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Volumn 281, Issue 12, 2014, Pages 2871-2882

Structure of the iron-free true C-terminal half of bovine lactoferrin produced by tryptic digestion and its functional significance in the gut

Author keywords

apo C lobe; crystal structure; lactoferrin; open conformation; trypsin digestion

Indexed keywords

IRON; LACTOFERRIN;

EID: 84903641852     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12827     Document Type: Article
Times cited : (12)

References (47)
  • 2
    • 0024389662 scopus 로고
    • Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8 Å resolution
    • Anderson BF, Baker HM, Norris GE, Rice DW, &, Baker EN, (1989) Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8 Å resolution. J Mol Biol 209, 711-734.
    • (1989) J Mol Biol , vol.209 , pp. 711-734
    • Anderson, B.F.1    Baker, H.M.2    Norris, G.E.3    Rice, D.W.4    Baker, E.N.5
  • 3
    • 0025674182 scopus 로고
    • CDNA and protein sequence of bovine lactoferrin
    • Mead PE, &, Tweedie JW, (1990) cDNA and protein sequence of bovine lactoferrin. Nucleic Acid Res 18, 7167.
    • (1990) Nucleic Acid Res , vol.18 , pp. 7167
    • Mead, P.E.1    Tweedie, J.W.2
  • 4
    • 0033231125 scopus 로고    scopus 로고
    • Structure of buffalo lactoferrin at 2.5 Å resolution using crystals grown at 303 K shows different orientations of the N and C lobes
    • Karthikeyan S, Paramasivam M, Yadav S, Srinivasan A, &, Singh TP, (1999) Structure of buffalo lactoferrin at 2.5 Å resolution using crystals grown at 303 K shows different orientations of the N and C lobes. Acta Crystallogr D 55, 1805-1813.
    • (1999) Acta Crystallogr D , vol.55 , pp. 1805-1813
    • Karthikeyan, S.1    Paramasivam, M.2    Yadav, S.3    Srinivasan, A.4    Singh, T.P.5
  • 5
    • 0030719461 scopus 로고    scopus 로고
    • Three-dimensional structure of diferric bovine lactoferrin at 2.8 Å resolution
    • Moore SA, Anderson BF, Groom CR, Haridas M, &, Baker EN, (1997) Three-dimensional structure of diferric bovine lactoferrin at 2.8 Å resolution. J Mol Biol 274, 222-236.
    • (1997) J Mol Biol , vol.274 , pp. 222-236
    • Moore, S.A.1    Anderson, B.F.2    Groom, C.R.3    Haridas, M.4    Baker, E.N.5
  • 6
    • 0009665799 scopus 로고
    • An iron-binding protein common to many external secretions
    • Masson PL, Heremans JF, &, Dive C, (1966) An iron-binding protein common to many external secretions. Clin Chim Acta 14, 735-739.
    • (1966) Clin Chim Acta , vol.14 , pp. 735-739
    • Masson, P.L.1    Heremans, J.F.2    Dive, C.3
  • 7
    • 0037981263 scopus 로고    scopus 로고
    • Lactoferrin concentrations in milk from normal and subclinical mastitic cows
    • Hagiwara S, Kawai K, Anri A, &, Nagahata H, (2003) Lactoferrin concentrations in milk from normal and subclinical mastitic cows. J Vet Med Sci 65, 319-323.
    • (2003) J Vet Med Sci , vol.65 , pp. 319-323
    • Hagiwara, S.1    Kawai, K.2    Anri, A.3    Nagahata, H.4
  • 8
    • 0016254525 scopus 로고
    • Tear lactoferrin: A bacteriostatic and complexing protein
    • Broekhuyse RM, (1974) Tear lactoferrin: a bacteriostatic and complexing protein. Invest Ophthalmol 13, 550-554.
    • (1974) Invest Ophthalmol , vol.13 , pp. 550-554
    • Broekhuyse, R.M.1
  • 9
    • 0023231398 scopus 로고
    • Secretion of antimicrobial proteins from the parotid glands of different aged healthy persons
    • Fox PC, Heft MW, Herrera M, Bowers MR, Mandel ID, &, Baum BJ, (1987) Secretion of antimicrobial proteins from the parotid glands of different aged healthy persons. J Gerontol 42, 466-469.
    • (1987) J Gerontol , vol.42 , pp. 466-469
    • Fox, P.C.1    Heft, M.W.2    Herrera, M.3    Bowers, M.R.4    Mandel, I.D.5    Baum, B.J.6
  • 11
    • 0014747557 scopus 로고
    • Association of lactoferrin with specific granules in rabbit heterophil leukocytes
    • Baggiolini M, De Duve C, Masson PL, &, Heremans JF, (1970) Association of lactoferrin with specific granules in rabbit heterophil leukocytes. J Exp Med 131, 559-570.
