메뉴 건너뛰기




Volumn 173, Issue , 2016, Pages S29-S36

Molecular Determinants of Milk Lactoferrin as a Bioactive Compound in Early Neurodevelopment and Cognition

Author keywords

BDNF Brain derived neurotrophic factor; bLF Bovine lactoferrin; CA Cornu ammonis; DEX Dexamethasone; HI Hypoxia ischemia; hLF Human lactoferrin; IUGR Intrauterine growth restriction; NCAM Neural cell adhesion molecule; polySia Polysialic acid; Sia Sialic acid

Indexed keywords

LACTOFERRIN; LTF PROTEIN, HUMAN;

EID: 84969969871     PISSN: 00223476     EISSN: 10976833     Source Type: Journal    
DOI: 10.1016/j.jpeds.2016.02.073     Document Type: Article
Times cited : (38)

References (66)
  • 1
    • 84866790269 scopus 로고    scopus 로고
    • Molecular mechanism underlying sialic acid as an essential nutrient for brain development and cognition
    • B. Wang Molecular mechanism underlying sialic acid as an essential nutrient for brain development and cognition Adv Nutr 3 2012 465S 472S
    • (2012) Adv Nutr , vol.3 , pp. 465S-472S
    • Wang, B.1
  • 2
    • 67749101393 scopus 로고    scopus 로고
    • Sialic acid is an essential nutrient for brain development and cognition
    • B. Wang Sialic acid is an essential nutrient for brain development and cognition Annu Rev Nutr 29 2009 177 222
    • (2009) Annu Rev Nutr , vol.29 , pp. 177-222
    • Wang, B.1
  • 3
    • 82355190918 scopus 로고    scopus 로고
    • The role of meta-analysis in the evaluation of the effects of early nutrition on mental and motor development in children
    • H. Szajewska The role of meta-analysis in the evaluation of the effects of early nutrition on mental and motor development in children Am J Clin Nutr 94 2011 1889S 1895S
    • (2011) Am J Clin Nutr , vol.94 , pp. 1889S-1895S
    • Szajewska, H.1
  • 4
    • 79951924700 scopus 로고    scopus 로고
    • Effects of maternal malnutrition and postnatal nutritional rehabilitation on brain fatty acids, learning, and memory
    • A.S. de Souza, F.S. Fernandes, and M. do Carmo Effects of maternal malnutrition and postnatal nutritional rehabilitation on brain fatty acids, learning, and memory Nutr Rev 69 2011 132 144
    • (2011) Nutr Rev , vol.69 , pp. 132-144
    • De Souza, A.S.1    Fernandes, F.S.2    Do Carmo, M.3
  • 5
    • 33846860608 scopus 로고    scopus 로고
    • Dietary sialic acid supplementation improves learning and memory in piglets
    • B. Wang, B. Yu, M. Karim, H. Hu, Y. Sun, P. McGreevy, and et al. Dietary sialic acid supplementation improves learning and memory in piglets Am J Clin Nutr 85 2007 561 569
    • (2007) Am J Clin Nutr , vol.85 , pp. 561-569
    • Wang, B.1    Yu, B.2    Karim, M.3    Hu, H.4    Sun, Y.5    McGreevy, P.6
  • 6
    • 0029126185 scopus 로고
    • Lactoferrin: A general review
    • P.F. Levay, and M. Viljoen Lactoferrin: a general review Haematologica 80 1995 252 267
    • (1995) Haematologica , vol.80 , pp. 252-267
    • Levay, P.F.1    Viljoen, M.2
  • 7
    • 69949124929 scopus 로고    scopus 로고
    • Interfacial adsorption and denaturization of human milk and recombinant rice lactoferrin
    • F. Pan, X. Zhao, T.A. Waigh, J.R. Lu, and F. Miano Interfacial adsorption and denaturization of human milk and recombinant rice lactoferrin Biointerphases 3 2008 FB36
