitality-quantitative real-time PCR was performed to quantify the dysbiotic effect of the peroxidases (adjusted to concentrations found in periodontal health, gingivitis, and periodontitis) on multispecies microbial communities. RESULTS: Agar plate and multispecies ecology experiments showed that production of hydrogen peroxide (H O ) by commensal bacteria decreases pathobiont growth and colonization. Peroxidases at concentrations found in crevicular fluid and saliva neutralized this inhibitory effect. In multispecies communities, myeloperoxidase, at the crevicular fluid concentrations found in periodontitis, resulted in a 1-3 Log increase in pathobionts when compared with the crevicular fluid concentrations found in periodontal health. The effect of salivary lactoperoxidase and salivary myeloperoxidase concentrations was, in general, similar to the effect of crevicular myeloperoxidase concentrations. CONCLUSIONS: Commensal species suppress pathobionts by producing H O . Catalase and peroxidases, at clinically relevant concentrations, can neutralize this effect and thereby can contribute to dysbiosis by allowing the outgrowth of pathobionts.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[St] Status:Publisher
[do] DOI:10.1111/jre.12534

  4 / 2610 MEDLINE  
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[PMID]: 29513734
[Au] Autor:Godlewska M; Krasuska W; Czarnocka B
[Ad] Address:Department of Biochemistry and Molecular Biology, Center of Postgraduate Medical Education, Warsaw, Poland.
[Ti] Title:Biochemical properties of thyroid peroxidase (TPO) expressed in human breast and mammary-derived cell lines.
[So] Source:PLoS One;13(3):e0193624, 2018.
[Is] ISSN:1932-6203
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Thyroid peroxidase (TPO) is an enzyme and autoantigen expressed in thyroid and breast tissues. Thyroid TPO undergoes a complex maturation process however, nothing is known about post-translational modifications of breast-expressed TPO. In this study, we have investigated the biochemical properties of TPO expressed in normal and cancerous human breast tissues, and the maturation process and antigenicity of TPO present in a panel of human breast tissue-derived cell lines. We found that the molecular weight of breast TPO was slightly lower than that of thyroid TPO due to decreased glycosylation and as suggest results of Western blot also shorter amino acid chain. Breast TPO exhibit enzymatic activity and isoelectric point comparable to that of thyroid TPO. The biochemical properties of TPO expressed in mammary cell lines and normal thyrocytes are similar regarding glycan content, molecular weight and isoelectric point. However, no peroxidase activity and dimer formation was detected in any of these cell lines since the majority of TPO protein was localized in the cytoplasmic compartment, and the TPO expression at the cell surface was too low to detect its enzymatic activity. Lactoperoxidase, a protein highly homologous to TPO expressed also in breast tissues, does not influence the obtained data. TPO expressed in the cell lines was recognized by a broad panel of TPO-specific antibodies. Although some differences in biochemical properties between thyroid and breast TPO were observed, they do not seem to be critical for the overall three-dimensional structure. This conclusion is supported by the fact that TPO expressed in breast tissues and cell lines reacts well with conformation-sensitive antibodies. Taking into account a close resemblance between both proteins, especially high antigenicity, future studies should investigate the potential immunotherapies directed against breast-expressed TPO and its specific epitopes.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1803
[Cu] Class update date: 180307
[Lr] Last revision date:180307
[St] Status:In-Data-Review
[do] DOI:10.1371/journal.pone.0193624

