Lactoperoxidase

Last updated
LPO
Lactoperoxidase 2R5L.png
Identifiers
Aliases LPO , SPO, lactoperoxidase
External IDs OMIM: 150205; MGI: 1923363; HomoloGene: 21240; GeneCards: LPO; OMA:LPO - orthologs
Orthologs
SpeciesHumanMouse
Entrez

4025

76113

Ensembl

ENSG00000167419

ENSMUSG00000009356

UniProt

P22079

n/a

RefSeq (mRNA)

NM_001160102
NM_006151

NM_080420

RefSeq (protein)

NP_001153574
NP_006142

n/a

Location (UCSC) Chr 17: 58.22 – 58.27 Mb Chr 11: 87.7 – 87.72 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Lactoperoxidase (LPO, EC 1.11.1.7) is a peroxidase enzyme secreted from mammary, salivary, tears and other mucosal glands including the lungs, bronchii and nose [5] that function as a natural, first line of defense against bacteria and viral agents. [6] Lactoperoxidase is a member of the heme peroxidase family of enzymes. In humans, lactoperoxidase is encoded by the LPO gene. [7] [8]

Contents

Lactoperoxidase catalyzes the oxidation of several inorganic and many organic substrates by hydrogen peroxide. [9] Lactoperoxidase rapidly oxidizes iodide and slowly oxidizes bromide and is designated a haloperoxidase. Another important substrate is the pseudo-halide thiocyanate. The oxidized products display potent, non-specific bactericidal and antiviral activities, including destruction of the influenza virus. Lactoperoxidase together with its inorganic ion substrates, hydrogen peroxide, DUOX1 and DUOX2 and products are termed the lactoperoxidase system. [10] Hence LPO is considered a very important defense against invasive bacteria and viral agents such as influenza and the SARS-CoV-2 virus when sufficient iodine is provided. [11] [12] [13]

The LPO system plays an important role in the innate immune system by destroying bacteria in milk and mucosal (linings of mostly endodermal origin, covered in epithelium involved in absorption and secretion) secretions. Hence augmentation of the lactoperoxidase system may have therapeutic applications and applications for controlling bacteria in food and consumer health care products. This system does not vigorously attack DNA and is not mutagenic. [14] However, under certain conditions, the LPO system may contribute to oxidative stress though recent evidence indicates LPO to be protective. [15] [16] LPO may contribute to the initiation of breast cancer, through its ability to oxidize estrogenic hormones producing free radical intermediates. [17]

Structure

The structure of lactoperoxidase consists mainly of alpha-helices plus two short antiparallel beta-strands. [18] Lactoperoxidase belongs to the heme peroxidase family of mammalian enzymes that also includes myeloperoxidase (MPO), eosinophil peroxidase (EPO), thyroid peroxidase (TPO), and prostaglandin H synthase (PGHS). A heme cofactor is covalently bound near the center of the protein. [19]

Function

Lactoperoxidase catalyzes the hydrogen peroxide (H2O2) oxidation of several acceptor molecules: [20]

reduced acceptor + H2O2 → oxidized acceptor + H2O

Specific examples include:

Depending on conditions the turnovers with SCN− or I− are roughly similar. The turnover with Br− is about 10−4 smaller than the other two anions. In mammals the source of hydrogen peroxide is one of the duox1 or duox2 enzymes which reduce dioxygen to H2O2 by oxidizing NADPH. [25] In the laboratory the source of the hydrogen peroxide (H2O2) usually is the reaction of glucose with oxygen in the presence of the enzyme glucose oxidase (EC 1.1.3.4) that also takes place in saliva. Glucose, in turn, can be formed from starch in the presence of the saliva enzyme amyloglucosidase (EC 3.2.1.3).