    • (2008) Biointerphases , vol.3 , pp. FB36
    • Pan, F.1    Zhao, X.2    Waigh, T.A.3    Lu, J.R.4    Miano, F.5
  • 8
    • 0029130333 scopus 로고
    • Lactoferrin: Molecular structure and biological function
    • B. Lönnerdal, and S. Iyer Lactoferrin: molecular structure and biological function Annu Rev Nutr 15 1995 93 110
    • (1995) Annu Rev Nutr , vol.15 , pp. 93-110
    • Lönnerdal, B.1    Iyer, S.2
  • 10
    • 84861356856 scopus 로고    scopus 로고
    • A structural perspective on lactoferrin function
    • H.M. Baker, and E.N. Baker A structural perspective on lactoferrin function Biochem Cell Biol 90 2012 320 328
    • (2012) Biochem Cell Biol , vol.90 , pp. 320-328
    • Baker, H.M.1    Baker, E.N.2
  • 11
    • 84861361791 scopus 로고    scopus 로고
    • Lactoferrin, a bird's eye view
    • H.J. Vogel Lactoferrin, a bird's eye view Biochem Cell Biol 90 2012 233 244
    • (2012) Biochem Cell Biol , vol.90 , pp. 233-244
    • Vogel, H.J.1
  • 12
    • 82355169684 scopus 로고    scopus 로고
    • Bovine lactoferrin can be taken up by the human intestinal lactoferrin receptor and exert bioactivities
    • B. Lönnerdal, R. Jiang, and X. Du Bovine lactoferrin can be taken up by the human intestinal lactoferrin receptor and exert bioactivities J Pediatr Gastroenterol Nutr 53 2011 606 614
    • (2011) J Pediatr Gastroenterol Nutr , vol.53 , pp. 606-614
    • Lönnerdal, B.1    Jiang, R.2    Du, X.3
  • 13
    • 84937915817 scopus 로고
    • Heterogeneity of human Lactoferrin due to differences in sialic acid content
    • D.R. Wolfson, and J.B. Robbins Heterogeneity of human Lactoferrin due to differences in sialic acid content Pediatr Res 5 1971 514 517
    • (1971) Pediatr Res , vol.5 , pp. 514-517
    • Wolfson, D.R.1    Robbins, J.B.2
  • 14
    • 79951996840 scopus 로고    scopus 로고
    • Comprehensive characterization of the site-specific N-glycosylation of wild-type and recombinant human lactoferrin expressed in the milk of transgenic cloned cattle
    • T. Yu, C. Guo, J. Wang, P. Hao, S. Sui, X. Chen, and et al. Comprehensive characterization of the site-specific N-glycosylation of wild-type and recombinant human lactoferrin expressed in the milk of transgenic cloned cattle Glycobiology 21 2011 206 224
    • (2011) Glycobiology , vol.21 , pp. 206-224
    • Yu, T.1    Guo, C.2    Wang, J.3    Hao, P.4    Sui, S.5    Chen, X.6
  • 16
    • 0024119835 scopus 로고
    • Comparative study of the primary structures of sero-, lacto- and ovotransferrin glycans from different species
    • G. Spik, B. Coddeville, and J. Montreuil Comparative study of the primary structures of sero-, lacto- and ovotransferrin glycans from different species Biochimie 70 1988 1459 1469
    • (1988) Biochimie , vol.70 , pp. 1459-1469
    • Spik, G.1    Coddeville, B.2    Montreuil, J.3
  • 17
    • 84862141706 scopus 로고    scopus 로고
    • Glycosylation of human milk lactoferrin exhibits dynamic changes during early lactation enhancing its role in pathogenic bacteria-host interactions
    • M111.015248