  5 / 2610 MEDLINE  
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[PMID]: 29272487
[Au] Autor:Rigoni A; Poulsom R; Jeffery R; Mehta S; Lewis A; Yau C; Giannoulatou E; Feakins R; Lindsay JO; Colombo MP; Silver A
[Ad] Address:Molecular Immunology Unit, Department of Research, Fondazione IRCCS Istituto Nazionale dei Tumori, Milan, Italy.
[Ti] Title:Separation of Dual Oxidase 2 and Lactoperoxidase Expression in Intestinal Crypts and Species Differences May Limit Hydrogen Peroxide Scavenging During Mucosal Healing in Mice and Humans.
[So] Source:Inflamm Bowel Dis;24(1):136-148, 2017 Dec 19.
[Is] ISSN:1536-4844
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Background: DUOX2 and DUOXA2 form the predominant H2O2-producing system in human colorectal mucosa. Inflammation, hypoxia, and 5-aminosalicylic acid increase H2O2 production, supporting innate defense and mucosal healing. Thiocyanate reacts with H2O2 in the presence of lactoperoxidase (LPO) to form hypothiocyanate (OSCN-), which acts as a biocide and H2O2 scavenging system to reduce damage during inflammation. We aimed to discover the organization of Duox2, Duoxa2, and Lpo expression in colonic crypts of Lieberkühn (intestinal glands) of mice and how distributions respond to dextran sodium sulfate (DSS)-induced colitis and subsequent mucosal regeneration. Methods: We studied tissue from DSS-exposed mice and human biopsies using in situ hybridization, reverse transcription quantitative polymerase chain reaction, and cDNA microarray analysis. Results: Duox2 mRNA expression was mostly in the upper crypt quintile while Duoxa2 was more apically focused. Most Lpo mRNA was in the basal quintile, where stem cells reside. Duox2 and Duoxa2 mRNA were increased during the induction and resolution of DSS colitis, while Lpo expression did not increase during the acute phase. Patterns of Lpo expression differed from Duox2 in normal, inflamed, and regenerative mouse crypts (P < 0.001). We found no evidence of LPO expression in the human gut. Conclusions: The spatial and temporal separation of H2O2-consuming and -producing enzymes enables a thiocyanate- H2O2 "scavenging" system in murine intestinal crypts to protect the stem/proliferative zones from DNA damage, while still supporting higher H2O2 concentrations apically to aid mucosal healing. The absence of LPO expression in the human gut suggests an alternative mechanism or less protection from DNA damage during H2O2-driven mucosal healing.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1712
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[St] Status:In-Data-Review
[do] DOI:10.1093/ibd/izx024

  6 / 2610 MEDLINE  
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[PMID]: 29266741
[Au] Autor:Bafort F; Damblon C; Smargiasso N; De Pauw E; Perraudin JP; Jijakli MH
[Ad] Address:Integrated and Urban Plant Pathology Laboratory, Gembloux Agro-Bio Tech, Liège University, Passage des Déportés 2, 5030, Gembloux, Belgium.
[Ti] Title:Reaction Product Variability and Biological Activity of the Lactoperoxidase System Depending on Medium Ionic Strength and pH, and on Substrate Relative Concentration.
[So] Source:Chem Biodivers;, 2017 Dec 20.
[Is] ISSN:1612-1880
[Cp] Country of publication:Switzerland
[La] Language:eng
[Ab] Abstract:The potential of ions produced in water by the lactoperoxidase system against plant pests has shown promising results. We tested the bioactivity of ions produced by the lactoperoxidase oxidation of I and SCN in several buffers or in tap water and characterized the ions produced. In vitro biological activity was tested against Penicillium expansum, the causal agent of mold in fruits, and the major cause of patulin contamination of fruit juices and compotes. In buffers, the ionic concentration was increased 3-fold, and pathogen inhibition was obtained down to the 1:15 dilution. In tap water, the ionic concentration was weaker, and pathogen inhibition was obtained only down to the 1:3 dilution. Acidic buffer increased ion concentrations as compared to less acidic (pH 5.6 or 6.2) or neutral buffers, as do increased ionic strength. C-labelled SCN and MS showed that different ions were produced in water and in buffers. In specific conditions the ion solution turned yellow and a product was formed, probably diiodothiocyanate (I SCN ), giving an intense signal at 49.7 ppm in C-NMR. The formation of the signal was unambiguously favored in acidic media and disadvantaged or inhibited in neutral or basic conditions. It was enhanced at a specific SCN : I ratio of 1:4.5, but decreased when the ratio was 1:2, and was inhibited at ratio SCN >I . We demonstrated that the formation of the signal required the interaction between I and SCN , and MS showed the presence of I SCN .
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1712
[Cu] Class update date: 180308
[Lr] Last revision date:180308
[St] Status:Publisher
[do] DOI:10.1002/cbdv.201700497