    • (1970) J Exp Med , vol.131 , pp. 559-570
    • Baggiolini, M.1    De Duve, C.2    Masson, P.L.3    Heremans, J.F.4
  • 12
    • 0017389761 scopus 로고
    • A bactericidal effect for human lactoferrin
    • Arnold RR, Cole MF, &, McGhee JR, (1977) A bactericidal effect for human lactoferrin. Science 197, 263-265.
    • (1977) Science , vol.197 , pp. 263-265
    • Arnold, R.R.1    Cole, M.F.2    McGhee, J.R.3
  • 13
    • 0015168183 scopus 로고
    • Inhibition of growth of Candida albicans by iron-unsaturated lactoferrin: Relation to host-defense mechanisms in chronic mucocutaneous candidiasis
    • Kirkpatrick CH, Green I, Rich RR, &, Schade AL, (1971) Inhibition of growth of Candida albicans by iron-unsaturated lactoferrin: relation to host-defense mechanisms in chronic mucocutaneous candidiasis. J Infect Dis 124, 539-544.
    • (1971) J Infect Dis , vol.124 , pp. 539-544
    • Kirkpatrick, C.H.1    Green, I.2    Rich, R.R.3    Schade, A.L.4
  • 17
    • 84879191482 scopus 로고    scopus 로고
    • Antimicrobial lactoferrin peptides: The hidden players in the protective function of a multifunctional protein
    • Sinha M, Kaushik S, Kaur P, Sharma S, &, Singh TP, (2013) Antimicrobial lactoferrin peptides: the hidden players in the protective function of a multifunctional protein. Int J Peptide. 2013, 390230.
    • (2013) Int J Peptide , vol.2013 , pp. 390230
    • Sinha, M.1    Kaushik, S.2    Kaur, P.3    Sharma, S.4    Singh, T.P.5
  • 18
    • 0020674602 scopus 로고
    • Immunoradiometric assay of plasma lactoferrin
    • Brown RD, Rickard KA, &, Kronenberg H, (1983) Immunoradiometric assay of plasma lactoferrin. Pathology 15, 27-31.
    • (1983) Pathology , vol.15 , pp. 27-31
    • Brown, R.D.1    Rickard, K.A.2    Kronenberg, H.3
  • 19
    • 0021983545 scopus 로고
    • Lactoferrin in plasma measured by an ELISA technique
    • Birgens HS, (1985) Lactoferrin in plasma measured by an ELISA technique. Scand J Haemat 34, 326-331.
    • (1985) Scand J Haemat , vol.34 , pp. 326-331
    • Birgens, H.S.1
  • 20
    • 0034062292 scopus 로고    scopus 로고
    • Expression of lactoferrin in the kidney: Implications for innate immunity and iron metabolism
    • Abrink M, Larsson E, Gobl A, &, Hellman L, (2000) Expression of lactoferrin in the kidney: implications for innate immunity and iron metabolism. Kidney Int 57, 2004-2010.
    • (2000) Kidney Int , vol.57 , pp. 2004-2010
    • Abrink, M.1    Larsson, E.2    Gobl, A.3    Hellman, L.4
  • 21
    • 33845683946 scopus 로고    scopus 로고
    • Serum lactoferrin and immunoglobulin G concentrations in healthy or ill neonatal foals and healthy adult horses
    • Barton MH, Hurley D, Norton N, Heusner G, Costa L, Jones S, Byars D, &, Watanabe K, (2006) Serum lactoferrin and immunoglobulin G concentrations in healthy or ill neonatal foals and healthy adult horses. J Vet Intern Med 20, 1457-1462.
    • (2006) J Vet Intern Med , vol.20 , pp. 1457-1462
    • Barton, M.H.1    Hurley, D.2    Norton, N.3    Heusner, G.4    Costa, L.5    Jones, S.6    Byars, D.7    Watanabe, K.8
  • 22
    • 28444462150 scopus 로고    scopus 로고
    • Lactoferrin: A modulator of immune and inflammatory responses
    • Legrand D, Elass E, Carpentier M, &, Mazurier J, (2005) Lactoferrin: a modulator of immune and inflammatory responses. Cell Mol Life Sci 62, 2549-2559.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2549-2559
    • Legrand, D.1    Elass, E.2    Carpentier, M.3    Mazurier, J.4
  • 23
    • 0035827177 scopus 로고    scopus 로고
    • Camel lactoferrin, a transferrin-cum-lactoferrin: Crystal structure of camel apolactoferrin at 2.6 Å resolution and structural basis of its dual role
    • Khan JA, Kumar P, Paramasivam M, Yadav RS, Sahani MS, Sharma S, Srinivasan A, &, Singh TP, (2001) Camel lactoferrin, a transferrin-cum- lactoferrin: crystal structure of camel apolactoferrin at 2.6 Å resolution and structural basis of its dual role. J Mol Biol 309, 751-761.
