Healthy Multifunctional Spectra of Milk Glycoproteins and Their Fragments - a Review Article

Open access

Healthy Multifunctional Spectra of Milk Glycoproteins and Their Fragments - a Review Article

The functionalities of glycoprotein lactoferrin (LF) and glycomacropeptide (GMP) were discussed. LF is considered a multifunctional protein. Its absorption in the bowel; immune response; antioxidant, anti-carcinogenic and anti-inflammatory properties; and protection against microbial infection, were the most widely studied functions to date. Besides, promotion of balanced intestinal flora by preventing growth of harmful bacteria and stimulating bifidus, LF helps to secure a correct balance of the intestinal flora. Although, most of the proposed biological activities of LF are related to the binding of iron, the non-iron related functions have been described as well, such as regulation of iron metabolism, prevention of oxidation and control of cell or tissues damage (result of aging).

Likewise, GMP, which is a carbohydrate-containing peptide formed from chymosin or pepsin digestion of κ-casein, exhibits several useful biological activities, including binding of cholera toxin and E. coli enterotoxins, inhibition of bacterial and viral adhesions, suppression of gastric secretions, promotion of bifidobacterial growth, and modulation of immune responses. GMP contains no aromatic amino acids and is therefore used for phenylketonuria (PKU) suffering patients.

The carbohydratic parts bound to such glycoprotein or glycopeptide, may act as prebiotics in the intestine and colon.

If the inline PDF is not rendering correctly, you can download the PDF file here.

  • Abe H. Saito H. Miyakawa H. Tamura Y. Shimamura S. Nagao E. Tomita M. Heat stability of bovine lactoferrin at acidic pH. J. Dairy Sci. 1991 74 65-71.

  • Adlerova L. Bartoskova A. Faldyna M. Lactoferrin: a review. Veterinarni Medicina 2008 53 457-468.

  • Ajello M. Greco R. Giansanti F. Massucci M.T. Antonini G. Valenti P. Anti-invasive activity of bovine lactoferrin towards group A streptococci. Biochem. Cell Biol. 2002 80 119-124.

  • Aleinik S.I. Stan E.Y. Chernikov M.P. Study of the mechanism of acid secretion inhibition with κ-casein peptides in the stomach. Fiziologicheskii Zhurnal SSSR 1986 72 799-803.

  • Andres M.T. Fierro J.F. Antimicrobial mechanism of action of transferrins: Selective inhibition of H+-ATPase. Antimicrob. Agents Chemother. 2010 54 4335-4342.

  • Andersen J.H. Osbakk S.A. Vorland L.H. Traavik T. Gutteberg T.J. Lactoferrin and cyclic lactoferricin inhibit the entry of human cytomegalovirus into human fibroblasts. Antiviral Res. 2001 51141-149.

  • Anonymous Overview of lactoferrin. Agro Food Industry Hi-Tech. 2003 14 32-35.

  • Arnold R.R. Cole M.F. McGhee J.R. A bactericidal effect for human lactoferrin. Science 1977 197 263-265.

  • Azuma N. Yamauchi K. Mitsouka T. Bifidius growth-promoting activity of a glycomacropeptide derived from human κ-casein. Agric. Biol. Chem. 1984 48 2159-2162.

  • Baker E.N. Baker H.M. Molecular structure binding properties and dynamics of lactoferrin. Cell. Mol. Life Sci. 2005 62 2531-2539.

  • Batish V.K. Chander H. Zumdegeni K.C. et al. Antibacterial activity of lactoferrin against some common food-borne pathogenic organisms. Aust. J. Dairy Tech. 1988 43 16-18.

  • Baveye S. Elass E. Mazurier J. Spik G. Legrand D. Lactoferrin: a multifunctional glycoprotein involved in the modulation of the inflammatory process. Clin. Chem. Lab. Med. 1999 37 281-286.

  • Bellamy W. Takase M. Wakabayashi H. Kawase K. Tomita M. Identification of the bactericidal domain of lactoferrin. Biochim. Biophys. Acta 1992 1121 130-136.

  • Bessler H.C. de Oliveira I.R. Giugliano L.G. Human milk glycoproteins inhibit the adherence of Salmonella typhimurium to HeLa cells. Microbiol. Immunol. 2006 50 877-882.

  • Beucher S. Levenez F. Yvon M. Corring T. Effect of gastric digestive products from casein on CCK release by intestinal cells in rat. J. Nutr. Biochem. 1994a 5 578-584.

  • Beucher S. Levenez F. Yvon M. Corring T. Effect of caseinomacropeptide (CMP) on cholecystokinin (CCK) release in rat. Reprod. Nutr. Dev. 1994b 34 613-614.

  • Bezkorovainy A. Grolich D. Nichols J.H. Isolation of a glycopolypeptide fraction with Lactobacillus bifidus subspecies pennsylvanicus growth-promoting activity from whole human milk casein. Am. Clin. Nutr. 1979 32 1428-1432.

  • Birgens H.S. Lactoferrin in plasma measured by an ELISA technique: evidence that plasma lactoferrin is an indicator of neutrophil turnover and bone marrow activity in acute leukemia. Scand. J. Haematol. 1985 34 326-331.

  • Bortner C.A. Arnold R.R. Miller R.D. Bactericidal effect of lactoferrin on Legionella pneumophila: effect of the physiological state of the organism. Can. J. Microbiol. 1989 35 1048-1051.

  • Boxer L.A. Coates T.D. Haak R.A. Wolach J.B. Hoffstein S. Baehner R.L. Lactoferrin deficiency associated with altered granulocyte function. New Engl. J. Med. 1982 307 404-410.

  • Breton-Gorius J. Mason D.Y. Buriot D. et al. Lactoferrin deficiency as a consequence of a lack of specific granules in neutrophils from a patient with recurrent infections. Detection by immunoperoxidase staining for lactoferrin and cytochemical electron microscopy. Am. J. Pathol. 1980 99 413-428.

  • Brody E.P. Biological activities of bovine glycomacropeptide. Br. J. Nutr. 2000 84 S39-S46.

  • Brock J.H. Human cytokines. 1998 in: Handbook for Basic and Clinical Research. Vol. 3. (ed. B.B. Aggarwal). Blackwell Publ. Inc. Malden Mass. pp. 92-123.

