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{{Infobox Protein
|Name = Lactoperoxidase
|Bild = Lactoperoxidase 2R5L.png
|Bild_legende = Bändermodell der Lactoperoxidase der [[Hausziege]] (''Capra hircus''). Das Protein ist in Regenbogenfarben dargestellt ([[N-Terminus]] = blau, [[C-Terminus]] = rot) während das [[Häme (Stoffgruppe)|Häm]] mit Kugeln dargestellt ist (Kohlenstoff-Atome = weiß, Sauerstoff-Atome = rot, Stickstoff-Atome = blau, Eisenatom = orange).<ref name="pmid18191143">{{PDB|2r5l}}; {{cite journal | author = A.K. Singh, N. Sharma, S. Kaur, P. Srinivasan, A. Singh, T.P. Singh | title = Crystal structure of lactoperoxidase at 2.4 Å resolution | journal = J. Mol. Biol. | volume = 376 | issue = 1 | pages = 1060–1075 | year = 2007 | month = September | pmid = 18191143 | doi = 10.2210/pdb2r5l/pdb | url = | issn = |language=en }}</ref>
|PDB = 
|Groesse = 612 aa
|Kofaktor = Ca2+, Häm ''b''
|Precursor = (712 aa)
|Struktur =
|Isoformen =
|HGNCid = 6678
|Symbol = LPO
|AltSymbols =
|OMIM = 150205
|UniProt = P22079
|MGIid = 1923363
|CAS =
|CASergänzend =
|ATC-Code = 
|DrugBank =
|Wirkstoffklasse =
|TCDB =
|TranspText =
|EC-Nummer = 1.11.1.7
|Kategorie = Oxidoreduktase
|Peptidase_fam =
|Inhibitor_fam =
|Reaktionsart = Redoxreaktion
|Substrat = Iodid, Bromid, Thiocyanat + H2O2
|Produkte = Hypoiodit, Hypobromit, Hypothiocyanit + H2O
|Homolog_fam =
|Taxon = Tiere
|Taxon_Ausnahme =
|Orthologe = {{Protein Orthologe
| Spezies1 = Mensch
| Spezies2 = Hausmaus
| S1_EntrezGene =4025
| S1_Ensembl =ENSG00000167419
| S1_RefseqmRNA =NM_001160102
| S1_RefseqProtein = NP_001153574
| S1_GenLoc_db =
| S1_GenLoc_chr =17
| S1_GenLoc_start =58237737
| S1_GenLoc_end =58268536
| S1_Uniprot =P22079
| S2_EntrezGene =76113
| S2_Ensembl = ENSMUSG00000009356
| S2_RefseqmRNA =NM_080420
| S2_RefseqProtein = NP_536345
| S2_GenLoc_db =
| S2_GenLoc_chr = 11
| S2_GenLoc_start = 87806428
| S2_GenLoc_end = 87826135
| S2_Uniprot = Q5SW46
}}
}}