    • (2001) J Mol Biol , vol.309 , pp. 751-761
    • Khan, J.A.1    Kumar, P.2    Paramasivam, M.3    Yadav, R.S.4    Sahani, M.S.5    Sharma, S.6    Srinivasan, A.7    Singh, T.P.8
  • 24
    • 0028813886 scopus 로고
    • Structure of human diferric lactoferrin refined at 2.2 Å resolution
    • Haridas M, Anderson BF, &, Baker EN, (1995) Structure of human diferric lactoferrin refined at 2.2 Å resolution. Acta Crystallogr D 51, 629-646.
    • (1995) Acta Crystallogr D , vol.51 , pp. 629-646
    • Haridas, M.1    Anderson, B.F.2    Baker, E.N.3
  • 25
    • 0033523098 scopus 로고    scopus 로고
    • Three-dimensional structure of mare diferric lactoferrin at 2.6 Å resolution
    • Sharma AK, Paramasivam M, Srinivasan A, Yadav MP, &, Singh TP, (1999) Three-dimensional structure of mare diferric lactoferrin at 2.6 Å resolution. J Mol Biol 289, 303-317.
    • (1999) J Mol Biol , vol.289 , pp. 303-317
    • Sharma, A.K.1    Paramasivam, M.2    Srinivasan, A.3    Yadav, M.P.4    Singh, T.P.5
  • 26
    • 0020508495 scopus 로고
    • The effect of trypsin and chymotrypsin on the in vitro antimicrobial and iron-binding properties of lactoferrin in human milk and bovine colostrum. Unusual resistance of human apolactoferrin to proteolytic digestion
    • Brines RD, &, Brock JH, (1983) The effect of trypsin and chymotrypsin on the in vitro antimicrobial and iron-binding properties of lactoferrin in human milk and bovine colostrum. Unusual resistance of human apolactoferrin to proteolytic digestion. Biochim Biophys Acta 759, 229-235.
    • (1983) Biochim Biophys Acta , vol.759 , pp. 229-235
    • Brines, R.D.1    Brock, J.H.2
  • 28
    • 0026293901 scopus 로고
    • Potent antibacterial peptides generated by pepsin digestion of bovine lactoferrin
    • Tomita M, Bellamy W, Takase M, Yamauchi K, Wakabayashi H, &, Kawase K, (1991) Potent antibacterial peptides generated by pepsin digestion of bovine lactoferrin. J Dairy Sci 74, 4137-4142.
    • (1991) J Dairy Sci , vol.74 , pp. 4137-4142
    • Tomita, M.1    Bellamy, W.2    Takase, M.3    Yamauchi, K.4    Wakabayashi, H.5    Kawase, K.6
  • 29
    • 0026475489 scopus 로고
    • Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin
    • Bellamy W, Takase M, Wakabayashi H, Kawase K, &, Tomita A, (1992) Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin. J Appl Bacteriol 73, 472-479.
    • (1992) J Appl Bacteriol , vol.73 , pp. 472-479
    • Bellamy, W.1    Takase, M.2    Wakabayashi, H.3    Kawase, K.4    Tomita, A.5
  • 30
    • 0027465990 scopus 로고
    • Antibacterial activity of lactoferrin and pepsin-derived lactoferrin peptide fragment
    • Yamauchi K, Tomita M, Giehl TJ, &, Ellison RT III, (1993) Antibacterial activity of lactoferrin and pepsin-derived lactoferrin peptide fragment Infect Immun 61, 719-728.
    • (1993) Infect Immun , vol.61 , pp. 719-728
    • Yamauchi, K.1    Tomita, M.2    Giehl, T.J.3    Ellison III, R.T.4
  • 32
    • 0033082082 scopus 로고    scopus 로고
    • Preparation and characterization of the N and C monoferric lobes of buffalo lactoferrin produced by proteolysis using proteinase K
    • Sharma S, Singh TP, &, Bhatia KL, (1999) Preparation and characterization of the N and C monoferric lobes of buffalo lactoferrin produced by proteolysis using proteinase K. J Dairy Res 66, 81-90.
    • (1999) J Dairy Res , vol.66 , pp. 81-90
    • Sharma, S.1    Singh, T.P.2    Bhatia, K.L.3
  • 33
    • 0041848518 scopus 로고    scopus 로고
    • Crystal structure of a proteolytically generated functional monoferric C-lobe of bovine lactoferrin at 1.9 Å resolution
    • Sharma S, Jasti J, Kumar J, Mohanty AK, &, Singh TP, (2003) Crystal structure of a proteolytically generated functional monoferric C-lobe of bovine lactoferrin at 1.9 Å resolution. J Mol Biol 331, 485-496.
    • (2003) J Mol Biol , vol.331 , pp. 485-496
    • Sharma, S.1    Jasti, J.2    Kumar, J.3    Mohanty, A.K.4    Singh, T.P.5
  • 34