  • Brock J.H. The physiology of lactoferrin. Biochem. Cell Biol. 2002 80 1-6.

  • Bruck W.M. Graverholt G. Gibson G.R. A two-stage continuous culture system to study the effect of supplemental alphalactalbumin and glycomacropeptide on mixed cultures of human gut bacteria challenged with enteropathogenic Escherichia coli and Salmonella serotype typhimurium. J. Appl. Microbiol. 2003a 95 44-53.

  • Bruck W.M. Kelleher S.L. Gibson G.R. Nielsen K.E. Chatterton D.E. Lönnerdal B. rRNA probes used to quantify the effects of glycomacropeptide and alpha-lactalbumin supplementation on the predominant groups of intestinal bacteria of infant rhesus monkeys challenged with enteropathogenic Escherichia coli. J. Pediatr. Gastroenterol. Nutr. 2003b 37 273-280.

  • Bruck W.M. Redgrave M. Tuohy K.M. Lönnerdal B. Graverholt G. Hernell O. Gibson G.R. Effects of bovine alpha-lactalbumin and casein glycomacropeptide-enriched infant formulae on faecal microbiota in healthy term infants. J. Pediatr. Gastroenterol. Nutr. 2006 43 673-679.

  • Caradonna L. Amati L. Lella P. Jirillo E. Caccavo D. Phagocytosis killing lymphocyte-mediated antibacterial activity serum autoantibodies and plasma endotoxins in inflammatory bowel disease. Am. J. Gastroeneterol. 2000 95 1495-1502.

  • Cirioni O. Giacometti A. Barchiesi F. Scalise G. Inhibition of growth of Pneumocystis carinii by lactoferrin alone and in combination with pyrimethamine clarithromycin and minocycline. J. Antimicrob. Chemother. 2000 46 577-582.

  • Clare R. The benefits of CMP. Dairy Industries Int. 1998 63 29-31.

  • Daddaoua A. Puerta V. Zarzuelo A. Sua'rez M.D. Sa'nchez de Medina F. Martinez-Augustin O. Bovine glycomacropeptide is anti-inflammatory in rats with Hapten-induced colitis. J. Nutr. 2005 135 1164-1170.

  • Damiens E. El Yazidi I. Mazurier J. Duthille I. Spik G. Boilly-Marer Y. Lactoferrin inhibits G1 cyclin-dependent kinases during growth arrest of human breast carcinoma cell. J. Cell Biochem. 1999 74 486-498.

  • Damiens E. Mazurier J. El Yazidi I. Masson M. Duthille I. Spik G. Boilly-Marer Y. Effects of human lactoferrin on NK cell cytotoxicity against haematopoietic and epithelial tumour cell. Biochim. Biophys. Acta 1998 1402 277-287.

  • Darewicz M. Dziuba B. Minkiewicz P. Dziuba J. The preventive potential of milk and colostrum proteins and protein fragments. Food Rev. Int. 2011 27 357-388.

  • Devi A.S. Das M.R. Pandit M.W. Lactoferrin contains structural motifs of ribonuclease. Biochim. Biophys. Acta 1994 1205 275-281.

  • Dial E.J. Lichtenberger L.M. Effect of lactoferrin on Helicobacter felis induced gastritis. Biochem. Cell Biol. 2002 80 113-117.

  • Di Mario F. Aragona G. Dal Bo N. Cavestro G.M. Cavallaro L. Iori V. Comparato G. Leandro G. Pilotto A. Franzè A. Use of bovine lactoferrin for Helicobacter pylori eradication. Dig. Liver Dis. 2003 35 706-710.

  • Doi H. Ibuki F. Kanamori M. Hetrogeneneity of reduced bovine κ-casein. J. Dairy Sci. 1979 62 195-203.

  • Doi H. Kobatake H. Fumio I. Kanamori M. Attachment sites of carbohydrate portions to peptide chain of κ-casein from bovine colostrum. Agric. Biol. Chem. 1980 44 2605-2611.

  • Dosako S. Kusano H. Deya E. Idota T. Infectionprotectant. United States Patent 1992 5147853.

  • Egashira M. Takayanagi T. Moriuchi M. Moriuchi H. Does daily intake of bovine lactoferrin-containing products ameliorate rotaviral gastroenteritis?. Acta Paediatr. 2007 96 1242-1244.

  • Eigel W.N. Butler J.E. Ernstrom C.A. Farrell H.M. Harwalkar V.R. Jenness R. Whitney R.M. Nomenclature of proteins of cow's milk: fifth revision. J. Dairy Sci. 1984 67 1599-1631.

  • Farnaud S. Evans R.W. Lactoferrin - a multifunctional protein with antimicrobial properties. Mol. Immunol. 2003 40 395-405.

  • Farrell H.M. Jr. Jimenez-Flores R. Bleck G.T. Brown E.M. Butler J.E. Creamer L.K. Hicks C.L. Hollar C.M. Ng-Kwai-Hang K.F. Swaisgood H.E. Nomenclature of the proteins of cows' milk—Sixth revision. J. Dairy Sci. 2004 87 1641-1674.

  • Faure J.-C. Schellenberg D.A. Bexter A. Wuerzner H.P. Barrier effect of Bifidobacterium longum on a pathogenic Escherichia coli strain by gut colonization in the germ-free rat. Zeitschrift fur Ernahrungswissenschaft 1984 23 41-51.

  • Fayed A.E. Hussein G.A. El-Mahdy L.D. Masoud M.S. Gab-Allah R.H. Glycoprotein fortification of bioyoghurt. Egypt. J. Food Sci. 2011a 39 81-106.

  • Fayed A.E. Hussein G.A. El-Mahdy L.D. Youssef M.S. Gab-Allah R.H. Improvement of yoghurt efficiency as functional food by glycoprotein fortification. J. Biol. Chem. Environ. Sci. 2011b 6 241-265.

  • Fiat A.-M. Alais C. Jolles P. Caesin 25. The amino-acid and carbohydrate sequences of a short glycopeptide isolated from bovine κ-casein. Eur. J. Biochem. 1972 27 408-412.