    • M. Barboza, J. Pinzon, S. Wickramasinghe, J.W. Froehlich, I. Moeller, J.T. Smilowitz, and et al. Glycosylation of human milk lactoferrin exhibits dynamic changes during early lactation enhancing its role in pathogenic bacteria-host interactions Mol Cell Proteomics 11 2012 M111.015248
    • (2012) Mol Cell Proteomics , vol.11
    • Barboza, M.1    Pinzon, J.2    Wickramasinghe, S.3    Froehlich, J.W.4    Moeller, I.5    Smilowitz, J.T.6
  • 18
    • 0034076597 scopus 로고    scopus 로고
    • Analysis of intestinal flora development in breast-fed and formula-fed infants by using molecular identification and detection methods
    • H.J. Harmsen, A.C. Wildeboer-Veloo, G.C. Raangs, A.A. Wagendorp, N. Klijn, J.G. Bindels, and et al. Analysis of intestinal flora development in breast-fed and formula-fed infants by using molecular identification and detection methods J Pediatr Gastroenterol Nutr 30 2000 61 67
    • (2000) J Pediatr Gastroenterol Nutr , vol.30 , pp. 61-67
    • Harmsen, H.J.1    Wildeboer-Veloo, A.C.2    Raangs, G.C.3    Wagendorp, A.A.4    Klijn, N.5    Bindels, J.G.6
  • 19
    • 84902649333 scopus 로고    scopus 로고
    • Profiling temporal changes in bovine milk lactoferrin glycosylation using lectin microarrays
    • N. O'Riordan, J.Q. Gerlach, M. Kilcoyne, J. O'Callaghan, M. Kane, R.M. Hickey, and et al. Profiling temporal changes in bovine milk lactoferrin glycosylation using lectin microarrays Food Chem 165 2014 388 396
    • (2014) Food Chem , vol.165 , pp. 388-396
    • O'Riordan, N.1    Gerlach, J.Q.2    Kilcoyne, M.3    O'Callaghan, J.4    Kane, M.5    Hickey, R.M.6
  • 20
    • 0029810761 scopus 로고    scopus 로고
    • Heterogeneity in utilization of N-glycosylation sites Asn624 and Asn138 in human lactoferrin: A study with glycosylation-site mutants
    • P.H. van Berkel, H.A. van Veen, M.E. Geerts, H.A. de Boer, and J.H. Nuijens Heterogeneity in utilization of N-glycosylation sites Asn624 and Asn138 in human lactoferrin: a study with glycosylation-site mutants Biochem J 319 Pt 1 1996 117 122
    • (1996) Biochem J , vol.319 , pp. 117-122
    • Van Berkel, P.H.1    Van Veen, H.A.2    Geerts, M.E.3    De Boer, H.A.4    Nuijens, J.H.5
  • 21
    • 1342322699 scopus 로고    scopus 로고
    • The role of N-linked glycosylation in the protection of human and bovine lactoferrin against tryptic proteolysis
    • H.A. van Veen, M.E. Geerts, P.H. van Berkel, and J.H. Nuijens The role of N-linked glycosylation in the protection of human and bovine lactoferrin against tryptic proteolysis Eur J Biochem 271 2004 678 684
    • (2004) Eur J Biochem , vol.271 , pp. 678-684
    • Van Veen, H.A.1    Geerts, M.E.2    Van Berkel, P.H.3    Nuijens, J.H.4
  • 23
    • 0034303264 scopus 로고    scopus 로고
    • Separation of lactoferrin-A and -b from bovine colostrum
    • S. Yoshida, Z. Wei, Y. Shinmura, and N. Fukunaga Separation of lactoferrin-a and -b from bovine colostrum J Dairy Sci 83 2000 2211 2215
    • (2000) J Dairy Sci , vol.83 , pp. 2211-2215
    • Yoshida, S.1    Wei, Z.2    Shinmura, Y.3    Fukunaga, N.4
  • 24
    • 0034166581 scopus 로고    scopus 로고
    • Presence of a glycan at a potential N-glycosylation site, Asn-281, of bovine lactoferrin
    • Z. Wei, T. Nishimura, and S. Yoshida Presence of a glycan at a potential N-glycosylation site, Asn-281, of bovine lactoferrin J Dairy Sci 83 2000 683 689