These relatively short lived oxidized intermediates have potent bactericidal effects, hence lactoperoxidase is part of the antimicrobial defense system in tissues that express lactoperoxidase. [10] The lactoperoxidase system is effective in killing a range of aerobic [26] and certain anaerobic microorganisms. [27] Research (1984): "The effect of lactoperoxidase-thiocyanate-hydrogen peroxide mixtures on bacteria is dependent on experimental conditions. If the bacteria are cultured after the exposure to lactoperoxidase-thiocyanate-hydrogen peroxide on nutrient agar under aerobic conditions, they may not grow, whereas they grow readily on blood agar under anaerobic conditions." [28] In its antimicrobial capacity, lactoperoxidase appears to acts synergistically with lactoferrin [29] and lysozyme. [30]

Applications

Lactoperoxidase is an effective antimicrobial and antiviral agent. Consequently, applications of lactoperoxidase are being found in preserving food, cosmetics, and ophthalmic solutions. Furthermore, lactoperoxidase have found application in dental and wound treatment. Finally lactoperoxidase may find application as anti-tumor and anti viral agents. [31] Lactoperoxidase has been used with radioactive iodine to selectively label membrane surfaces. [32]

Dairy products

Lactoperoxidase is an effective antimicrobial agent and is used as an antibacterial agent in reducing bacterial microflora in milk and milk products. [33] Activation of the lactoperoxidase system by addition of hydrogen peroxide and thiocyanate extends the shelf life of refrigerated raw milk. [20] [34] [35] [36] It is fairly heat resistant and is used as an indicator of overpasteurization of milk. [37]

Oral care

A lactoperoxidase system is claimed to be appropriate for the treatment of gingivitis and paradentosis. [38] Lactoperoxidase has been used in toothpaste or a mouthrinse to reduce oral bacteria and consequently the acid produced by those bacteria. [39]

Cosmetics

A combination of lactoperoxidase, glucose, glucose oxidase (GOD), iodide and thiocyanate is claimed to be effective in the preservations of cosmetics. [40]

Cancer

Antibody conjugates of glucose oxidase and to lactoperoxidase have been found to effective in killing tumor cells in vitro. [41] In addition, macrophages exposed to lactoperoxidase are stimulated to kill cancer cells. [42] Knockout mice deficient in lactoperoxidase suffer ill-health and develop tumors. [43]

Clinical significance

Innate immune system

The antibacterial and anti-viral activities of lactoperoxidase play an important role in the mammalian immune defense system; the lactoperoxidase system is considered the first line of defense against airborne bacteria and viral agents. [44] [45] [46] Importantly, lactoperoxidase is also extruded into the lung, bronchii and nasal mucus. [47]

Hypothiocyanite is one of the reactive intermediates produced by the activity of lactoperoxidase on thiocyanate and hydrogen peroxide produced by dual oxidase 2 proteins, also known as Duox2. [48] [49] Thiocyanate secretion [50] in cystic fibrosis patients is decreased, resulting in a reduced production of the antimicrobial hypothiocyanite and consequently contributes to increased risk of airway infection. [51] [52]

Viral infections

Peroxidase-generated hypoiodous acid (HOI), hypoiodite and hypothiocyanite all destroy the herpes simplex virus [53] and human immunodeficiency virus. [54] Both the hypothiocyanite and the hypoiodate ion products are very potent and importantly non-specific antiviral oxidants which are lethal, even in small concentrations, to the influenza virus. [55] The anti-viral activity of lactoperoxidase is enhanced with increasing concentrations of iodide ion. [56] This enzyme has been shown effective against a highly dangerous and tough RNA virus (poliovirus) and a long-lived DNA virus (vaccina). [57]

Bacterial infections

The duox2-lactoperoxidase system has been shown to offer protection against many dozens of bacteria and mycoplasmas including varieties of the clinically important Staphylococcus and many Streptococcus types. [58] The lactoperoxidase system efficiently inhibits the common helicobacter pylori in buffer; however, in whole human saliva, it seems to have a weaker effect against this microbe. [59] It has been shown that lactoperoxidase in the presence of thiocyanide can catalyze the bactericidal and cytotoxic effects of hydrogen peroxide under specific conditions when hydrogen peroxide is present in excess of thiocyanide. [28] The combination of lactoperoxidase, hydrogen peroxide and thiocyanide is much more effective than hydrogen peroxide alone to inhibit bacterial metabolism and growth. [60]