  • Fiat A-M. Jolles P. Caseins of various origins and biologically active casein peptides and oligosaccharides: structural and physiological aspects. Mol. and Cell. Biochem. 1989 87 5-30.

  • Fiat A-M. Jolles J. Loucheux-Lefebvre M.-H. Alais C. Jolles P. Localization of the prosthetic sugar groups of bovine colostrum κ-casein. Hoppe-Seyler's Zeitschrift fur Physiologische Chem. 1981 362 1447-1454.

  • Fournet B. Fiat A.-M. Alais C. Jolles P. Cow κ-casein: structure of the carbohydrate portion. Biochim. Biophys. Acta 1979 576 339-346.

  • Fournet B. Fiat A.-M. Montreuil J. Jolles P. The sugar part of κ-caseins from cow milk and colostrum and its microheterogeneity. Biochimie 1975 57 161-165.

  • Furmanski P. Li Z.P. Fortuna M.B. Swamy C.V. Das M.R. 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 170 415-429.

  • Gahr M. Speer C.P. Damerau B. Sawatzki G. Influence of lactoferrin on the function of human polymorphonuclear leukocytes and monocytes. J. Leukoc. Biol. 1991 49 427-433.

  • Gasymov O.K. Abduragimov A.R. Yusifov T.N. Glasgow B.J. Interaction of tear lipocalin with lysozyme and lactoferrin. Biochem. Biophys. Res. Comm. 1999 265 322-325.

  • Gauthier S.F. Pouliot Y. Saint-Sauveur D. Immunomodulatory peptides obtained by the enzymatic hydrolysis of whey proteins. Int. Dairy J. 2006 16 1315-1323.

  • Giansanti F. Rossi P. Massucci M.T. Botti D. Valenti G. Seganti L. Antiviral activity of ovotransferrin discloses an evolutionary strategy for defensive activities of lactoferrin. Biochem. Cell Biol. 2002 80 125-130.

  • Gill H.S. Rutherford K.J. Cross M.L. Bovine milk: a unique source of immunomodulatory ingredients for functional foods. 2000 in: Functional Foods II - Claims and Evidence (eds. J. Buttriss M. Saltmarsh). Royal Society of Chemistry Press Cambridge England pp. 82-90.

  • Glasgow L.R. Hill R.L. Interaction of Mycoplasma gallisepticum with sialyl glycoproteins. Inf. Immun. 1980 30 353-361.

  • Gonzalez-Chavez S.A. Arevalo-Gallegos S. Rascon-Cruz Q. Lactoferrin: structure function and applications. Int. J. Antimicrob. Agents 2009 33 301e1-301e8.

  • Gray-Owen S.D. Schryvers A.B. Bacterial transferring and lactoferrin receptors. Trends Microbiol. 1996 4 185-191.

  • Griffiths C.E. Cumberbatch M. Tucker S.C. Dearman R.J. Andrew S. Headon D.R. Kimber I. Exogenous topical lactoferrin inhibits allergen-induced Langerhans cell migration and cutaneous inflammation in humans. Br. J. Dermatol. 2001 144 715-725.

  • Guillen C. McInnes I.B. Vaughan D. Speekenbrink A.B. Brock J.H. The effect of local administration of lactoferrin on inflammation in murine autoimmune and infectious arthritis. Arthritis Rheum. 2000 43 2073-2080.

  • Guilloteau P. Chayvialle J.A. Mendy F. Roger L. Toullec R. Bernard C. Mouats A. Faverdin P. Effect of caseinomacropeptide (CMP) on gastric secretion and plasma levels of digestive hormones in preruminant calves. Reprod. Nutr. Dev. 1987 27 287-288.

  • Guilloteau P. Huerou-Luron I. Chayviaille J.A. Toullec R. Legeas M. Bernard C. Roger L. Mendy F. Effect of caseinomacropeptide (CMP) on gastric secretion and plasma gut regulatory peptides in preruminant calves. Reprod. Nutr. Dev. 1994 34 612-613.

  • Gyorgy P. Jeanloz R.W. Hubertus N. Zilliken F. Undialyzable growth factors for Lactobacillus bifidus var. pennsylvanicus. Eur. J. Biochem. 1974 43 29-33.

  • Gyorgy P. Kuhn R. Rose C.S. Zilliken F. Bifidus factor. II. Its occurrence in milk from different species and in other natural products. Arch. Biochem. Biophys. 1954a 48 202-208.

  • Gyorgy P. Norris R.F. Rose C.S. Bifidus factor. I. A variant of Lactobacillus bifidus requiring a special growth factor. Arch. Biochem. Biophys. 1954b 48 193-201.

  • Holmgren J. Actions of cholera toxin and the prevention and treatment of cholera. Nature 1981 292 413-416.

  • Hutchens T.W. Henry J.F. Yip T.T. Hachey D.L. Schanler R.J. Motil K.J. Garza C. Origin of intact lactoferrin and its DNA-binding fragments found in the urine of human milk-fed preterm infants. Evaluation by stable isotopic enrichment. Pediatric Res. 1991 29 243-250.

  • Idota T. Sialylated compounds in human milk and their physiological significance in infants. Snow Brand R&D Reports 1996 106 1-55.

  • Iigo M. Kuhara T. Ushida Y. Moore M.A. Tsuda H. Inhibitory effects of bovine lactoferrin on colon carcinoma 26 lung metastasis in mice. Clin. Exp. Metastasis 1999 17 35-40.

  • Ikeda M. Nozaki A. Sugiyama K. Tanaka T. Naganuma A. Tanaka K Sekihara H. Shimotohno K. Saito M. Kato N. Characterization of antiviral of lactoferrin against hepatitis C virus infection in human cultured cells. Virus Res. 2000 66 51-63.

  • Ikeda M. Sugiyama K. Tanaka T. Lactoferrin markedly inhibits hepatitis C virus infection in cultured human hepatocytes. Biochem. Biophys. Res. Commun. 1998 245 549-553.

  • Imoto I. Okuda M. Nakazawa T. Miyashiro E. Yamauchi K. Takakura N. Teraguchi S. Tamura Y. Adachi Y. Suppressive effect of bovine lactoferrin against Helicobacter pylori. Milk Sci. 2004 53 288-290.