  7 / 2610 MEDLINE  
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[PMID]: 29355443
[Au] Autor:Priyanka BS; Rastogi NK
[Ad] Address:a Department of Food Engineering, Academy of Scientific and Innovative Research , CSIR-Central Food Technological Research Institute , Mysore , India.
[Ti] Title:Downstream processing of lactoperoxidase from milk whey by involving liquid emulsion membrane.
[So] Source:Prep Biochem Biotechnol;:1-9, 2018 Jan 22.
[Is] ISSN:1532-2297
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:The current work deals with downstream processing of lactoperoxidase using liquid emulsion membrane from the bovine milk whey, which is a by-product from dairy industry. It is an alternate separation technique that can be used for the selective extraction of lactoperoxidase. The extraction of lactoperoxidase in liquid emulsion membrane takes place due to the electrostatic interaction between the enzyme and polar head group of reverse micellar surfactant. The optimum conditions resulted in 2.86 factor purity and activity recovery of 75.21%. Downstream processing involving liquid emulsion membrane is a potential technique for the extraction of lactoperoxidase from bovine whey.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180305
[Lr] Last revision date:180305
[St] Status:Publisher
[do] DOI:10.1080/10826068.2018.1425713

  8 / 2610 MEDLINE  
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[PMID]: 29174286
[Au] Autor:Singh PK; Iqbal N; Sirohi HV; Bairagya HR; Kaur P; Sharma S; Singh TP
[Ad] Address:Department of Biophysics, All India Institute of Medical Sciences, New Delhi, India.
[Ti] Title:Structural basis of activation of mammalian heme peroxidases.
[So] Source:Prog Biophys Mol Biol;133:49-55, 2018 Mar.
[Is] ISSN:1873-1732
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:The mammalian heme peroxidases including lactoperoxidase (LPO), myeloperoxidase (MPO), eosinophil peroxidase (EPO) and thyroid peroxidase (TPO) contain a covalently linked heme moiety. Initially, it was believed that the heme group was fully cross-linked to protein molecule through at least two ester linkages involving conserved glutamate and aspartate residues with 1-methyl and 5-methyl groups of pyrrole rings A and C respectively. In MPO, an additional sulfonium ion linkage was present between 2-vinyl group of pyrrole ring A of the heme moiety and a methionine residue of the protein. These linkages were formed through a self processing mechanism. Subsequently, biochemical studies indicated that the heme moiety was partially attached to protein. The recent structural studies have shown that the covalent linkage involving glutamate and 1-methyl group of pyrrole ring of heme moiety was partially formed. When glutamate is not covalently linked to heme moiety, its side chain occupies a position in the substrate binding site on the distal heme side and blocks the substrate binding site leading to inactivation. However, an exposure to H O converts it to a fully covalently linked state with heme. Thus in mammalian heme peroxidases, the Glu-heme linkage is essential for catalytic action.
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Em] Entry month:1711
[Cu] Class update date: 180304
[Lr] Last revision date:180304
[St] Status:In-Data-Review