    • (2000) J Dairy Sci , vol.83 , pp. 683-689
    • Wei, Z.1    Nishimura, T.2    Yoshida, S.3
  • 25
    • 68249103612 scopus 로고    scopus 로고
    • Core fucose and bisecting GlcNAc, the direct modifiers of the N-glycan core: Their functions and target proteins
    • M. Takahashi, Y. Kuroki, K. Ohtsubo, and N. Taniguchi Core fucose and bisecting GlcNAc, the direct modifiers of the N-glycan core: their functions and target proteins Carbohydr Res 344 2009 1387 1390
    • (2009) Carbohydr Res , vol.344 , pp. 1387-1390
    • Takahashi, M.1    Kuroki, Y.2    Ohtsubo, K.3    Taniguchi, N.4
  • 26
    • 77951225235 scopus 로고    scopus 로고
    • Human lactoferrin activates NF-kappaB through the Toll-like receptor 4 pathway while it interferes with the lipopolysaccharide-stimulated TLR4 signaling
    • K. Ando, K. Hasegawa, K. Shindo, T. Furusawa, T. Fujino, K. Kikugawa, and et al. Human lactoferrin activates NF-kappaB through the Toll-like receptor 4 pathway while it interferes with the lipopolysaccharide-stimulated TLR4 signaling FEBS J 277 2010 2051 2066
    • (2010) FEBS J , vol.277 , pp. 2051-2066
    • Ando, K.1    Hasegawa, K.2    Shindo, K.3    Furusawa, T.4    Fujino, T.5    Kikugawa, K.6
  • 27
    • 48149090000 scopus 로고    scopus 로고
    • Sialic acids in human health and disease
    • A. Varki Sialic acids in human health and disease Trends Mol Med 14 2008 351 360
    • (2008) Trends Mol Med , vol.14 , pp. 351-360
    • Varki, A.1
  • 28
    • 0027318961 scopus 로고
    • Biological roles of oligosaccharides: All of the theories are correct
    • A. Varki Biological roles of oligosaccharides: all of the theories are correct Glycobiology 3 1993 97 130
    • (1993) Glycobiology , vol.3 , pp. 97-130
    • Varki, A.1
  • 29
    • 85007875098 scopus 로고
    • Inhibitory effects of milk gangliosides on the adhesion of Escherichia coli to human intestinal carcinoma cells
    • T. Idota, and H. Kawakami Inhibitory effects of milk gangliosides on the adhesion of Escherichia coli to human intestinal carcinoma cells Biosci Biotechnol Biochem 59 1995 69 72
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 69-72
    • Idota, T.1    Kawakami, H.2
  • 31
    • 79958699963 scopus 로고    scopus 로고
    • Lactoferrin in relation to biological functions and applications: A review
    • M.M. El-Loly, and B. Mahfouz Lactoferrin in relation to biological functions and applications: a review Int J Dairy Sci 6 2011 97 111
    • (2011) Int J Dairy Sci , vol.6 , pp. 97-111
    • El-Loly, M.M.1    Mahfouz, B.2
  • 32
    • 0015225776 scopus 로고
    • Lactoferrin in milk from different species
    • P.L. Masson, and J.F. Heremans Lactoferrin in milk from different species Comp Biochem Physiol B 39 1971 119 129
    • (1971) Comp Biochem Physiol B , vol.39 , pp. 119-129
    • Masson, P.L.1    Heremans, J.F.2
  • 34
    • 0037901694 scopus 로고    scopus 로고
    • Nutritional and physiologic significance of human milk proteins
    • B. Lönnerdal Nutritional and physiologic significance of human milk proteins Am J Clin Nutr 77 2003 1537S 1543S
    • (2003) Am J Clin Nutr , vol.77 , pp. 1537S-1543S
    • Lönnerdal, B.1