  • Isoda H. Kawasaki Y. Tanimoto M. Dosako S. Idota T. Use of compounds containing or binding sialic acid to neutralize bacterial toxins. Eur. Patent 1999 385112.

  • Jolles J. Schoentgen F. Alais C. Fiat A.M. Jolles P. Studies on the primary structure of cow κ-casein - Structural features of para-κ-casein; N-termianl sequence of κ-caseinoglycopeptide studied with a sequencer. Helv. Chim. Acta 1972 55 2872-2883.

  • Jones E.M. Smart A. Bloomberg G. Burgess G. Millar M.R. Lactoferricin a new antimicrobial peptide. J. Appl. Bacteriol. 1994 77 208-214.

  • Kanyshkova T.G. Buneva V.N. Nevinsky G.A. Lactoferrin and its biological functions. Biochemistry (Moscow) 2001 66 1-7.

  • Kawaguchi S. Hayashi T. Masano J. Okuyama K. Suzuki T. Kawase K. A study concerning the effect of lactoferrin-enriched infant formula on low birth weight infants. Periant. Med. 1989 19 557-562.

  • Kawasaki Y. Isoda H. Shinmoto H. Tanimoto M. Dosako S. Idota T. Nakajima I. Inhibition by κ-casein glycomacropeptide and lactoferrin of influenza virus hemaglutination. Biosci. Biotech. Biochem. 1993 57 1214-1215.

  • Kawasaki Y. Isoda H. Tanimoto M. Dosako S. Idota T. Ahiko K. Inhibition by lactoferrin and κ-casein glycomacropeptide of binding of cholera toxin to its receptor. Biosci. Biotech. Biochem. 1992 56 195-198.

  • Kehagias C. Jao Y.C. Micolajcik E.M. Hansen P.M. Growth response of Bifidobacterium bifidum to a hydrolytic product isolated from bovine casein. J. Food Sci. 1977 42 146-150.

  • Kelleher S.L. Chatterton D. Nielsen K. Lönnerdal B. Glycomacropeptide and α-lactalbumin supplementation of infant formula affects growth and nutritional status in infant rhesus monkeys. Am. J. Clin. Nutr. 2003 77 1261-1268.

  • Kim W. S. Ohashi M. Tanaka T. Kumura H. Kim G.Y. Kwon I.K. Goh J.S. Shimazaki K.I. Growth-promoting effects of lactoferrin on L. acidophilus and Bifidobacterium spp. Biometals 2004 17 279-283.

  • Korhonen H. Pihlanto A. Bioactive peptides: production and functionality. Int. Dairy J. 2006 16 945-690.

  • Kozu T. Saito Y. Matsuda T. Akasu T. Iinuma G. Ohashi Y. Saito D. Tsuda H. Iigo M. Kakizoe T. The efficacy of lactoferrin for suppression of colorectal adenomas. in: Proc. Sixty-fifth Ann. Meet. the Japan. Cancer Assoc. 2006 pp. 461

  • Kuwata H. Yamauchi K. Teraguchi S. Ushida Y. Shimo-Kawa Y. Toida T. Hayasawa H. Functional fragments of ingested lactoferrin are resistant to proteolytic degradation in the gastrointestinal tract of adult rats. J. Nutr. 2001 131 2121-2127.

  • LaBell F. Health-enhancing whey proteins. Prepared Foods 1998 167 143.

  • Lampreave F. Piňeiro A. Brock J.H. Castillo H. Sánchez L. Calvo M. Interaction of bovine lactoferrin with other proteins of milk whey. Int. J. Biol. Macromol. 1990 12 2-5.

  • Levay P.F. Viljoen M. Lactoferrin: a general review. Haematologica 1995 80 252-267.

  • Li E.W. Mine Y. Immunoenhancing effects of bovine glycomacropeptide and its derivatives on the proliferative response and phagocytic activities of human acrophagelike cells U937. J. Agric. Food Chem. 2004 52 2704-2708.

  • Lim K. Van Calcar S.C. Nelson K.L. Gleason S.T. Ney D.M. Acceptable low-phenylalanine foods and beverages can be made from glycomacropeptide from cheese whey for individuals with PKU. Mol. Genet. Metab. 2007 92 176-178.

  • Liukkonen J. Haataja S. Tikkanen K. Kelm S. Finne J. Identification of N-acetylneuraminyl a2-3 poly-N-acteyl lactosamine glycans as the receptors of sialic acid-binding Streptococcus suis strains. J. Biol. Chem. 1992 267 21105-21111.

  • Loomes L.M. Uemura K. Childs R.A. Paulson J.C. Rogers G.N. Scudder P.R. Michalski J.C. Housell E.F. Taylor-Robinson D. Feizi T. Erythrocyte receptors for Mycoplasma pneumoniae are silaylated oligosaccharides of II antigen type. Nature 1984 306 560-563.

  • Machnicki M. Zimecki M. Zagulski T. Lactoferrin regulates the release of tumour necrosis factor alpha and interleukin 6 in vivo. Int. J. Exp. Pathol. 1993 74 433-439.

  • Manso M.A. Lopez-Fandino R. κ-casein macropeptides from cheese whey: physicochemical biological nutritional and technological features for possible uses. Food Rev. Int. 2004 20 329-355.

  • Marshall K. Therapeutic applications of whey protein. Altern. Med. Rev. 2004 9 136-156.

  • Marshall S.C. Casein macropeptide from whey. A new product opportunity. Food Res. Quarterly 1991 51 86-91.

  • Masson P.L. Heremans J. Lactoferrin in milk from different species. Comp. Biochem. Physiol. 1971 39 119-129.

  • McAbee D.D. Esbensen K. Binding and endocytosis of apoand holo-lactoferrin by isolated rat hepatocytes. J. Biol. Chem. 1991 266 23624-23631.

  • McCormick J.A. Markey G.M. Morris T.C. Lactoferrin-inducible monocyte cytotoxicity for K562 cells and decay of natural killer lymphocyte cytotoxicity. Clin. Exp. Immunol. 1991 83 154-156.

  • Mencacci A. Cenci E. Boelaert J.R. Mosci P. d'Ostiani C.F. Bistoni F. Romani L. Iron overload alters innate and T helper cell responses to Candida albicans in mice. J. Infect. Dis. 1997 175 1467-1476.

