Rys historyczny wiedzy o laktoferynie

• Autorzy: Jamka Małgorzata

Warianty tytułu

EN

Historical overview on knowledge about lactoferrin

• Języki publikacji: PL

Abstrakty

PL

Laktoferyna jest glikoproteiną z rodziny transferryn, która została po raz pierwszy odkryta w mleku krowim w 1939 r. Pomimo krótkiej historii, jaką posiada laktoferyna, ma ona obecnie szerokie zastosowane w profilaktyce i terapii wielu schorzeń. Od momentu wyizolowania laktoferyny z mleka, opisanych zostało wiele właściwości tego białka, takich jak: działanie przeciwbakteryjne, przeciwwirusowe, przeciwgrzybicze, przeciwpasożytnicze, przeciwnowotworowe, immunomodulujące,przeciwzapalne i inne. Co więcej, nadal trwają badania mające na celu poznanie nowych właściwości laktoferyny. W niniejszej pracy opisano historię odkrycia i badań nad laktoferyną oraz omówiono budowę i funkcje tego niezwykłego białka

EN

Lactoferrin is a glycoprotein of the transferrin family that was first discovered in bovine milk in 1939. Despite the short history of research on lactoferrin, this protein is now widely used in the preventionand treatment of many diseases. Since the isolation of lactoferrin from bovine milk, a numberof different properties of this protein have been described in the literature, e.g. antibacterial, antiviral,antifungal, antiparasitic, antineoplastic, immunomodulatory, anti-inflammatory and many other activities. Moreover, new researches aimed at finding the other properties of lactoferrin are still being conducted. This paper describes the history of discovery and research on lactoferrin and discusses the structure and functions of this extraordinary protein.

Słowa kluczowe

PL

białka mleka,; laktoferyna,; historia mleka

EN

milk proteins,; lactoferrin,; history of milk

• Wydawca: Uniwersytet Medyczny w Poznaniu
• Czasopismo: Acta Medicorum Polonorum
• Rocznik: 2017
• Tom: 7
• Numer: 2
• Strony: 44-53

Daty

otrzymano

2017-11-18

zaakceptowano

2017-12-10

wydrukowano

2017-12-28

Twórcy

autor

Jamka Małgorzata

• Klinika Gastroenterologii Dziecięcej i Chorób Metabolicznych, Uniwersytet Medyczny im. K. Marcinkowskiego w Poznaniu