Breast cancer

The oxidation of estradiol by lactoperoxidase is a possible source of oxidative stress in breast cancer. [15] [17] The ability of lactoperoxidase to propagate a chain reaction leading to oxygen consumption and intracellular hydrogen peroxide accumulation could explain the hydroxyl radical-induced DNA base lesions recently reported in female breast cancer tissue. [15] Lactoperoxidase may be involved in breast carcinogenesis, because of its ability to interact with estrogenic hormones and oxidise them through two one-electron reaction steps. [17] Lactoperoxidase reacts with the phenolic A-ring of estrogens to produce reactive free radicals. [61] In addition, lactoperoxidase may activate carcinogenic aromatic and heterocyclic amines and increase binding levels of activated products to DNA, which suggests a potential role of lactoperoxidase-catalyzed activation of carcinogens in the causation of breast cancer. [62]

Oral Care

During the last decades, several clinical studies describing the clinical efficacy of the lactoperoxidase system in a variety of oral care products (tooth pastes, mouth rinses) have been published. After showing indirectly, by means of measuring experimental gingivitis and caries parameters, that mouth rinses [63] [64] containing amyloglucosidase (γ-amylase) and glucose oxidase activate the lactoperoxidase system, the protective mechanism of the enzymes in oral care products has been partially elucidated. Enzymes such as lysozyme, lactoperoxidase and glucose oxidase are transferred from the tooth pastes to the pellicle. Being components of the pellicle, these enzymes are catalytically highly active. [65] [66] Also, as part of tooth pastes, the lactoperoxidase system has a beneficial influence to avoid early childhood caries [67] by reducing the number of colonies formed by the cariogenic microflora while increasing the thiocyanate concentration. With xerostomia patients, tooth pastes with the lactoperoxidase system are seemingly superior to fluoride-containing tooth pastes with respect to plaque formation and gingivitis. [68] More studies are required [66] to examine further the protective mechanisms. [69]

The application of lactoperoxidase is not restricted to caries, gingivitis, and periodontitis. [70] A combination of lysozyme and lactoperoxidase can be applied to support the treatment of the burning mouth syndrome (glossodynia). In combination with lactoferrin, lactoperoxidase combats halitosis; [71] in combination with lactoferrin and lysozyme, lactoperoxidase helps to improve symptoms of xerostomia. [72] Furthermore, gels with lactoperoxidase help to improve symptoms of oral cancer when saliva production is compromised due to irradiation. In this case, also the oral bacterial flora are influenced favorably. [73] [74] [75]