    • 0032189645 scopus 로고    scopus 로고
    • Crystal structure of a complex formed between proteolytically generated lactoferrin fragment and proteinase K
    • Singh TP, Sharma S, Karthikeyan S, Betzel C, &, Bhatia KL, (1998) Crystal structure of a complex formed between proteolytically generated lactoferrin fragment and proteinase K. Proteins 33, 30-38.
    • (1998) Proteins , vol.33 , pp. 30-38
    • Singh, T.P.1    Sharma, S.2    Karthikeyan, S.3    Betzel, C.4    Bhatia, K.L.5
  • 35
    • 0027236660 scopus 로고
    • Structure of the recombinant N-terminal lobe of human lactoferrin at 2.0 Å resolution
    • Day CL, Anderson BF, Tweedie JW, &, Baker EN, (1993) Structure of the recombinant N-terminal lobe of human lactoferrin at 2.0 Å resolution. J Mol Biol 232, 1084-1100.
    • (1993) J Mol Biol , vol.232 , pp. 1084-1100
    • Day, C.L.1    Anderson, B.F.2    Tweedie, J.W.3    Baker, E.N.4
  • 36
    • 0026628351 scopus 로고
    • Studies of the N-terminal half of human lactoferrin produced from the cloned cDNA demonstrate that interlobe interactions modulate iron release
    • Day CL, Stowell KM, Baker EN, &, Tweedie JW, (1992) Studies of the N-terminal half of human lactoferrin produced from the cloned cDNA demonstrate that interlobe interactions modulate iron release. J Biol Chem 267, 13857-13862.
    • (1992) J Biol Chem , vol.267 , pp. 13857-13862
    • Day, C.L.1    Stowell, K.M.2    Baker, E.N.3    Tweedie, J.W.4
  • 37
    • 0013932518 scopus 로고
    • Ionic constituents and osmolality of gastric and small intestinal fluids after eating
    • Fordtran JS, &, Locklear TW, (1966) Ionic constituents and osmolality of gastric and small intestinal fluids after eating. Am J Dig Dis 11, 503-521.
    • (1966) Am J Dig Dis , vol.11 , pp. 503-521
    • Fordtran, J.S.1    Locklear, T.W.2
  • 39
    • 0032213139 scopus 로고    scopus 로고
    • Structure of human apolactoferrin at 2.0 Å resolution. Refinement and analysis of ligand-induced conformational change
    • Jameson GB, Anderson BF, Norris GE, Thomas DH, &, Baker EN, (1998) Structure of human apolactoferrin at 2.0 Å resolution. Refinement and analysis of ligand-induced conformational change. Acta Crystallogr D 54, 1319-1335.
    • (1998) Acta Crystallogr D , vol.54 , pp. 1319-1335
    • Jameson, G.B.1    Anderson, B.F.2    Norris, G.E.3    Thomas, D.H.4    Baker, E.N.5
  • 40
    • 0036008506 scopus 로고    scopus 로고
    • Crystal structure of equine apolactoferrin at 303 K providing further evidence of closed conformations of N and C lobes
    • Kumar P, Khan JA, Yadav S, &, Singh TP, (2002) Crystal structure of equine apolactoferrin at 303 K providing further evidence of closed conformations of N and C lobes. Acta Crystallogr D 58, 225-232.
    • (2002) Acta Crystallogr D , vol.58 , pp. 225-232
    • Kumar, P.1    Khan, J.A.2    Yadav, S.3    Singh, T.P.4
  • 41
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, &, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 42
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, &, Dodson EJ, (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 53, 240-255.
    • (1997) Acta Crystallogr D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 43
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, &, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D 60, 2126-2132.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 44
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones TA, Zou JY, Cowan SW, &, Kjeldgaard M, (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A 47, 110-119.
    • (1991) Acta Crystallogr A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 46
    • 0000243829 scopus 로고
    • PROCHECK - A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, &, Thornton JM, (1993) PROCHECK-a program to check the stereochemical quality of protein structures. J Appl Crystallogr 26, 283-291.
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4


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