  • 35
    • 0026341232 scopus 로고
    • Structurally intact (78-kDa) forms of maternal lactoferrin purified from urine of preterm infants fed human milk: Identification of a trypsin-like proteolytic cleavage event in vivo that does not result in fragment dissociation
    • T.W. Hutchens, J.F. Henry, and T.T. Yip Structurally intact (78-kDa) forms of maternal lactoferrin purified from urine of preterm infants fed human milk: identification of a trypsin-like proteolytic cleavage event in vivo that does not result in fragment dissociation Proc Natl Acad Sci U S A 88 1991 2994 2998
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 2994-2998
    • Hutchens, T.W.1    Henry, J.F.2    Yip, T.T.3
  • 36
    • 0028650374 scopus 로고
    • Maternal lactoferrin in the urine of preterm infants. Evidence for retention of structure and function
    • R.D. Knapp, and T.W. Hutchens Maternal lactoferrin in the urine of preterm infants. Evidence for retention of structure and function Adv Exp Med Biol 357 1994 177 181
    • (1994) Adv Exp Med Biol , vol.357 , pp. 177-181
    • Knapp, R.D.1    Hutchens, T.W.2
  • 37
    • 0024405628 scopus 로고
    • Gastric luminal digestion of lactoferrin and transferrin by preterm infants
    • J.R. Britton, and O. Koldovsky Gastric luminal digestion of lactoferrin and transferrin by preterm infants Early Hum Dev 19 1989 127 135
    • (1989) Early Hum Dev , vol.19 , pp. 127-135
    • Britton, J.R.1    Koldovsky, O.2
  • 38
    • 0019949535 scopus 로고
    • Characterization and properties of the human and bovine lactotransferrins extracted from the faeces of newborn infants
    • G. Spik, B. Brunet, C. Mazurier-Dehaine, G. Fontaine, and J. Montreuil Characterization and properties of the human and bovine lactotransferrins extracted from the faeces of newborn infants Acta Paediatr Scand 71 1982 979 985
    • (1982) Acta Paediatr Scand , vol.71 , pp. 979-985
    • Spik, G.1    Brunet, B.2    Mazurier-Dehaine, C.3    Fontaine, G.4    Montreuil, J.5
  • 39
    • 0023200493 scopus 로고
    • Persistence of human milk proteins in the breast-fed infant
    • L.A. Davidson, and B. Lönnerdal Persistence of human milk proteins in the breast-fed infant Acta Paediatr Scand 76 1987 733 740
    • (1987) Acta Paediatr Scand , vol.76 , pp. 733-740
    • Davidson, L.A.1    Lönnerdal, B.2
  • 40
    • 0022470744 scopus 로고
    • Enhanced fecal excretion of selected immune factors in very low birth weight infants fed fortified human milk
    • R.J. Schanler, R.M. Goldblum, C. Garza, and A.S. Goldman Enhanced fecal excretion of selected immune factors in very low birth weight infants fed fortified human milk Pediatr Res 20 1986 711 715
    • (1986) Pediatr Res , vol.20 , pp. 711-715
    • Schanler, R.J.1    Goldblum, R.M.2    Garza, C.3    Goldman, A.S.4
  • 42
    • 0034894840 scopus 로고    scopus 로고
    • Gastric digestion of bovine lactoferrin in vivo in adults
    • F.J. Troost, J. Steijns, W.H. Saris, and R.J. Brummer Gastric digestion of bovine lactoferrin in vivo in adults J Nutr 131 2001 2101 2104
    • (2001) J Nutr , vol.131 , pp. 2101-2104
    • Troost, F.J.1    Steijns, J.2    Saris, W.H.3    Brummer, R.J.4
  • 43
    • 34748837915 scopus 로고    scopus 로고