Bibliografia

• Anderson B. F., Baker H. M., Dodson E. J. i in., Structure of human lactoferrin at 3.2-A resolution, “Proc Natl Acad Sci USA” 1987, s. 1769-1773
• Ando K., Hasegawa K., Shindo K. i in., Human lactoferrin activates NF-κB through the Toll-like receptor 4 pathway while it interferes with the lipopolysaccharide-stimulated TLR4 signaling, “FEBS J” 2010, s. 2051-2066. doi: 10.1111/j.1742-4658.2010.07620.x
• Artym J., Laktoferyna – niezwykłe białko, Warszawa 2016
• Artym J., Złoty środek na otyłość? Udział laktoferyny w metabolizmue glukozy i lipidów, “Postepy Hig Med Dosw” 2012, s. 937-953
• Bellamy W., Takase M., Yamauchi K. i in., Identification of the bactericidal domain of lactoferrin, “Biochim Biophys Acta” 1992, s. 130-136
• Berlutti F., Pantanella F., Natalizi T. i in., Antiviral properties of lactoferrin – a natural immunity molecule, “Molecules” 2011, s. 6992-7018. doi: 10.3390/molecules16086992
• Birgens H. S. i in., Receptor binding of lactoferrin by human monocytes, “Br J Haematol” 1983, s. 383-391
• Bullen J. J., Rogers H. J., Leigh L., Iron-binding proteins in milk and resistance to Escherichia coli infection in infants, “Br Med J” 1972, s. 69-75
• Dziennik Urzędowy Unii Europejskiej, 2012, L 327/52-L 327/54
• Dial E. J., Hall L. R., Serna H. i in., Antibiotic properties of bovine lactoferrin on Helicobacter pylori, “Dig Dis Sci” 1998, s. 2750-2756
• Fillebeen C., Dexter D., Mitchell V. i in., Lactoferrin is synthesized by mouse brain tissue and its expression is enhanced after MPTP treatment, “Adv Exp Med Biol” 1998, s. 293-300
• Furmanski P., Li Z. P., Fortuna M. B. i in., Multiple molecular forms of human lactoferrin. Identification of a class of lactoferrins that possess ribonuclease activity and lack iron-binding capacity, “J Exp Med” 1989, s. 415-429
• Groves M. L., The isolation of a red protein from milk, “J Am Chem Soc” 1960, s. 3345-3350. doi: 10.1021/ja01498a029
• Hwang S.-A., Kruzel M. L., Actor J. K., Lactoferrin augments BCG vaccine efficacy to generate T helper response and subsequent protection against challenge with virulent Mycobacterium tuberculosis, “Int Immunopharmacol” 2005, s. 591-599. doi: 10.1016/j.intimp.2004.11.006
• Johanson B., Isolation of an iron-containing red protein from human milk, “Acta Chem Scand” 1960, s. 510-512. doi: 10.3891/acta.chem.scand.14-0510
• Keijser S., Jager M. J., Dogterom-Ballering H. C. M. i in., Lactoferrin Glu561Asp polymorphism is associated with susceptibility to herpes simplex keratitis, “Exp Eye Res” 2008, s. 105-109. doi: 10.1016/j.exer.2007.09.013
• Kim W.-S., Ohashi M., Tanaka T. i in., Growth-promoting effects of lactoferrin on L. acidophilus and Bifidobacterium spp, “Biometals” 2004, s. 279-283
• Kirkpatrick C. H. i in., Inhibition of growth of Candida albicans by iron-unsaturated lactoferrin: relation to host-defense mechanisms in chronic mucocutaneous candidiasis, “J Infect Dis” 1971, s. 539-544
• Kuwata H., Yip T. T., Yip C. L. i in., Direct detection and quantitative determination of bovine lactoferricin and lactoferrin fragments in human gastric contents by affinity mass spectrometry, “Adv Exp Med Biol” 1998, s. 23-32
• Legrand D., Elass E., Pierce A. i in., Lactoferrin and host defence: an overview of its immuno-modulating and anti-inflammatory properties, “Biometals” 2004, s. 225-229
• Małaczewska J., Rotkiewicz Z., Laktoferyna – białko multipotencjalne, “Medycyna Wet” 2007, s. 136-139.
• Mann D. M., Romm E., Migliorini M., Delineation of the glycosaminoglycan-binding site in the human inflammatory response protein lactoferrin, “J Biol Chem” 1994, s. 23661-23667
• Masson P. L. i in., Immunohistochemical localization and bacteriostatic properties of an iron-binding protein from bronchial mucus, “Thorax” 1966, s. 538-544
• McAbee D. D., Jiang X., Walsh K. B., Lactoferrin binding to the rat asialoglycoprotein receptor requires the receptor’s lectin properties, “Biochem J.” 2000, s. 113-117.
• Meilinger M., Haumer M., Szakmary K. i in., Removal of lactoferrin from plasma is mediated by binding to low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor and transport to endosomes, “FEBS Lett” 1995, s. 70-74