Das [[Enzym]] '''Lactoperoxidase (LPO)''' kommt in den meisten Tieren vor und wird im Menschen von den [[Brustdrüse]]n, [[Speicheldrüse]]n und [[Schleimdrüse]]n der [[Bronchie]]n ausgeschieden. Es [[Katalyse|katalysiert]] die [[Oxidation]] von [[Phenole]]n und verschiedenen [[Anion]]en durch [[Wasserstoffperoxid]]. Die Reaktionsprodukte sind hochreaktive Moleküle, die toxisch auf in den Körper eingedrungene [[Mikroorganismus|Mikroorganismen]] wirken. LPO ist daher ein Teil des angeborenen (unspezifischen) [[Angeborene Immunantwort|Immunsystems]] und ermöglicht die Neutralisierung von [[Bakterien]] in der [[Milch]] und anderen [[Schleimhaut]]sekreten.<ref name="pmid6931123">{{cite journal | author =EL. Thomas, KP. Bates, MM. Jefferson | title = Hypothiocyanite ion: detection of the antimicrobial agent in human saliva | journal = [[J Dent Res]] | volume = 59 | issue = 9 | pages = 1466–1472 | year = 1980 | month = September | pmid = 6931123 | doi = 10.1177/00220345800590090201| url = |language=en }}</ref><ref name="Tenovuo_1985">{{cite book | author = JO Tenovuo | editor = JO. Tenovuo, KM. Pruitt | others = | title = The Lactoperoxidase system: chemistry and biological significance | edition = | publisher = Dekker | location = New York | year = 1985 | origyear = | pages = 272 | isbn = 0-8247-7298-9 | doi = | chapter = The peroxidase system in human secretions |language=en}}</ref><ref name="pmid2222811">{{cite journal | author = TJ. Dull, C. Uyeda, AD. Strosberg, G. Nedwin, JJ. Seilhamer | title = Molecular cloning of cDNAs encoding bovine and human lactoperoxidase | journal = DNA Cell Biol. | volume = 9 | issue = 7 | pages = 499–509 | year = 1990 | month = September | pmid = 2222811 | doi = 10.1089/dna.1990.9.499| url = |language=en }}</ref><ref name="pmid8964511">{{cite journal | author = C. Kiser, CK. Caterina, JA. Engler, B. Rahemtulla, F. Rahemtulla | title = Cloning and sequence analysis of the human salivary peroxidase-encoding cDNA | journal = Gene | volume = 173 | issue = 2 | pages = 261–264 | year = 1996 | month = September | pmid = 8964511 | doi = 10.1016/0378-1119(96)00078-9| url = |language=en }}</ref><ref name="pmid2545551">{{cite journal | author = H. Kohler, H. Jenzer | title = Interaction of lactoperoxidase with hydrogen peroxide. Formation of enzyme intermediates and generation of free radicals | journal = [[Free Radical Biology and Medicine]] | volume = 6 | issue = 3 | pages = 323–339 | year = 1989 | pmid = 2545551 | doi = 10.1016/0891-5849(89)90059-2| url = |language=en }}</ref><ref name="Pruitt_Reiter_1985">{{cite book | author = KM. Pruitt, B. Reiter | editor = JO. Tenovuo, KM. Pruitt | others = | title = The Lactoperoxidase system: chemistry and biological significance | edition = | publisher = Dekker | location = New York | year = 1985 | origyear = | pages = 272 | isbn = 0-8247-7298-9 | doi = | chapter = Biochemistry of peroxidase systems: antimicrobial effects |language=en}}</ref><ref name="pmid12626341">{{cite journal | author = C. Wijkstrom-Frei, S. El-Chemaly, R. Ali-Rachedi, C. Gerson, MA. Cobas, R. Forteza, M. Salathe, GE. Conner | title = Lactoperoxidase and human airway host defense | journal = Am. J. Respir. Cell Mol. Biol. | volume = 29 | issue = 2 | pages = 206–212 | year = 2003 | month = August | pmid = 12626341 | doi = 10.1165/rcmb.2002-0152OC | url = |language=en }}</ref><ref name="pmid12471090">{{cite journal | author = GE. Conner, M. Salathe, R. Forteza | title = Lactoperoxidase and hydrogen peroxide metabolism in the airway | journal = Am. J. Respir. Crit. Care Med | volume = 166 | issue = 12 Pt 2 | pages = S57–61 | year = 2002 | month = December | pmid = 12471090 | doi = 10.1164/rccm.2206018 | url = |language=en }}</ref><ref name="pmid17204267">{{cite journal | author = GE. Conner, C. Wijkstrom-Frei, SH. Randell, VE. Fernandez, M. Salathe | title = The Lactoperoxidase System Links Anion Transport To Host Defense in Cystic Fibrosis | journal = [[FEBS Lett]]. | volume = 581 | issue = 2 | pages = 271–278 | year = 2007 | month = January | pmid = 17204267 | pmc = 1851694 | doi = 10.1016/j.febslet.2006.12.025 | url = |language=en }}</ref><ref name="ISBN 0-8247-7298-9" />

Unter dem '''Lactoperoxidase-System''' versteht man die Kombination aus Lactoperoxidase und dessen ionischen Substraten, dem Wasserstoffperoxid sowie den Oxidationsprodukten.
Bekannte Substrate sind [[Bromide|Bromid]]- und [[Iodide|Iodid]]-Ionen, aber auch das [[Thiocyanate|Thiocyanat]]-Ion. Die Produkte der enzymkatalysierten Oxidation sind stark antibakteriell wirksam, vermutlich durch Hemmung der Glucose-Aufnahme.<ref name="pmid9872115">{{cite journal | author = Loimaranta V, Tenuovo J, Korhonen H | title = Combined inhibitory effect of bovine immune whey and peroxidase-generated hypothiocyanite against glucose uptake by Streptococcus mutans | journal = Oral Microbiol Immunol | volume = 13 | issue = 6 | pages = 378–381 | year = 1998 | month = | pmid = 9872115 | pmc = | doi = | url = |language=en }}</ref>

== Struktur ==

Die Struktur der Lactoperoxidase besteht hauptsächlich aus [[Alpha-Helix|α-Helices]]. Hinzu kommen zwei kurze antiparallele [[Beta-Faltblatt|β-Faltblätter]]. Ein [[Häme (Stoffgruppe)|Häm]]-Cofaktor befindet sich nahe dem Zentrum des [[Apoprotein]]s.<ref name="pmid18191143" />