  • Mikkelsen T.L. Rasmussen E. Olsen A. Barkhott V. Frøkiær H. Immunogenicity of κ-casein and glycomacropeptide. J. Dairy Sci. 2006 89 824-830.

  • Miyazawa K. Mantel C. Lu L. Morrison D.C. Broxmeyer H.E. Lactoferrin- lipopolysaccharide interactions. Effect on lactoferrin binding to monocyte/macrophage-differentiated HL-60 cells. J. Immunol. 1991 146 723-729.

  • Monnai M. Otani H. Effect of bovine κ-caseinoglycopeptide on secretion of interleukin-1 family cytokines by P388D1 cells a line derived from mouse monocyte/macrophage. Milchwissenschaft 1997 52 192-196.

  • Naidu A.S. Lactoferrin: Natural Multifunctional Antimicrobial. 2000 CRC Press LLC USA.

  • Nakajima K. Tamura N. Kobayashi-Hattori K. Yoshida T. Hara-Kudo Y. Ikedo M. Sugita-Konishi Y. Hattori M. Prevention of intestinal infection by glycomacropeptide. Biosci. Biotechnol. Biochem. 2005 69 2294-2301.

  • Neeser J.R. Anti-plaque and anticaries agent. United States Patent 1991a 4992420.

  • Neeser J.R. Anti-plaque and anticaries agent. United States Patent 1991b 4994441.

  • Neeser J.R. Chambaz A. Hoang K.Y. Link-Amster H. Screening for complex carbohydrates inhibiting hemaggluatinations by CFA/I- and CFA/II-expressing enterotoxigenic Escherichia coli strains. FEMS Microbiol. Letters 1988a 49 301-307.

  • Neeser J.R. Chambaz A. del Vedovo S.D. Prigent M.J. Guggenheim B. Specific and nonspecific inhibition of adhesion of oral actinomyces and streptococci to erythrocytes and polystrene by caseinoglycopeptide derivatives. Inf. Immun. 1988b 56 3201-3208.

  • Neeser J.R. Golliard M. Woltz A. Rouvet M. Dillmann M.L. Guggenheim B. In vitro modulation of oral bacterial adhesion to saliva-coated hydroxyapatite beads by milk casein derivatives. Oral Microbiol. Immunol. 1994 9 193-201.

  • Neeser J.R. Grafstrom R.C. Woltz A. Brassart D. Fryder V. Guggenheim B. A 23 kda membrane glycoprotein bearing NeuNacalpha2-3Gal beta1-3GalNAc O-linked carbohydrate chains acts as a receptor for Streptococcus sanguis OMZ 9 on human buccal epithelial cells. Glycobiology 1995 5 97-104.

  • Nejad A.S. Kanekanian A. Tatham A. The inhibitory effect of glycomacropeptide on dental erosion. Dairy Sci. Technol. 2009 89 233-239.

  • Ney D.M. Gleason S.T. Van Calcar S.C. Nutritional management of PKU with glycomacropeptide from cheese whey. J. Inherit. Metab. Dis. 2009 32 32-39.

  • Nielsen P. Tromholt N. Method for production of a kappacasein glycomacropeptide and use of a kappa-casein glycomacropeptide. World Patent 1994 9415952.

  • Nishiya K. Horwitz D.A. Contrasting effects of lactoferrin on human lymphocyte and monocyte natural killer activity and antibody-dependent cell-mediated cytotoxicity. J. Immunol. 1982 129 2519-2523.

  • Ofek I. Sharon N. Adhesins as lectins: specificity and role in infection. Curr. Topics Microbiol. Immunol. 1990 151 91-113.

  • Ohashi A. Murata E. Yamamoto K. Majima E. Sano E. Le Q.T. Katunuma N. New functions of lactoferrin and β-casein in mammalian milk as cysteine protease inhibitors. Biochem. Biophys. Res. Commun. 2003 306 98-103.

  • Okazaki K. Uchida K. Ohana M. Nakase H. Uose S. Inai M. Matsushima Y. Katamura K. Ohmori K. Chiba T. Autoimmune-related pancreatitis is associated with autoantibodies and a Th1/Th2-type cellular immune response. Gastroenterology 2000 118 573-581.

  • Okuda M. Nakazawa T. Yamauchi K. Miyashiro E. Koizumi R. Booka M. Teraguchi S. Tamura Y. Yoshikawa N. Adachi Y. Imoto I. Bovine lactoferrin is effective to suppress Helicobacter pylori colonization in the human stomach: a randomized double-blind placebo-controlled study. J. Infect. Chemother. 2005 11 265-269.

  • Omata Y. Satake M. Maeda R. Saito A. Shimazaki K. Yamauchi K. Uzuka Y. Tanabe S. Sarashina T. Mikami T. Reduction of the infectivity of Toxoplasma gondii and Eimeria stiedai sporozoites by treatment with bovine lactoferricin. J. Vet. Med. Sci. 2001 63 189-190.

  • Otani H. Hata I. Inhibition of proliferative responses of mouse spleen lymphocytes and rabbit Peyer's patch cells by bovine milk caseins and their digests. J. Dairy Res. 1995 62 339-348.

  • Otani H. Horimoto Y. Monnai M. Suppression of interleukin-2 receptor expression on mouse CD4(+) T cells by bovine κ-caseinoglycopeptide. Biosci. Biotechnol. Biochem. 1996 60 1017-1019.

  • Otani H. Monnai M. Inhibition of proliferative responses of mouse spleen lymphocytes by bovine milk κ-casein digests. Food Agri. Immunol. 1993 5 219-229.

  • Otani H. Monnai M. Induction of an interleuken-1receptor antagonist-like component produced from mouse GMP biological activities S45 spleen cells by bovine κ-caseinoglycopeptide. Biosci. Biotechnol. Biochem. 1995 59 1166-1168.

  • Otani H. Monnai M. Hosono A. Bovine κ-casein as inhibitor of the proliferation of mouse splenocytes induced by lipopoly-saccharide stimulation. Milchwissenschaft 1992 47 512-515.