• Metz-Boutigue M. H., Jollès J., Mazurier J. i in., Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins, “Eur J Biochem” 1984, s. 659-676
• Montreuil J., Tonnelat J., Mullet S., Preparation and properties of lactosiderophilin (lactotransferrin) of human milk, “Biochim Biophys Acta” 1960, s. 413-421
• Moore S. A., Anderson B. F., Groom C. R. i in., Three-dimensional structure of diferric bovine lactoferrin at 2.8 Å resolution, “J Mol Biol” 1997, s. 222-236. doi: 10.1006/jmbi.1997.1386
• Moreno-Navarrete J. M., Ortega F. J., Bassols J. i in., Association of circulating lactoferrin concentration and 2 nonsynonymous LTF gene polymorphisms with dyslipidemia in men depends on glucose-tolerance status, “Clin Chem” 2008, s. 301-309. doi: 10.1373/clinchem.2007.095943
• Rado T. A., Wei X. P., Benz E. J., Isolation of lactoferrin cDNA from a human myeloid library and expression of mRNA during normal and leukemic myelopoiesis, “Blood” 1987, s. 989-993
• Schwerin M., Solinas Toldo S., Eggen A. i in., The bovine lactoferrin gene (LTF) maps to chromosome 22 and syntenic group U12, “Mamm Genome” 1994, s. 486-489
• Sipponen T., Björkesten C.-G. A., Färkkilä M. i in., Faecal calprotectin and lactoferrin are reliable surrogate markers of endoscopic response during Crohn’s disease treatment, “Scand J Gastroenterol” 2010, s. 325-331. doi: 10.3109/00365520903483650
• Siqueiros-Cendón T., Arévalo-Gallegos S., Iglesias-Figueroa B.F. i in., Immunomodulatory effects of lactoferrin, “Acta Pharmacol Sin” 2014, s. 557-566. doi: 10.1038/aps.2013.200
• Sørensen M., Sørensen S. P. L., The proteins in whey, “Compt Rend Lab Carlsberg” 1939, s. 55-99
• Suzuki Y. A., Shin K., Lönnerdal B., Molecular cloning and functional expression of a human intestinal lactoferrin receptor, “Biochemistry” 2001, s. 15771-15779
• Takayama Y., Aoki R., Roles of lactoferrin on skin wound healing, “Biochem Cell Biol” 2012, s. 497-503. doi: 10.1139/o11-054
• Teng C. T., Pentecost B. T., Marshall A. i in., Assignment of the lactotransferrin gene to human chromosome 3 and to mouse chromosome 9, “Somat Cell Mol Genet” 1987, s. 689-693
• Teraguchi S., Ozawa K., Yasuda S. i in., The bacteriostatic effects of orally administered bovine lactoferrin on intestinal Enterobacteriaceae of SPF mice fed bovine milk, “Biosci Biotech Biochem” 1994, s. 482-487
• van der Kraan M. I., Groenink J., Nazmi K. i in., Lactoferrampin: a novel antimicrobial peptide in the N1-domain of bovine lactoferrin, “Peptide” 2004, s. 177-183. doi: 10.1016/j.peptides.2003.12.006
• van Snick J. L., Masson P. L., The binding of human lactoferrin to mouse peritoneal cells, “J Exp Med” 1976, s. 1568-1580
• Velliyagounder K., Kaplan J. B., Furgan D. i in., One of two human lactoferrin variants exhibits increased antibacterial and transcriptional activation activities and is associated with localized juvenile periodontitis, “Infect Immun” 2003, s. 6141-6147
• Ward P. P. i in., Iron status in mice carrying a targeted disruption of lactoferrin, “Mol Cell Biol” 2003, s. 178-185
• Włodarski K. H., Galus R., Brodzikowska A. i in., Znaczenie laktoferyny w regeneracji kości, „Pol Merkur Lekarski” 2013, s. 65-67
• Yoo Y. C., Watanabe S., Watanabe R. i in., Bovine lactoferrin and lactoferricin inhibit tumor metastasis in mice, “Adv Exp Med Biol” 1998, s. 285-291
• Zander Z., Zander L., Mickiewicz D., Laktoferyna – multipotencjalne białko mleka, “Innowacyjne Mleczarstwo” 2014, s. 18-21
• Zarember K. A., Cruz A. R., Huang C.-Y. i in., Antifungal activities of natural and synthetic iron chelators alone and in combination with azole and polyene antibiotics against Aspergillus fumigatus, “Antimicrob Agents Chemother” 2009, s. 2654-2656. doi: 10.1128/AAC.01547-08
• Zielinska-Blizniewska H., Sitarek P., Milonski J. i in., Association of the -33C/G OSF-2 and the 140A/G LF gene polymorphisms with the risk of chronic rhinosinusitis with nasal polyps in a Polish population, “Mol Biol Rep” 2012, s. 5449-5457. doi: 10.1007/s11033-011-1345-6