== Funktion ==

Die Lactoperoxidase katalysiert die Oxidation verschiedener Sauerstoff-Akzeptoren durch [[Wasserstoffperoxid]] (H2O2):<ref name="de Wit_1996">{{cite journal | author = de Wit JN, van Hooydonk ACM | title = Structure, functions and applications of lactoperoxidase in natural antimicrobial systems | journal = Netherlands Milk & Dairy Journal |volume = 50 | issue = | pages = 227–244 | year = 1996 | month = | pmid = | doi = | url = |language=en }}</ref>

* reduzierter Akzeptor + H2O2 → oxidierter Akzeptor + H2O

Beispiele solcher [[Oxidation]]sreaktionen sind:

* [[Thiocyanate|Thiocyanat]] (SCN−) → [[Hypothiocyanit]] (OSCN−)<ref name="Wever_1982">{{cite journal | author = R. Wever, WM. Kast, JH. Kasinoedin, R. Boelens | title = The peroxidation of thiocyanate catalysed by myeloperoxidase and lactoperoxidase | journal = [[Biochim. Biophys. Acta]] | volume = 709 | issue = 2 | pages = 212–219 | year = 1982 | month = December | pmid = 6295491 | doi = 10.1016/0167-4838(82)90463-0| url = |language=en }}</ref><ref name="pmid7066307">{{cite journal | author = KM. Pruitt, J. Tenovuo, RW. Andrews, T. McKane | title = Lactoperoxidase-catalyzed oxidation of thiocyanate: polarographic study of the oxidation products | journal = [[Biochemistry]] | volume = 21 | issue = 3 | pages = 562–567 | year = 1982 | month = February | pmid = 7066307 | doi = 10.1021/bi00532a023| url = |language=en }}</ref>
* [[Bromide|Bromid]] (Br−) → [[Hypobromite|Hypobromit]] (BrO−)
* [[Iodide|Iodid]] (I−) → [[Hypoiodite|Hypoiodit]] (IO−)