  9 / 2610 MEDLINE  
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[PMID]: 29475188
[Au] Autor:Kim J; Chang JY; Kim YY; Kim MJ; Kho HS
[Ad] Address:Dept. of Oral Medicine and Oral Diagnosis, School of Dentistry and Dental Research Institute, Seoul National University, 101 Daehak-ro, Jongno-gu, Seoul 03080, Republic of Korea.
[Ti] Title:Effects of molecular weight of hyaluronic acid on its viscosity and enzymatic activities of lysozyme and peroxidase.
[So] Source:Arch Oral Biol;89:55-64, 2018 Feb 14.
[Is] ISSN:1879-1506
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:OBJECTIVES: To investigate the effects of the molecular weight of hyaluronic acid on its viscosity and enzymatic activities of lysozyme and peroxidase in solution and on the hydroxyapatite surface. DESIGN: Hyaluronic acids of four different molecular weights (10 kDa, 100 kDa, 1 MDa, and 2 MDa), hen egg-white lysozyme, bovine lactoperoxidase, and human whole saliva were used. Viscosity values of hyaluronic acids were measured using a cone-and-plate viscometer at six different concentrations (0.1-5.0 mg/mL). Enzymatic activities of lysozyme and peroxidase were examined by hydrolysis of fluorescein-labeled Micrococcus lysodeikticus and oxidation of fluorogenic 2',7'-dichlorofluorescein to fluorescing 2',7'-dichlorofluorescein, respectively. RESULTS: In solution assays, only 2 MDa-hyaluronic acid significantly inhibited lysozyme activities in saliva. In surface assays, hyaluronic acids inhibited lysozyme and peroxidase activities; the inhibitory activities were more apparent with high-molecular-weight ones in saliva than in purified enzymes. The 100 kDa-hyaluronic acid at 5.0 mg/mL, 1 MDa-one at 0.5 mg/mL, and 2 MDa-one at 0.2 mg/mL showed viscosity values similar to those of human whole saliva at a shear rate range required for normal oral functions. The differences among the influences of the three conditions on the enzymatic activities were not statistically significant. CONCLUSIONS: High-molecular-weight hyaluronic acids at low concentration and low-molecular-weight ones at high concentration showed viscosity values similar to those of human whole saliva. Inhibitory effects of hyaluronic acids on lysozyme and peroxidase activities were more significant with high-molecular-weight ones on the surface and in saliva compared with in solution and on purified enzymes.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1802
[Cu] Class update date: 180223
[Lr] Last revision date:180223
[St] Status:Publisher

  10 / 2610 MEDLINE  
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[PMID]: 29377356
[Au] Autor:Shoemake BM; Vander Ley BL; Newcomer BW; Heller MC
[Ad] Address:College of Veterinary Medicine, University of Missouri, Columbia, MO.
[Ti] Title:Efficacy of Oral Administration of Sodium Iodide to Prevent Bovine Respiratory Disease Complex.
[So] Source:J Vet Intern Med;32(1):516-524, 2018 Jan.
[Is] ISSN:1939-1676
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:BACKGROUND: The prevention of bovine respiratory disease complex (BRD) in beef cattle is important to maintaining health and productivity of calves in feeding operations. OBJECTIVE: Determine whether BRD bacterial and viral pathogens are susceptible to the lactoperoxidase/hydrogen peroxide/iodide (LPO/H O /I ) system in vitro and to determine whether the oral administration of sodium iodide (NaI) could achieve sufficient concentrations of iodine (I) in the respiratory secretions of weaned beef calves to inactivate these pathogens in vivo. ANIMALS: Sixteen weaned, apparently healthy, commercial beef calves from the University of Missouri, College of Veterinary Medicine teaching herd. METHODS: In vitro viral and bacterial assays were performed to determine susceptibility to the LPO/H O /I system at varying concentrations of NaI. Sixteen randomly selected, healthy crossbred beef weanlings were administered 70 mg/kg NaI, or water, orally in a blinded, placebo-controlled trial. Blood and nasal secretions were collected for 72 hours and analyzed for I concentration. RESULTS: Bovine herpesvirus-1, parainfluenza-3, Mannheimia haemolytica and Bibersteinia trehalosi were all inactivated or inhibited in vitro by the LPO/H O /I reaction. Oral administration of NaI caused a marked increase in nasal fluid I concentration with a C  = 181 (1,420 µM I), T , a sufficient concentration to inactivate these pathogens in vitro. CONCLUSIONS AND CLINICAL IMPORTANCE: In vitro, the LPO/H O /I system inactivates and inhibits common pathogens associated with BRD. The administration of oral NaI significantly increases the I concentration of nasal fluid indicating that this system might be useful in preventing bovine respiratory infections.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1801
[Cu] Class update date: 180209
[Lr] Last revision date:180209
[St] Status:In-Process
[do] DOI:10.1111/jvim.14903


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