    • Cloning of a pig homologue of the human lactoferrin receptor: Expression and localization during intestinal maturation in piglets
    • Y. Liao, V. Lopez, T.B. Shafizadeh, C.H. Halsted, and B. Lönnerdal Cloning of a pig homologue of the human lactoferrin receptor: expression and localization during intestinal maturation in piglets Comp Biochem Physiol A Mol Integr Physiol 148 2007 584 590
    • (2007) Comp Biochem Physiol A Mol Integr Physiol , vol.148 , pp. 584-590
    • Liao, Y.1    Lopez, V.2    Shafizadeh, T.B.3    Halsted, C.H.4    Lönnerdal, B.5
  • 44
    • 84861386961 scopus 로고    scopus 로고
    • The multifunctional glycolytic protein glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a novel macrophage lactoferrin receptor
    • P. Rawat, S. Kumar, N. Sheokand, C.I. Raje, and M. Raje The multifunctional glycolytic protein glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a novel macrophage lactoferrin receptor Biochem Cell Biol 90 2012 329 338
    • (2012) Biochem Cell Biol , vol.90 , pp. 329-338
    • Rawat, P.1    Kumar, S.2    Sheokand, N.3    Raje, C.I.4    Raje, M.5
  • 46
    • 78649907781 scopus 로고    scopus 로고
    • Cognitive testing of pigs (Sus scrofa) in translational biobehavioral research
    • B.R. Kornum, and G.M. Knudsen Cognitive testing of pigs (Sus scrofa) in translational biobehavioral research Neurosci Biobehav Rev 35 2011 437 451
    • (2011) Neurosci Biobehav Rev , vol.35 , pp. 437-451
    • Kornum, B.R.1    Knudsen, G.M.2
  • 48
    • 0029008633 scopus 로고
    • Polysialylation as a regulator of neural plasticity in rodent learning and aging
    • C.M. Regan, and G.B. Fox Polysialylation as a regulator of neural plasticity in rodent learning and aging Neurochem Res 20 1995 593 598
    • (1995) Neurochem Res , vol.20 , pp. 593-598
    • Regan, C.M.1    Fox, G.B.2
  • 49
    • 0037313166 scopus 로고    scopus 로고
    • Iron deficiency anemia in infancy: Long-lasting effects on auditory and visual system functioning
    • C. Algarin, P. Peirano, M. Garrido, F. Pizarro, and B. Lozoff Iron deficiency anemia in infancy: long-lasting effects on auditory and visual system functioning Pediatr Res 53 2003 217 223
    • (2003) Pediatr Res , vol.53 , pp. 217-223
    • Algarin, C.1    Peirano, P.2    Garrido, M.3    Pizarro, F.4    Lozoff, B.5
  • 50
    • 33750368838 scopus 로고    scopus 로고
    • Iron deficiency in infancy predicts altered serum prolactin response 10 years later
    • B. Felt, E. Jimenez, J. Smith, A. Calatroni, N. Kaciroti, G. Wheatcroft, and et al. Iron deficiency in infancy predicts altered serum prolactin response 10 years later Pediatr Res 60 2006 513 517
    • (2006) Pediatr Res , vol.60 , pp. 513-517
    • Felt, B.1    Jimenez, E.2    Smith, J.3    Calatroni, A.4    Kaciroti, N.5    Wheatcroft, G.6
  • 51
    • 33750213273 scopus 로고    scopus 로고
    • Double burden of iron deficiency in infancy and low socioeconomic status: A longitudinal analysis of cognitive test scores to age 19 years
    • B. Lozoff, E. Jimenez, and J.B. Smith Double burden of iron deficiency in infancy and low socioeconomic status: a longitudinal analysis of cognitive test scores to age 19 years Arch Pediatr Adolesc Med 160 2006 1108 1113