Quelle des Wasserstoffperoxids ist vielfach die Reaktion von [[Glucose]] mit [[Sauerstoff]] in Gegenwart des Enzyms [[Glucose-Oxidase]] ({{EC|1.1.3.4}}), die ebenfalls im [[Speichel]] stattfindet. Die Glucose wiederum kann in Gegenwart des Speichel-Enzyms Amyloglucosidase (γ-[[Amylasen|Amylase]] ({{EC|3.2.1.3}})) aus [[Stärke]] entstehen.
Derartige Oxidationsprodukte sind hoch reaktiv und antibakteriell stark wirksam.<ref name="ISBN 0-8247-7298-9">{{cite book | author = | authorlink = | editor = JO. Tenovuo, KM. Pruitt | others = | title = The Lactoperoxidase system: chemistry and biological significance | edition = | publisher = Dekker | location = New York | year = 1985 | pages = 272| isbn = 0-8247-7298-9 | doi = | accessdate = |language=en }}</ref><ref name="pmid352945">{{cite journal | author = EL. Thomas, TM. Aune | title = Lactoperoxidase, peroxide, thiocyanate antimicrobial system: correlation of sulfhydryl oxidation with antimicrobial action | journal = [[Infection and Immunity]] | volume = 20 | issue = 2 | pages = 456–463 | year = 1978 | month = May | pmid = 352945 | pmc = 421877 | doi = | url = |language=en }}</ref> Das Lactoperoxidase-System ist in der Lage, eine ganze Reihe von [[Aerobe Atmung|aerobischen]]<ref name="pmid18565914">{{cite journal | author =LW. Fweja, MJ. Lewis, AS. Grandison | title = Challenge testing the lactoperoxidase system against a range of bacteria using different activation agents | journal = J. Dairy Sci. | volume = 91 | issue = 7 | pages = 2566–2574 | year = 2008 | month = July | pmid = 18565914 | doi = 10.3168/jds.2007-0322 | url = |language=en }}</ref> und [[Anaerobe Atmung|anaerobischen]] Bakterien,<ref name="pmid1481764">{{cite journal | author = P. Courtois, P. Majerus, M. Labbé, Vanden A. Abbeele, E. Yourassowsky, M. Pourtois | title = Susceptibility of anaerobic microorganisms to hypothiocyanite produced by lactoperoxidase | journal = Acta Stomatol Belg | volume = 89 | issue = 3 | pages = 155–162 | year = 1992 | month = September | pmid = 1481764 | doi = | url = |language=en }}</ref> darunter auch [[mikroaerophil]]e [[Helicobacter pylori]].<ref name="pmid15314191">{{cite journal | author = A. Haukioja, R. Ihalin, V. Loimaranta, M. Lenander, J. Tenovuo | title = Sensitivity of Helicobacter pylori to an innate defence mechanism, the lactoperoxidase system, in buffer and in human whole saliva | journal = J. Med. Microbiol | volume = 53 | issue = Pt 9 | pages = 855–860 | year = 2004 | month = September | pmid = 15314191 | doi = 10.1099/jmm.0.45548-0| url = |language=en }}</ref>
Der Effekt des Lactoperoxidase-Systems hängt von bestimmten experimentellen Bedingungen ab. Wenn Bakterien unter aerobischen Bedingungen auf Nähragar kultiviert werden sollen, nachdem sie dem Lactoperoxidase-System ausgesetzt waren, wachsen sie nicht. Allerdings wachsen sie sehr wohl auf Blut-Agar unter anaerobischen Bedingungen.<ref name="pmid6724690" /> Das Lactoperoxidase-System scheint synergistisch mit [[Lactoferrin]]<ref name="pmid6345430">{{cite journal | author =B. Reiter | title = The biological significance of lactoferrin | journal = Int J Tissue React | volume = 5 | issue = 1 | pages = 87–96 | year = 1983 | pmid = 6345430 | doi = | url = |language=en }}</ref> und [[Lysozym]]<ref name="pmid7850845">{{cite journal | author =V. Roger, J. Tenovuo, M. Lenander-Lumikari, E. Söderling, P. Vilja | title = Lysozyme and lactoperoxidase inhibit the adherence of Streptococcus mutans [[National Collection of Type Cultures|NCTC]] 10449 (serotype c) to saliva-treated hydroxyapatite in vitro | journal = [[Caries Res]]. | volume = 28 | issue = 6 | pages = 421–428 | year = 1994 | pmid = 7850845 | doi = 10.1159/000262015| url = |language=en }}</ref> zu agieren.
Ist [[Wasserstoffperoxid]] im Überschuss zum Thiocyanat vorhanden, kann das Lactoperoxidase-System auch cytotoxisch wirken.<ref name="pmid6724690">{{cite journal | author = J. Carlsson, MB. Edlund, L. Hänström | title = Bactericidal and cytotoxic effects of hypothiocyanite-hydrogen peroxide mixtures | journal = Infect Immun | volume = 44 | issue = 3 | pages = 581–6 | year = 1984 | month = June | pmid = 6724690 | pmc = 263633 | doi = | url = |language=en }}</ref>

== Anwendungen ==

Aufgrund der antibakteriellen Wirksamkeit des Lactoperoxidase-Systems<ref name="Harper_2000">{{cite book | last = Harper | first = W. James | title = Biological properties of whey components a review | publisher = American Dairy Products Institute | location = Chicago IL | year = 2000 | pages = 54 |language=en}}</ref> wird es zur Konservierung von Nahrungsmitteln und Kosmetika sowie in der Augenheilkunde eingesetzt. Weitere Anwendungen finden sich in den Bereichen Zahnheilkunde und Wundbehandlung. Möglicherweise kann das Lactoperoxidase-System auch zur Bekämpfung von Tumoren und Viren eingesetzt werden.<ref name="pmid2790777">{{cite journal | author = M. Stanislawski, V. Rousseau, M. Goavec, H. Ito | title = Immunotoxins containing glucose oxidase and lactoperoxidase with tumoricidal properties: in vitro killing effectiveness in a mouse plasmacytoma cell model | journal = [[Cancer Res]]. | volume = 49 | issue = 20 | pages = 5497–5504 | year = 1989 | month = October | pmid = 2790777 | doi = | url = |language=en }}</ref><ref name="pmid2402192">{{cite journal | author = DL. Lefkowitz, TC. Hsieh, K. Mills, A. Castro | title = Induction of tumor necrosis factor and cytotoxicity by macrophages exposed to lactoperoxidase and microperoxidase | journal = [[Life Sci]]. | volume = 47 | issue = 8 | pages = 703–709 | year = 1990 | pmid = 2402192 | doi = 10.1016/0024-3205(90)90625-2| url = |language=en }}</ref><ref name="pmid7605114">{{cite journal | author = H. Mikola, M. Waris, J. Tenovuo | title = Inhibition of herpes simplex virus type 1, respiratory syncytial virus and echovirus type 11 by peroxidase-generated hypothiocyanite | journal = [[Antiviral Res]]. | volume = 26 | issue = 2 | pages = 161–171 | year = 1995 | month = March | pmid = 7605114 | doi = 10.1016/0166-3542(94)00073-H| url = |language=en }}</ref><ref name="pmid1650564">{{cite journal | author = M. Pourtois, C. Binet, Van N. Tieghem, PR. Courtois, A. Vandenabbeele, L. Thirty | title = Saliva can contribute in quick inhibition of HIV infectivity | journal = [[AIDS (Zeitschrift)|AIDS]] | volume = 5 | issue = 5 | pages = 598–600 | year = 1991 | month = May | pmid = 1650564 | doi = 10.1097/00002030-199105000-00022| url = |language=en }}</ref>