  • Otani H Monnai M. Kawasaki Y. Kawakami H. Tanimoto M. Inhibition of mitogen-induced proliferative responses of lymphocytes by bovine κ-caseinoglycopeptides having different carbohydrate chains. J. Dairy Res. 1995 62 349-357.

  • Pan Y. Lee A. Wan J. Coventry M.J. Michalski W.P. Shiell B. Roginski H. Antiviral properties of milk proteins and peptides. Int. Dairy J. 2006 16 1252-1261.

  • Parkkinen A. Rogers G.N. Korhonen T. Dahr W. Finne J. Identification of the O-linked sialyloligosaccharides of glycophorin A as the erythrocyte receptors for S-fimbriated Escherichia coli. Inf. Immun. 1986 54 37-42.

  • Payne K.D. Davidson P.M. Oliver S.P. Influence of bovine lactoferrin on the growth of Listeria monocytogenes. J. Food Prot. 1990 53 468-472.

  • Petschow B.W. Talbott R.D. Response of Bifidobacterium species to growth promoters in human and cow milk. Pediatric Res. 1991 29 208-213.

  • Pierce A. Colavizza D. Benaissa M. Maes P. Tartar A. Montreul J. Spik G. Molecular cloning and sequence analysis of bovine lactotransferrin. Eur. J. Biochem. 1991 196 177-184.

  • Poch M. Bezkorovainy A. Growth-enhancing supplements for various species of the genus Bifidobacterium. J. Dairy Sci. 1988 71 3214-4221.

  • Poch M. Bezkorovainy A. Bovine milk κ-casein trypsin digest is a growth enhancer for the genus Bifidobacterium. J. Agri. Food Chem. 1991 39 73-77.

  • Powell W.L. Jazwinska E. Halliday J.W. Primary iron overload. 1994 in: Iron Metabolism in Health and Disease. 1st Ed. (eds. J.H. Brock J.W. Halliday M.J. Pippard L.W. Powell). pub. W.B. Saunders Co. London UK pp. 227-270.

  • Proulx M. Gauthier S.F. Roy D. Effect of casein hydrolysates on the growth of Bifidobacteria. Le Lait 1992 72 393-404.

  • Qiu J. Hendrixson D.R. Baker E.N. Murphy T.F. St Geme J.W. Plaut A.G. Human milk lactoferrin inactivates two putative colonization factors expressed by Haemophilus influenzae. Proc. Natl. Acad. Sci. U.S.A. 1998 95 12641-12646.

  • Reiter B. The biological significance of the non-immunoglobulin protective proteins in milk: lysozome lactoferrin lactoper-oxidase. Dev. Dairy Chem. 1985 3 281-336.

  • Roberts A.K. Chierici R. Sawatzki G. Hill M.J. Volpato S. Vigi V. Supplementation of an adapted formula with bovine lactoferrin: 1. Effect on the infant faecal flora. Acta Paediatr 1992 81 119-124.

  • Saito H. Miyakawa H. Tamura Y. Potent bactericidal activity of bovine lactoferrin hydrolysate produced by heat treatment at acidic pH. J. Dairy Sci. 1991 74 3724-3730.

  • Saito T. Itoh T. Variations and distributions of Oglycosidically linked sugar chains in bovine κ-casein. J. Dairy Sci. 1992 75 1768-1774.

  • Saito T. Itoh T. Adachi S. The chemical structure of a tetrasaccharide containing N-acetylglucosamine obtained from bovine colostrum κ-casein. Biochim. Biophys. Acta 1981 673 487-494.

  • Sawatzki G. Rich I.N. Lactoferrin stimulates colony stimulating factor production in vitro and in vivo. Blood Cells 1989 15 371-385.

  • Schengrund C.L. Ringler N.J. Binding of Vibrio cholera toxin and the heat-labile enterotoxin of Escherichia coli to GM1 derivatives of GM1 and nonlipid oligosaccharide polyvalent ligands. J. Biol. Chem. 1989 264 13233-13237.

  • Schupbach P. Neeser J.R. Golliard M. Rouvet M. Guggenheim B. Incorporation of caseinoglycomacropeptide and caseinophosphopeptide into the salivary pellicle inhibits adherence of mutans streptococci. J. Dental Res. 1996 75 1779-1788.

  • Sekine K. Murakoshi M. Satomi Y. Nishino H. Kakizoe T. Tsuda H. Inhibition of initiation and early stage development of aberrant crypt foci and enhanced natural killer activity in male rats administered bovine lactoferrin concomitantly with azoxymethane. Cancer Lett. 1997 121 211-216.

  • Shah N.P. Effects of milk-derived bioactives: an overview. Br. J. Nutr. 2000 84 S3-S10.

  • Shakibaei M. Frevert U. Dual interaction of the malaria circumsporozoite protein with the low density lipoprotein receptor-related protein (LRP) and heparin sulfate proteoglycans. J. Exp. Med. 1996 184 1699-1711.

  • Shin K. Wakabayashi H. Yamauchi K. Teraguchi S. Tamura Y. Kurokawa M. Shiraki K. Effects of orally administered bovine lactoferrin and lactoperoxidase on influenza virus infection in mice. J. Med. Microbiol. 2005 54 717-723.

  • Siciliano R. Rega B. Marchetti M. Seganti L. Antonini G. Valenti P. Bovine lactoferrin peptidic fragments involved in inhibition of herpes simplex virus type 1 infection. Biochem. Biophys. Res. Commun. 1999 264 19-23.

  • Simon P.M. Pharmaceutical oligosaccharides. Drug Discovery Today 1996 1 522-528.

  • Smithers G.W. Regester G.O. Bradford R.S. Pearce R.J. New casein protein products for the food industry: physical chemical and enzymatic manipulation of milk. Food Aust. 1991 43 252-254.

  • Sorrentino S. D'Alessandro A.M. Maras B. Ciccio L.D. D'Andrea G. De Prisco R. Bossa F. Libonati M. Oratore A. Purification of a 76-kDa iron-binding protein from human seminal plasma by affinity chromatography specific for ribonuclease: structural and functional identity with milk lactoferrin. Biochim. Biophys. Acta 1999 1430 103-110.

  • Stan E.Y. Chernikov M.P. On the physiological activity of κ-casein glycomacropeptide. Voprosy Meditsinskoi Khimii 1979 25 348-352.