See also

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000167419 – Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000009356 – Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ Tenovuo JO (1985). "The peroxidase system in human secretions". In Tenovuo JO, Pruitt KM (eds.). The Lactoperoxidase system: chemistry and biological significance. New York: Dekker. p. 272. ISBN   978-0-8247-7298-7.
  6. ↑ Pruitt KM, Reiter B (1985). "Biochemistry of peroxidase systems: antimicrobial effects". In Tenovuo JO, Pruitt KM (eds.). The Lactoperoxidase system: chemistry and biological significance. New York: Dekker. p. 272. ISBN   978-0-8247-7298-7.
  7. ↑ Dull TJ, Uyeda C, Strosberg AD, Nedwin G, Seilhamer JJ (September 1990). "Molecular cloning of cDNAs encoding bovine and human lactoperoxidase". DNA and Cell Biology. 9 (7): 499–509. doi:10.1089/dna.1990.9.499. PMID   2222811.
  8. ↑ Kiser C, Caterina CK, Engler JA, Rahemtulla B, Rahemtulla F (September 1996). "Cloning and sequence analysis of the human salivary peroxidase-encoding cDNA". Gene. 173 (2): 261–4. doi:10.1016/0378-1119(96)00078-9. PMID   8964511.
  9. ↑ Kohler H, Jenzer H (1989). "Interaction of lactoperoxidase with hydrogen peroxide. Formation of enzyme intermediates and generation of free radicals". Free Radical Biology & Medicine. 6 (3): 323–39. doi:10.1016/0891-5849(89)90059-2. PMID   2545551.
  10. 1 2 Tenovuo JO, Pruitt KM, eds. (1985). The Lactoperoxidase system: chemistry and biological significance. New York: Dekker. p. 272. ISBN   978-0-8247-7298-7.
  11. ↑ Rayman MP (November 2020). "Iodine and Selenium as Antiviral Agents: Potential Relevance to SARS-CoV-2 and Covid-19". Archives of Oral and Maxillofacial Surgery. 3 (1): 69. doi: 10.36959/379/357 . ISSN   2689-8772.
  12. ↑ Derscheid RJ, van Geelen A, Berkebile AR, Gallup JM, Hostetter SJ, Banfi B, et al. (February 2014). "Increased concentration of iodide in airway secretions is associated with reduced respiratory syncytial virus disease severity". American Journal of Respiratory Cell and Molecular Biology. 50 (2): 389–97. doi:10.1165/rcmb.2012-0529OC. PMC   3930944 . PMID   24053146.
  13. ↑ Smith ML, Sharma S, Singh TP (September 2021). "Iodide supplementation of the anti-viral duox-lactoperoxidase activity may prevent some SARS-CoV-2 infections". European Journal of Clinical Nutrition. 76 (4): 629–630. doi:10.1038/s41430-021-00995-2. PMC   8408568 . PMID   34471253.
  14. ↑ White WE, Pruitt KM, Mansson-Rahemtulla B (February 1983). "Peroxidase-thiocyanate-peroxide antibacterial system does not damage DNA". Antimicrobial Agents and Chemotherapy. 23 (2): 267–72. doi:10.1128/aac.23.2.267. PMC   186035 . PMID   6340603.
  15. 1 2 3 Sipe HJ, Jordan SJ, Hanna PM, Mason RP (November 1994). "The metabolism of 17 beta-estradiol by lactoperoxidase: a possible source of oxidative stress in breast cancer". Carcinogenesis. 15 (11): 2637–43. doi:10.1093/carcin/15.11.2637. PMID   7955118.
  16. ↑ Jokumsen, KV, et al. (August 2024). "Elevated levels of iodide promote peroxidase-mediated protein iodination and inhibit protein chlorination". Free Radic Biol Med. 220: 207–221. doi: 10.1016/j.freeradbiomed.2024.04.230 . PMID   38663830.
  17. 1 2 3 Ghibaudi EM, Laurenti E, Beltramo P, Ferrari RP (2000). "Can estrogenic radicals, generated by lactoperoxidase, be involved in the molecular mechanism of breast carcinogenesis?". Redox Report. 5 (4): 229–35. doi: 10.1179/135100000101535672 . PMID   10994878. S2CID   24253204.