=== Milch und Milchprodukte ===

Das Lactoperoxidase-System hemmt das Wachstum der bakteriellen [[Flora]] in der [[Milch]] und in Milchprodukten.<ref name="Reiter_1984">{{cite journal | author = B. Reiter, BG Härnulv | title = The preservation of refrigerated and uncooled milk by its natural lactoperoxidase system | journal = Dairy Ind. Int. | volume = 47 | issue = 5 | pages = 13–19 |language=en}}</ref> Die Zugabe von [[Wasserstoffperoxid]] und einem [[Thiocyanate|Thiocyanat]] verlängert die Haltbarkeit gekühlter Rohmilch.<ref name="de Wit_1996" /><ref name="Zajac_1983a">{{cite journal | author = M. Zajac, J. Glandys, M. Skarzynska, G. Härnulv, K. Eilertsen | year = 1983 | title = Milk quality preservation by heat treatment or activation of the lactoperoxidase system in combination with refrigerated storage | journal = Milchwissenschaft | volume = 38 | issue = 11 |language=en}}</ref><ref name="Zajac_1983b">{{cite journal | author = M. Zajac, J. Glandys, M. Skarzynska, G. Härnulv, L. Björck | title = Changes in bacteriological quality of raw milk stabilized by activation of its lactoperoxidase system and stored at different temperatures | year = 1983 | journal= J. Of Food Prot. | volume = 46 | issue = 12 | pages = 1065–1068 |language=en}}</ref><ref name="Korhonen_1980">{{cite journal | author = H. Korhonen | title = A new method for preserving raw milk: The lactoperoxidase antibacterial system | journal = World Anim. Rev. | volume = 35 |issue = | pages = 23–29 | year = 1980 | month = | pmid = | doi = | url = |language=en }}</ref> Das Lactoperoxidase-System ist vergleichsweise wärmestabil und wird als Indikator für eine Überpasteurisierung von Milch verwendet.<ref name="Marks_2008">{{cite journal |author=NE. Marks, AS. Grandison, MJ. Lewis |title=Use of hydrogen peroxide detection strips to determine the extent of pasteurization in whole milk |journal=International Journal of Dairy Technology |issue=1 |volume=54 |pages=20–22 |year=2008 |doi=10.1046/j.1471-0307.2001.00008.x |url=https://onlinelibrary.wiley.com/doi/10.1046/j.1471-0307.2001.00008.x |language=en}}</ref>

=== Zahnheilkunde ===

Das Lactoperoxidase-System scheint auch zur Behandlung von [[Karies]], [[Gingivitis]] und [[Parodontitis]] geeignet zu sein<ref name="Poulson OM">{{patent
| Land = WO
| V-Nr = 1988002600
| Typ = Patentanmeldung
| Titel = Enzyme-containing bactericidal composition, and dental and wound treatment preparations comprising this composition
| A-Datum = 1988-04-21
| V-Datum =
| Erfinder = Poulson OM
| Anmelder =
| Kommentar =
}}</ref> und wird daher als Bestandteil von Zahnpasten und Mundspüllösungen eingesetzt. Weil es das Bakterienwachstum in der Mundhöhle hemmt, hemmt es auch die Säureproduktion dieser Bakterien.<ref name="Hoogedoorn_1985">{{cite book | author = H. Hoogedoorn | editor = Tenovuo JO, Pruitt KM | others = | title = The Lactoperoxidase system: chemistry and biological significance | edition = | publisher = Dekker | location = New York | year = 1985 | origyear = | pages = 217–228 | isbn = 0-8247-7298-9 | doi = | chapter = Activation of the salivary peroxidase system: clinical studies | accessdate = |language=en }}</ref>