    • (2006) Arch Pediatr Adolesc Med , vol.160 , pp. 1108-1113
    • Lozoff, B.1    Jimenez, E.2    Smith, J.B.3
  • 52
    • 33745502924 scopus 로고    scopus 로고
    • Long-lasting neural and behavioral effects of iron deficiency in infancy
    • discussion S72-91
    • B. Lozoff, J. Beard, J. Connor, F. Barbara, M. Georgieff, and T. Schallert Long-lasting neural and behavioral effects of iron deficiency in infancy Nutr Rev 64 2006 S34 S43 discussion S72-91
    • (2006) Nutr Rev , vol.64 , pp. S34-S43
    • Lozoff, B.1    Beard, J.2    Connor, J.3    Barbara, F.4    Georgieff, M.5    Schallert, T.6
  • 53
    • 84937950414 scopus 로고    scopus 로고
    • Lactoferrin promotes early neurodevelopment and cognition in postnatal piglets by upregulating the BDNF signaling pathway and polysialylation
    • Y. Chen, Z. Zheng, X. Zhu, Y. Shi, D. Tian, F. Zhao, and et al. Lactoferrin promotes early neurodevelopment and cognition in postnatal piglets by upregulating the BDNF signaling pathway and polysialylation Mol Neurobiol 52 2015 256 269
    • (2015) Mol Neurobiol , vol.52 , pp. 256-269
    • Chen, Y.1    Zheng, Z.2    Zhu, X.3    Shi, Y.4    Tian, D.5    Zhao, F.6
  • 55
    • 0037762690 scopus 로고    scopus 로고
    • Neurotrophins and their receptors: A convergence point for many signalling pathways
    • M.V. Chao Neurotrophins and their receptors: a convergence point for many signalling pathways Nat Rev Neurosci 4 2003 299 309
    • (2003) Nat Rev Neurosci , vol.4 , pp. 299-309
    • Chao, M.V.1
  • 56
    • 58549090329 scopus 로고    scopus 로고
    • The molecular and cellular biology of enhanced cognition
    • Y.S. Lee, and A.J. Silva The molecular and cellular biology of enhanced cognition Nat Rev Neurosci 10 2009 126 140
    • (2009) Nat Rev Neurosci , vol.10 , pp. 126-140
    • Lee, Y.S.1    Silva, A.J.2
  • 57
    • 38349144906 scopus 로고    scopus 로고
    • Impact of the polysialyltransferases ST8SiaII and ST8SiaIV on polysialic acid synthesis during postnatal mouse brain development
    • I. Oltmann-Norden, S.P. Galuska, H. Hildebrandt, R. Geyer, R. Gerardy-Schahn, H. Geyer, and et al. Impact of the polysialyltransferases ST8SiaII and ST8SiaIV on polysialic acid synthesis during postnatal mouse brain development J Biol Chem 283 2008 1463 1471
    • (2008) J Biol Chem , vol.283 , pp. 1463-1471
    • Oltmann-Norden, I.1    Galuska, S.P.2    Hildebrandt, H.3    Geyer, R.4    Gerardy-Schahn, R.5    Geyer, H.6
  • 58
    • 57049188226 scopus 로고    scopus 로고
    • Direct binding of polysialic acid to a brain-derived neurotrophic factor depends on the degree of polymerization
    • Y. Kanato, K. Kitajima, and C. Sato Direct binding of polysialic acid to a brain-derived neurotrophic factor depends on the degree of polymerization Glycobiology 18 2008 1044 1053
    • (2008) Glycobiology , vol.18 , pp. 1044-1053
    • Kanato, Y.1    Kitajima, K.2    Sato, C.3
  • 59
    • 84856713410 scopus 로고    scopus 로고
    • Novel regulation of fibroblast growth factor 2 (FGF2)-mediated cell growth by polysialic acid
    • S. Ono, M. Hane, K. Kitajima, and C. Sato Novel regulation of fibroblast growth factor 2 (FGF2)-mediated cell growth by polysialic acid J Biol Chem 287 2012 3710 3722