  • Stan E.Y. Chernikov M.P. Formation of a peptide inhibitor of gastric secretion from rat milk proteins in vivo. Bull. Exp. Biol. Med. 1982 94 1087-1089.

  • Stan E.Y. Groisman S.D. Krasil'shchikov K.B. Chernikov M.P. Effects of κ-casein glycomacropeptide motility in dogs. Bull. Exp. Biol. Med. 1983 95 889-891.

  • Steijns J. Dietary proteins as the source of new health promoting bio-active peptides with special attention to glutamine peptide. Food Tech. Eur. 1996 3 80-84.

  • Steijns J.M. Van Hooijdonk A.C. Occurrence structure bio-chemical properties and technological characteristics of lactoferrin. Br. J. Nutr. 2000 84 S11-S17.

  • Strøm M.B. Haug B.E. Rekdal Ø. Skar M.L. Stensen W. Svendsen J.S. Important structural features of 15-residue lactoferrin derivatives and methods for improvement of antimicrobial activity. Biochem. Cell Biol. 2002 80 65-74.

  • Strøm M.B. Rekdal O. Svendsen J.S. Antibacterial activity of 15-residue lactoferricin derivatives. J. Peptide Res. 2000 56 265-274.

  • Sugii S. Tsuji T. Binding and hemagglutinating properties of the B Subunit(s) of heat-labile enterotoxin isolated from human enterotoxigenic Escherichia coli. FEMS Microbiol. Letters 1990 66 45-50.

  • Suzuki T. Yamauchi K. Kawase K. Collaborative bacteriostatic activity of bovine lactoferrin with lysozyme against E. coli O111. Agric. Biol. Chem. 1989 53 1705-1706.

  • Suzuki Y.A. Lopez V. Lonnerdal B. Mammalian lactoferrin receptors: structure and function. Cell. Molec. Life Sci. 2005 62 2560-2575.

  • Suzuki Y. Lonnerdal B. Characterization of mammalian receptors for lactoferrin. Biochem. Cell Biol. 2002 80 75-80.

  • Tachezy J. Kulda J. Bahnikova I. Suchan P. Razga J. Schrevel J. Tritrichomonas foetus: iron acquisition from lactoferrin and transferrin. Exp. Parasitol. 1996 83 216-228.

  • Tanaka K. Ikeda M. Nozaki A. Kato N. Tsuda H. Saito S. Sekihara H. Lactoferrin inhibits C virus viremia in patients with chronic hepatitis C: a pilot study. Jpn. J. Cancer Res. 1999 90 367-371.

  • Tanaka K. Kawabata K. Kohno H. Honjo S. Murakami M. Ota T. Tsuda H. Chemopreventive effect of bovine lactoferrin on 4-nitroquinoline 1-oxide induced tongue carcinogenesis in male F344 rats. Jpn. J. Cancer Res. 2000 91 25-33.

  • Teraguchi S. Ozawa K. Yasuda S. Shin K. Fukuwatari Y. Shimamura S. The bacteriostatic effects of orally administered bovine lactoferrin on intestinal Enterobacteriaceae of SPF mice fed bovine milk. Biosci. Biotechnol. Biochem. 1994 58 482-487.

  • Teraguchi S. Shin K. Ogata T. Kingaku M. Kaino A. Miyauchi H. Fukuwatari Y. Shimamura S. Orally administered bovine lactoferrin inhibits bacterial translocation in mice fed bovine milk. Appl. Environ. Microbiol. 1995 61 4131-4134.

  • Teraguchi S. Wakabayashi H. Kuwata H. Yamauchi K. Tamura Y. Protection against infection by oral lactoferrin: evaluation in animal models. Biometals 2004 17 231-234.

  • Tomita M. Wakabayashi H. Shin K. Yamauchi K. Yaeshima T. Iwatsuki K. Twenty-five years of research on bovine lactoferrin applications. Biochimie 2009 91 52-57

  • Tomita M. Wakabayashi H. Yamauchi K. Teraguchi S. Hayasawa H. Bovine lactoferrin and lactoferricin derived from milk: production and applications. Biochem. Cell Biol. 2002 80 109-112.

  • Trif M. Guillen C. Vaughan D.M. Telfer J.M. Brewer J.M. Roseanu A. Brock J.H. Liposomes as possible carriers for lactoferrin in the local treatment of inflammatory diseases. Exp. Biol. Med. 2001 226 559-564.

  • Tran V.D. Baker B.E. Casein IX. Carbohydrate moiety of κ-casein. J. Dairy Sci. 1970 53 1009-1012.

  • Tsuda H. Sekine K. Fujita K. Iigo M. Cancer prevention by bovine lactoferrin and underlying mechanisms - a review of experimental and clinical studies. Biochem. Cell Biol. 2002 80 131-136.

  • Ushida Y. Sekine K. Kuhara T. Takasuka N. Iigo M. Tsuda H. Inhibitory effects of bovine lactoferrin on intestinal polyposis in the Apc (Min) mouse. Cancer Lett. 1998 134 141-145.

  • Van Calcar S.C. MacLeod E.L. Gleason S.T. Etzel M.R. Clayton M.K. Wolff J.A. Ney D.M. Improved nutritional management of phenylketonuria by using a diet containing glycomacropeptide compared with amino acids. Am. J. Clin. Nutr. 2009 89 1068-1077.

  • Van Halbeek H. Dorland L. Vliegenthart J.F.G. Fiat A.M. Jolles P. A 360-MHz 1H-NMR study of three oligosaccharides isolated from cow κ-casein. Biochim. Biophys. Acta 1980 623 295-300.

  • Van Heyningen S. Cholera toxin: interaction of subunits with ganglioside GM1. Science 1974 183 656-657.

  • Van Hooijdonk A.C. Kussendrager K.D. Steijns J.M. In vivo antimicrobial and antiviral activity of components in bovine milk and colostrums involved in non-specific defence. Br. J. Nut. 2000 84 S127-S134.

  • Van Hooydonk A.C.M. Olieman C. Hagedoorn H.G. Kinetics of the chymosin-catalyzed proteolysis of κ-casein in milk. Neth. Milk Dairy J. 1984 38 207-222.