== Klinische Bedeutung des Lactoperoxidase-Systems ==

=== Zahn- und Mundgesundheit ===
In den letzten Jahrzehnten sind eine Reihe von klinischen Studien zur Wirksamkeit des Lactoperoxidase-Systems in verschiedenen Mundhygiene-Produkten (Zahnpasten, Mundspüllösungen) veröffentlicht worden. Nachdem indirekt über die Messung experimenteller [[Gingivitis]]- und [[Karies]]-Parameter gezeigt worden war, dass Mundspüllösungen,<ref name="pmid4522423">{{cite journal | author = A. Hugoson, G. Koch, H. Thilander, H. Hoogendorn | title = Lactoperoxidase in the prevention of plaque accumulation, gingivitis and dental caries (III) | journal = Odont revy | volume = 25 | issue = | pages = 69–80 | year = 1974 | month = | pmid = 4522423 | pmc = | doi = | url = |language=en }}</ref><ref name="pmid3098804">{{cite journal | author = Midda M, Cooksey MV | title = Clinical use of an enzyme-containing dentifrice | journal = [[J Clin Periodontol]] | volume = 13 | issue = 10| pages = 959–956 | year = 1986 | month = | pmid = 3098804 |language=en}}</ref> welche Amyloglucosidase (γ-[[Amylasen|Amylase]]) und [[Glucose-Oxidase]] enthalten, das Lactoperoxidase-System aktivieren, sind aus jüngster Zeit Studien bekannt, die den Mechanismus der Schutzfunktion von [[Enzyme]]n in Mundhygieneprodukten beleuchten. So werden Enzyme wie [[Lysozym]], Lactoperoxidase und Glucose-Oxidase von den Zahnpasten auf das [[Pellikel (Zahnmedizin)|Pellikel]] übertragen. Als Bestandteil des Pellikels sind diese Enzyme katalytisch hoch aktiv.<ref name="pmid20417500">{{cite journal | author =C. Hannig, B. Spitzmüller, HC. Lux, M. Altenburger, A. Al-Ahmad, M. Hannig | title = Efficacy of enzymatic toothpastes for immobilisation of protective enzymes in the in situ pellicle | journal = Arch Oral Biol | volume = 55 | issue = | pages = 463–469 | year = 2010 | month = | pmid = 20417500 | pmc = | doi = | url = |language=en }}</ref><ref name="pmid15693823">{{cite journal | author = C. Hannig, M. Hannig, T. Attin | title = Enzymes in the acquired enamel pellicle | journal = Eur J Oral Sci | volume = 113 | issue = | pages = 2–13 | year = 2005 | month = | pmid = 15693823 | pmc = | doi = | url = |language=en }}</ref> Ebenso hat das Lactoperoxidase-System als Bestandteil von Zahnpasten einen günstigen Einfluss auf die Vermeidung frühkindlicher Karies,<ref name="pmid19725235">{{cite journal | author = S. Jyoti, ND. Shasikiran, VV. Reddy | title = Effect of lactoperoxidase system containing toothpaste on cariogenic bacteria in children with early childhood caries | journal = J Clin Pediatr Dent | volume = 33 | issue = 4 | pages = 299–303 | year = 2009 | month = | pmid = 19725235 | pmc = | doi = | url = |language=en }}</ref> indem es die Zahl gebildeter Kolonien kariogener Mikroflora herabsetzt, während gleichzeitig die [[Thiocyanat]]-Konzentration steigt. Zahnpasten mit dem Lactoperoxidase-System erwiesen sich bei [[Xerostomie]]-Patienten im Vergleich zu [[fluorid]]haltigen Zahnpasten hinsichtlich [[Zahnbelag|Plaque]]-Bildung und [[Zahnfleisch]]entzündungen als überlegen.<ref name="pmid8063434-1">{{cite journal | author = D. van Steenberghe, E. Van den Eynde, R. Jacobs, M. Quirynen | title = Effect of a lactoperoxidase containing toothpaste in radiation-induced xerostomia | journal = Int Dent J | volume = 44 | issue = 2 | pages = 133–138 | year = 1994 | month = | pmid = 15693823 | pmc = | doi = | url = |language=en }}</ref> Weitere Studien dieser Art sollten folgen,<ref name="pmid8063434-2">{{cite journal | author = C. Hannig, M. Hannig, T. Attin| title = Enzymes in the acquired enamel pellicle | journal = Eur J Oral Sci | volume = 113 | issue = | pages = 2–13 | year = 2005 | month = | pmid = 15693823 | pmc = | doi = | url = |language=en }}</ref> nicht zuletzt um den Mechanismus der Schutzwirkung näher zu beleuchten, welcher noch nicht genau aufgeklärt ist.