  18. ↑ Singh AK, Smith ML, Yamini S, Ohlsson PI, Sinha M, Kaur P, et al. (October 2012). "Bovine carbonyl lactoperoxidase structure at 2.0Å resolution and infrared spectra as a function of pH". The Protein Journal. 31 (7): 598–608. doi:10.1007/s10930-012-9436-3. PMID   22886082. S2CID   22945713.
  19. ↑ PDB: 2r5l ​; Singh AK, Singh N, Sharma S, Singh SB, Kaur P, Bhushan A, et al. (February 2008). "Crystal structure of lactoperoxidase at 2.4 A resolution". Journal of Molecular Biology. 376 (4): 1060–75. doi:10.1016/j.jmb.2007.12.012. PMID   18191143.
  20. 1 2 de Wit JN, van Hooydonk AC (1996). "Structure, functions and applications of lactoperoxidase in natural antimicrobial systems". Netherlands Milk & Dairy Journal. 50: 227–244.
  21. ↑ Wever R, Kast WM, Kasinoedin JH, Boelens R (December 1982). "The peroxidation of thiocyanate catalysed by myeloperoxidase and lactoperoxidase". Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 709 (2): 212–9. doi:10.1016/0167-4838(82)90463-0. PMID   6295491.
  22. ↑ Pruitt KM, Tenovuo J, Andrews RW, McKane T (February 1982). "Lactoperoxidase-catalyzed oxidation of thiocyanate: polarographic study of the oxidation products". Biochemistry. 21 (3): 562–7. doi:10.1021/bi00532a023. PMID   7066307.
  23. ↑ Furtmüller, PG, et al. (August 2002). "Reaction of Lactoperoxidase Compound I with Halides and Thiocyanate". Biochemistry. 41 (39): 11895–11900. doi:10.1021/bi026326x. PMID   12269834.
  24. ↑ Singh, Prashant K.; Ahmad, Nayeem; Yamini, Shavait; Singh, Rashmi P.; Singh, Amit K.; Sharma, Pradeep; Smith, Michael L.; Sharma, Sujata; Singh, Tej P. (2022). "Structural evidence of the oxidation of iodide ion into hyper-reactive hypoiodite ion by mammalian heme lactoperoxidase". Protein Science. 31 (2): 384–395. doi:10.1002/pro.4230. PMC   8819834 . PMID   34761444.
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  28. 1 2 Carlsson J, Edlund MB, Hänström L (June 1984). "Bactericidal and cytotoxic effects of hypothiocyanite-hydrogen peroxide mixtures". Infection and Immunity. 44 (3): 581–6. doi:10.1128/IAI.44.3.581-586.1984. PMC   263633 . PMID   6724690.
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  31. ↑ Harper WJ (2000). Biological properties of whey components a review. Chicago, IL: American Dairy Products Institute. p. 54.
  32. ↑ Poduslo JF, Braun PE (February 1975). "Topographical arrangement of membrane proteins in the intact myelin sheath. Lactoperoxidase incorporation of iodine into myelin surface proteins". The Journal of Biological Chemistry. 250 (3): 1099–105. doi: 10.1016/S0021-9258(19)41895-4 . PMID   1112791.
  33. ↑ Reiter B.; Härnulv BG. "The preservation of refrigerated and uncooled milk by its natural lactoperoxidase system". Dairy Ind. Int. 47 (5): 13–19.
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  35. ↑ Zajac M, Gladys J, Skarzynska M, Härnulv G, Björck L (December 1983). "Changes in Bacteriological Quality of Raw Milk Stabilized by Activation of its Lactoperoxidase System and Stored at Different Temperatures". Journal of Food Protection. 46 (12): 1065–1068. doi: 10.4315/0362-028x-46.12.1065 . PMID   30921865.
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  37. ↑ Marks NE, Grandison AS, Lewis MJ (2008). "Use of hydrogen peroxide detection strips to determine the extent of pasteurization in whole milk". International Journal of Dairy Technology. 54 (1): 20–22. doi:10.1046/j.1471-0307.2001.00008.x.
  38. ↑ WOapplication WO1988002600,Poulson OM,"Enzyme-containing bactericidal composition, and dental and wound treatment preparations comprising this composition",published 1988-04-21