  • Van Snick J.L. Masson P.L. Heremans J.F. The involvement of lactoferrin in the hyposideremia of acute inflammation. J. Exp. Med. 1974 140 1068-1084.

  • Vasilevskaya L.S. Stan E.Y. Chernikov M.P. Shlygin G.K. Inhibitory action of glycomacropeptide produced on the gastric secretion by various humoral stimulants. Voprosy Pitaniya 1977 4 21-24.

  • Viejo-Diaz M. Andres M.T. Fierro J.F. Modulation of in vitro fungicidal activity of human lactoferrin against Candida albicans by extracellular cation concentration and target cell metabolic activity. Antimicrob. Agents Chemother. 2004 48 1242-1248.

  • Wakabayashi H. Kurokawa M. Shin K. Teraguchi S. Tamura Y. Shiraki K. Oral lactoferrin prevents body weight loss and increase cytokine responses during herpes simplex virus type 1 infection of mice. Biosci. Biotechnol. Biochem. 2004a 68 537-544.

  • Wakabayashi H. Kuwata H. Yamauchi K. Teraguchi S. Tamura Y. No detectable transfer of dietary lactoferrin or its functional fragments to portal blood in health adult rats. Biosci. Biotechnol. Biochem. 2004b 68 853-860.

  • Wakabayashi H. Uchida K. Yamauchi K. Teraguchi S. Hayasawa H. Yamaguchi H. Lactoferrin given in food facilitates dermatophytosis cure in guinea pig models. J. Antimicrob. Chemother. 2000 46 595-601.

  • Wakabayashi H. Yamauchi K. Takase M. Lactoferrin research technology and applications. Int. Dairy J. 2006 16 1241-1251.

  • Walzem R.L. Dillard C.J. German J.B. Whey components: millennia of evolution create functionalities for mammalian nutrition: what we know and what we may be overlooking. Crit Rev. Food Sci. Nut. 2002 42 353-375.

  • Wang X. Hirmo S. Willen R. Wadstrom T. Inhibition of Helicobacter pylori infection by bovine milk glycoconjugates in a BAlb/cA mouse model. J Med. Microbiol. 2001 50 430-435.

  • Ward P.P. Uribe-Luna S. Conneely O.M. Lactoferrin and host defense. Biochem. Cell Biol. 2002 80 95-102.

  • Weinberg E.D. Acquisition of iron and other nutrients in vivo. 1995 in: Virulence Mechanisms of Bacterial Pathogens 2nd ed. (eds. J. A. Roth C. A. Bolin K. A. Brogden F. C. Minion M.J. Wannemuehler). American Society for Microbiology Washington D.C. USA pp. 79-93.

  • Whitney R.M. Proteins in milk. 1988 in: Fundamentals of Dairy Chemistry (eds. N.P. Wong R. Jenness M. Keeney E.H. Marth). Van Nostrand Reinhold New York USA pp. 89-92.

  • Yakabe T. Kawakami H. Idota T. Growth simulation agent for bifidus and lactobacillus. Jpn. Patent 1994 7267866.

  • Yamada Y. Amagasaki T. Jacobsen D. W. Green R. Lactoferrin binding by leukemia cell lines. Blood 1987 70 264-270.

  • Yamauchi K. Biologically functional proteins of milk and peptides derived from milk proteins. Bull. Int. Dairy Fed. 1992 272 51-58.

  • Yamauchi K. Hiruma M. Yamazaki N. Wakabayashi H. Kuwata H. Teraguchi S. Hayasawa H. Suegara N. Yamaguchi H. Oral administration of bovine lactoferrin for treatment of tinea pedis. A placebo-controlled double-blind study. Mycoses 2000 43 197-202.

  • Yamauchi K. Tomita M. Giehl T.J. Ellison R.T. Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Inf. Immun. 1993 61 719-728.

  • Ye X.Y. Wang H.X. Liu F. Ng T.B. Ribonuclease cell-free translation-inhibitory and superoxide radical scavenging activities of the iron-binding protein lactoferrin from bovine milk. Int. J. Biochem. Cell. Biol. 2000 32 235-241.

  • Yoo Y.C. Watanabe R. Koike Y. Mitobe M. Shimazaki K. Watanabe S. Azuma I. Apoptosis in human leukemic cells induced by lactoferricin a bovine milk protein-derived peptide: involvement of reactive oxygen species. Biochem. Biophys. Res. Commun. 1997 237 624-628.

  • Yoo Y.C. Watanabe S. Watanabe R. Bovine lactoferrin and lactoferricin inhibit tumor metastasis in mice. Adv. Exp. Med Biol. 1998 443 285-291.

  • Yu R.H. Schryvers A.B. Bacterial lactoferrin receptors: insight from characterizing the Moraxella bovis receptors. Biochem. Cell Biol. 2002 80 81-90.

  • Yun S.S. Sugita-Konishi Y. Kumagai S. Yamauchi K. Glycomacropeptide from cheese whey protein concentrate enhances IgA production by lipopolysaccharide-stimulated murine spleen cells. Ann. Sci. Technol. 1996 67 458-462.

  • Yvon M. Beucher S. Guilloteau P. Huerou-Luron I.L. Corring T. Effects of caseinomacropeptide (CMP) on digestion regulation. Reprod. Nutr. Dev. 1994 34 527-537.

  • Zakharova E.T. Shavlovski M.M. Bass M.G. Gridasova A.A. Pulina M.O. De Filippis V. Beltramini M. Di Muro P. Salvato B. Fontana A. Vasilyev V.B. Gaitskhoki V.S. Interaction of lactoferrin with ceruloplasmin. Arch. Biochem. Biophys. 2000 374 222-228.

  • Zhang Y.P. Shapiro P. Fluoride free dental remineralization. World Patent 1998 9852524.

Search
Journal information
Impact Factor


IMPACT FACTOR 2017: 1.697
5-year IMPACT FACTOR: 1.760



CiteScore 2018: 1.92

SCImago Journal Rank (SJR) 2018: 0.621
Source Normalized Impact per Paper (SNIP) 2018: 0.908

Metrics
All Time Past Year Past 30 Days
Abstract Views 0 0 0
Full Text Views 265 57 0
PDF Downloads 129 61 3