<ref name="pmid7887144">{{cite journal | author = V. Kirstilä, M. Lenander-Lumikari, J. Tenuovo | title = Effects of a lactoperoxidase-system-containing toothpaste on dental plaque and whole saliva in vivo | journal = Acta Odontol Scan | volume = 52 | issue = 6 | pages = 346–353 | year = 1994 | month = | pmid = 7887144 | pmc = | doi = | url = |language=en }}</ref> Die Anwendung von Lactoperoxidase ist nicht auf Karies, Gingivitis und [[Parodontitis]] beschränkt.<ref name="pmid20701667">{{cite journal | author = R. Marino, S. Torretta, P. Capaccio, L. Pignataro, F. Spadari | title = Different therapeutic strategies for burning mouth syndrome: preliminary data | journal = [[J Oral Pathol Med]] | volume = 39 | issue = 8 | pages = 611–616 | year = 2010 | month = | pmid = 20701667 | pmc = | doi = 10.1111/j.1600-0714.2010.00922.x | url = |language=en }}</ref> So kann eine Kombination aus Lysozym und Lactoperoxidase auch zur unterstützenden Behandlung des Burning Mouth Syndroms ([[Glossodynie]]) eingesetzt werden. In Kombination mit Lactoferrin wirkt Lactoperoxidase gegen [[Mundgeruch]],<ref name="pmid20512389">{{cite journal | author = K. Shin, K. Yaegaki, T. Murata, H. Ii, T. Tanaka, I. Aoyama, K. Yamauchi, T. Toida, K. Iwatsuki | title = Effects of a composition containing [[lactoferrin]] and lactoperoxidase on oral malodor and salivary bacteria: a randomized, double-blind, crossover, placebo-controlled clinical trial | journal = [[Clin Oral Investig]] | volume = 15 | issue = 4 | pages = 485–493 | year = 2011 | month = | pmid = 20512389 | pmc = | doi = | url = |language=en }}</ref> in Kombination mit [[Lactoferrin]] und Lysozym trägt Lactoperoxidase zur Linderung von Beschwerden wegen Mundtrockenheit (Xerostomie) bei.<ref name="pmid18194332">{{cite journal | author = JA. Gil-Montoya, I. Guardia-Lopéz, MA. Gonzaléz-Moles | title = Evaluation of the clinical efficacy of a mouthwash and oral gel containing the antimicrobial proteins lactoperoxidase, lysozyme and lactoferrin in elderly patients with dry mouth – a pilot study | journal = Gerodontology | volume = 25 | issue = 1 | pages = 3–9 | year = 2008 | month = | pmid = 18194332 | pmc = | doi = | url = |language=en }}</ref> Ebenso können Gele mit Lactoperoxidase bei Mundhöhlenkrebs-Patienten, deren [[Speichel]]fluss infolge von Bestrahlungen eingeschränkt ist (Xerostomie), zur Symptomlinderung beitragen und gleichzeitig die Bakterien[[flora]] günstig beeinflussen.<ref name="pmid17912104">{{cite journal | author = K. Nagy, E. Urban, O. Fazwkas, L. Thurzo, E. Nagy | title = Controlled study of lactoperoxidase gel on oral flora and saliva in irradiated patients with oral cancer | journal = J Craniofac Surg | volume = 18 | issue = 5 | pages = 1157–1164 | year = 2007 | month = | pmid = 17912104 | pmc = | doi = | url = |language=en }}</ref><ref name="pmid16098116">{{cite journal | author = SA. Shahdad, C. Taylor, SC. Barclay, IN. Steeb, PM. Preshaw | title = A double-blind, crossover study of Biotène Oralbalance and BioXtra systems as salivary substitutes in patients with post- radiotherapy xerostomia | journal = [[Eur J Cancer Care]] | volume = 14 | issue = 4 | pages = 319–326 | year = 2005 | month = | pmid = 16098116 | pmc = | doi = | url = |language=en }}</ref><ref name="pmid15712851">{{cite journal | author = DW. Matear, J. Barbaro | title = Effectiveness of saliva substitute products in the treatment of dry mouth in the elderly: a pilot study | journal = J R Soc Promot Health | volume = 125 | issue = 1 | pages = 35–41 | year = 2005 | month = | pmid = 15712851 | pmc = | doi = | url = |language=en }}</ref>