  39. ↑ Hoogedoorn H (1985). "Activation of the salivary peroxidase system: clinical studies". In Tenovuo JO, Pruitt KM (eds.). The Lactoperoxidase system: chemistry and biological significance. New York: Dekker. pp. 217–228. ISBN   978-0-8247-7298-7.
  40. ↑ US 5607681,Galley E, Godfrey DC, Guthrie WG, Hodgkinson DM, Linnington HL,"Antimicrobial Compositions Containing Iodide, Thiocyanate, Glucose And Glucose Oxidase",published 1997-03-04, assigned to The Boots Company PLC
  41. ↑ Stanislawski M, Rousseau V, Goavec M, Ito H (October 1989). "Immunotoxins containing glucose oxidase and lactoperoxidase with tumoricidal properties: in vitro killing effectiveness in a mouse plasmacytoma cell model". Cancer Research. 49 (20): 5497–504. PMID   2790777.
  42. ↑ Lefkowitz DL, Hsieh TC, Mills K, Castro A (1990). "Induction of tumor necrosis factor and cytotoxicity by macrophages exposed to lactoperoxidase and microperoxidase". Life Sciences. 47 (8): 703–9. doi:10.1016/0024-3205(90)90625-2. PMID   2402192.
  43. ↑ Yamakaze J, Lu, Z (2021). "Deletion of the lactoperoxidase gene causes multisystem inflammation and tumors in mice". Scientific Reports. 11 (1): 12429. doi:10.1038/s41598-021-91745-8. PMC   8203638 . PMID   34127712.
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  58. ↑ Tenovuo JO (1985). "Biochemistry of Peroxidase System: Antimicrobial Effects". In Tenovuo JO, Pruitt KM (eds.). The Lactoperoxidase system: chemistry and biological significance. New York: Dekker. p. 272. ISBN   978-0-8247-7298-7.
  59. ↑ Haukioja A, Ihalin R, Loimaranta V, Lenander M, Tenovuo J (September 2004). "Sensitivity of Helicobacter pylori to an innate defence mechanism, the lactoperoxidase system, in buffer and in human whole saliva". Journal of Medical Microbiology. 53 (Pt 9): 855–860. doi: 10.1099/jmm.0.45548-0 . PMID   15314191.
  60. ↑ Thomas EL, Milligan TW, Joyner RE, Jefferson MM (February 1994). "Antibacterial activity of hydrogen peroxide and the lactoperoxidase-hydrogen peroxide-thiocyanate system against oral streptococci". Infection and Immunity. 62 (2): 529–35. doi:10.1128/IAI.62.2.529-535.1994. PMC   186138 . PMID   8300211.
  61. ↑ Løvstad RA (December 2006). "A kinetic study on the lactoperoxidase catalyzed oxidation of estrogens". Biometals. 19 (6): 587–92. doi:10.1007/s10534-006-0002-3. PMID   16944280. S2CID   19254664.
  62. ↑ Gorlewska-Roberts KM, Teitel CH, Lay JO, Roberts DW, Kadlubar FF (December 2004). "Lactoperoxidase-catalyzed activation of carcinogenic aromatic and heterocyclic amines". Chemical Research in Toxicology. 17 (12): 1659–66. doi:10.1021/tx049787n. PMID   15606142.
  63. ↑ Hugoson A, Koch G, Thilander H, Hoogendoorn H (1974). "Lactoperoxidase in the prevention of plaque accumulation, gingivitis and dental caries. 3. Effect of mouthrinses with amyloglucosidase and glucoseoxidase in the model system of experimental gingivitis and caries in man". Odontologisk Revy. 25 (1): 69–80. PMID   4522423.
  64. ↑ Midda M, Cooksey MW (November 1986). "Clinical uses of an enzyme-containing dentifrice". Journal of Clinical Periodontology. 13 (10): 950–6. doi:10.1111/j.1600-051x.1986.tb01433.x. PMID   3098804.
  65. ↑ Hannig C, Spitzmüller B, Lux HC, Altenburger M, Al-Ahmad A, Hannig M (July 2010). "Efficacy of enzymatic toothpastes for immobilisation of protective enzymes in the in situ pellicle". Archives of Oral Biology. 55 (7): 463–9. doi:10.1016/j.archoralbio.2010.03.020. PMID   20417500.
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