    • (2012) J Biol Chem , vol.287 , pp. 3710-3722
    • Ono, S.1    Hane, M.2    Kitajima, K.3    Sato, C.4
  • 60
    • 84893254174 scopus 로고    scopus 로고
    • Protective effects of maternal nutritional supplementation with lactoferrin on growth and brain metabolism
    • E. Somm, P. Larvaron, Y. van de Looij, A. Toulotte, A. Chatagner, M. Faure, and et al. Protective effects of maternal nutritional supplementation with lactoferrin on growth and brain metabolism Pediatr Res 75 2014 51 61
    • (2014) Pediatr Res , vol.75 , pp. 51-61
    • Somm, E.1    Larvaron, P.2    Van De Looij, Y.3    Toulotte, A.4    Chatagner, A.5    Faure, M.6
  • 61
    • 84920273699 scopus 로고    scopus 로고
    • Behavioral effects of bovine lactoferrin administration during postnatal development of rats
    • J. Shumake, D.W. Barrett, M.A. Lane, and A.J. Wittke Behavioral effects of bovine lactoferrin administration during postnatal development of rats Biometals 27 2014 1039 1055
    • (2014) Biometals , vol.27 , pp. 1039-1055
    • Shumake, J.1    Barrett, D.W.2    Lane, M.A.3    Wittke, A.J.4
  • 62
    • 84888878250 scopus 로고    scopus 로고
    • The iron-binding protein lactoferrin protects vulnerable dopamine neurons from degeneration by preserving mitochondrial calcium homeostasis
    • E. Rousseau, P.P. Michel, and E.C. Hirsch The iron-binding protein lactoferrin protects vulnerable dopamine neurons from degeneration by preserving mitochondrial calcium homeostasis Mol Pharmacol 84 2013 888 898
    • (2013) Mol Pharmacol , vol.84 , pp. 888-898
    • Rousseau, E.1    Michel, P.P.2    Hirsch, E.C.3
  • 64
    • 7744231642 scopus 로고    scopus 로고
    • Suppressive effects of milk-derived lactoferrin on psychological stress in adult rats
    • N. Kamemori, T. Takeuchi, K. Hayashida, and E. Harada Suppressive effects of milk-derived lactoferrin on psychological stress in adult rats Brain Res 1029 2004 34 40
    • (2004) Brain Res , vol.1029 , pp. 34-40
    • Kamemori, N.1    Takeuchi, T.2    Hayashida, K.3    Harada, E.4
  • 65
    • 70349501374 scopus 로고    scopus 로고
    • Neuroprotection in a 6-hydroxydopamine-lesioned Parkinson model using lactoferrin-modified nanoparticles
    • R. Huang, L. Han, J. Li, F. Ren, W. Ke, C. Jiang, and et al. Neuroprotection in a 6-hydroxydopamine-lesioned Parkinson model using lactoferrin-modified nanoparticles J Gene Med 11 2009 754 763
    • (2009) J Gene Med , vol.11 , pp. 754-763
    • Huang, R.1    Han, L.2    Li, J.3    Ren, F.4    Ke, W.5    Jiang, C.6
  • 66
    • 42149092521 scopus 로고    scopus 로고
    • Trans-endothelial and trans-epithelial transfer of lactoferrin into the brain through BBB and BCSFB in adult rats
    • N. Kamemori, T. Takeuchi, A. Sugiyama, M. Miyabayashi, H. Kitagawa, H. Shimizu, and et al. Trans-endothelial and trans-epithelial transfer of lactoferrin into the brain through BBB and BCSFB in adult rats J Vet Med Sci 70 2008 313 315
    • (2008) J Vet Med Sci , vol.70 , pp. 313-315
    • Kamemori, N.1    Takeuchi, T.2    Sugiyama, A.3    Miyabayashi, M.4    Kitagawa, H.5    Shimizu, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.