=== Zystische Fibrose ===

Im Speichel von Patienten mit [[Zystische Fibrose|zystischer Fibrose]] wird weniger Thiocyanat gefunden als in gesunden Patienten.<ref name="pmid19918082">{{cite journal | author = Y. Xu, S. Szép, Z. Lu | title = The antioxidant role of thiocyanate in the pathogenesis of cystic fibrosis and other inflammation-related diseases | journal = [[Proc. Natl. Acad. Sci. U.S.A.]] | volume = 106 | issue = 48 | pages = 20515–9 | year = 2009 | month = December | pmid = 19918082 | pmc = 2777967 | doi = 10.1073/pnas.0911412106 | url = |language=en }}</ref> Weil so auch weniger antibakteriell wirksames Hypothiocyanit gebildet werden kann, könnte dies ein Grund dafür sein, dass diese Patienten gehäuft unter Atemwegserkrankungen leiden.<ref name="pmid17082494">{{cite journal | author = P. Moskwa, D. Lorentzen, KJ. Excoffon, J. Zabner, PB. McCray, WM. Nauseef, C. Dupuy, B. Bánfi | title = A Novel Host Defense System of Airways Is Defective in Cystic Fibrosis | journal = Am. J. Respir. Crit. Care Med | volume = 175 | issue = 2 | pages = 174–183 | year = 2007 | month = January | pmid = 17082494 | pmc = 2720149 | doi = 10.1164/rccm.200607-1029OC | url = |language=en }}</ref><ref name="pmid18519245">{{cite journal | author = Minarowski Ł, D. Sands, A. Minarowska, A. Karwowska, A. Sulewska, M. Gacko, E. Chyczewska | title = Thiocyanate concentration in saliva of cystic fibrosis patients | journal = Folia Histochem. Cytobiol. | volume = 46 | issue = 2 | pages = 245–246 | year = 2008 | pmid = 18519245 | doi = 10.2478/v10042-008-0037-0 | url = |language=en }}</ref>

=== Krebs ===

Antikörper-Konjugate mit Lactoperoxidase töten Tumorzellen ab.<ref name="pmid2790777" /> Makrophagen, die Lactoperoxidase ausgesetzt waren, können Tumorzellen verstärkt neutralisieren.<ref name="pmid2402192" />
Die Oxidation von [[Estradiol]] durch Lactoperoxidase wird als mögliche Quelle für [[Oxidativer Stress|oxidativen Stress]] bei [[Brustkrebs]] gehandelt.<ref name="pmid7955118">{{cite journal | author = HJ. Sipe, SJ. Jordan, PM. Hanna, RP. Mason | title = The metabolism of 17 alpha-estradiol by lactoperoxidase: a possible source of oxidative stress in breast cancer | journal = [[Carcinogenesis]] | volume = 15 | issue = 11 | pages = 2637–2643 | year = 1994 | month = November | pmid = 7955118 | doi = 10.1093/carcin/15.11.2637| url = |language=en }}</ref><ref name="pmid10994878">{{cite journal | author = EM. Ghibaudi, E. Laurenti, P. Beltramo, RP. Ferrari | title = Can estrogenic radicals, generated by lactoperoxidase, be involved in the molecular mechanism of breast carcinogenesis? | journal = Redox Rep. | volume = 5 | issue = 4 | pages = 229–235 | year = 2000 | pmid = 10994878 | doi = 10.1179/135100000101535672| url = |language=en }}</ref><ref name="pmid10994878" /> Auch [[Östrogen]] wird in Gegenwart von Lactoperoxidase oxidiert. Dabei entsteht am phenolischen A-Ring des Östrogens ein reaktives Phenoxy-Radikal.<ref name="pmid16944280">{{cite journal | author = Løvstad RA | title = A kinetic study on the lactoperoxidase catalyzed oxidation of estrogens | journal = Biometals | volume = 19 | issue = 6 | pages = 587–592 | year = 2006 | month = December | pmid = 16944280 | doi = 10.1007/s10534-006-0002-3 | url = |language=en }}</ref> Durch die Einwirkung von Lactoperoxidase könnten carcinogene Amine so aktiviert werden, dass sie vermehrt mit DNS reagieren und so zur Bildung von Brustkrebs beitragen.<ref name="pmid15606142">{{cite journal | author = KM. Gorlewska-Roberts, CH. Teitel, JO. Lay, DW. Roberts, FF. Kadlubar | title = Lactoperoxidase-catalyzed activation of carcinogenic aromatic and heterocyclic amines | journal = [[Chemical Research in Toxicology]] | volume = 17 | issue = 12 | pages = 1659–1666 | year = 2004 | month = December | pmid = 15606142 | doi = 10.1021/tx049787n | url = |language=en }}</ref>

== Weblinks ==
* {{MeshName|Lactoperoxidase}}

== Einzelnachweise ==
<references />

[[Kategorie:Oxidoreduktase]]
[[Kategorie:Codiert auf Chromosom 17 (Mensch)]]

Lactoperoxidase - Versionsgeschichte

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