Lactotransferrin

NameLactotransferrin
Synonyms
  • 3.4.21.-
  • GIG12
  • Growth-inhibiting protein 12
  • Lactoferrin
  • LF
  • Talalactoferrin
Gene NameLTF
OrganismHuman
Amino acid sequence
>lcl|BSEQ0001979|Lactotransferrin
MKLVFLVLLFLGALGLCLAGRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDS
PIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKG
GSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGA
DKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDE
AERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKD
KSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRKSEEEVAAR
RARVVWCAVGEQELRKCNQWSGLSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVYT
AGKCGLVPVLAENYKSQQSSDPDPNCVDRPVEGYLAVAVVRRSDTSLTWNSVKGKKSCHT
AVDRTAGWNIPMGLLFNQTGSCKFDEYFSQSCAPGSDPRSNLCALCIGDEQGENKCVPNS
NERYYGYTGAFRCLAENAGDVAFVKDVTVLQNTDGNNNEAWAKDLKLADFALLCLDGKRK
PVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGSDCPDKFCLFQSETKNL
LFNDNTECLARLHGKTTYEKYLGPQYVAGITNLKKCSTSPLLEACEFLRK
Number of residues710
Molecular Weight78181.225
Theoretical pI8.17
GO Classification
Functions
  • heparin binding
  • serine-type endopeptidase activity
  • protein serine/threonine kinase activator activity
  • DNA binding
  • iron ion binding
Processes
  • ossification
  • ion transport
  • negative regulation of viral process
  • positive regulation of toll-like receptor 4 signaling pathway
  • phagosome maturation
  • retina homeostasis
  • negative regulation by host of viral process
  • positive regulation of I-kappaB kinase/NF-kappaB signaling
  • bone morphogenesis
  • iron assimilation by chelation and transport
  • positive regulation of NF-kappaB transcription factor activity
  • negative regulation of lipopolysaccharide-mediated signaling pathway
  • positive regulation of protein serine/threonine kinase activity
  • humoral immune response
  • negative regulation of osteoclast development
  • antibacterial humoral response
  • interaction with host
  • negative regulation of single-species biofilm formation in or on host organism
  • innate immune response in mucosa
  • negative regulation of tumor necrosis factor (ligand) superfamily member 11 production
  • negative regulation of viral genome replication
  • positive regulation of bone mineralization involved in bone maturation
  • regulation of cytokine production
  • positive regulation of chondrocyte proliferation
  • regulation of tumor necrosis factor production
  • positive regulation of osteoblast proliferation
  • cellular protein metabolic process
  • response to host immune response
  • antifungal humoral response
  • negative regulation of apoptotic process
  • transcription, DNA-templated
  • positive regulation of osteoblast differentiation
  • negative regulation of ATPase activity
Components
  • protein complex
  • extracellular region
  • phagocytic vesicle lumen
  • nucleus
  • extracellular space
  • cell surface
  • extracellular exosome
  • secretory granule
  • specific granule
  • cytoplasm
General FunctionSerine-type endopeptidase activity
Specific FunctionTransferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.Lactotransferrin is a major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucosal secretions. Has antimicrobial activity, which depends on the extracellular cation concentration. Antimicrobial properties include bacteriostasis, which is related to its ability to sequester free iron and thus inhibit microbial growth, as well as direct bactericidal properties leading to the release of lipopolysaccharides from the bacterial outer membrane. Can also prevent bacterial biofilm development in P.aeruginosa infection. Has weak antifungal activity against C.albicans. Has anabolic, differentiating and anti-apoptotic effects on osteoblasts and can also inhibit osteoclastogenesis, possibly playing a role in the regulation of bone growth. Promotes binding of species C adenoviruses to epithelial cells, promoting adenovirus infection. Can inhibit papillomavirus infections. Stimulates the TLR4 signaling pathway leading to NF-kappa-B activation and subsequent pro-inflammatory cytokine production while also interfering with the lipopolysaccharide (LPS)-stimulated TLR4 signaling. Inhibits neutrophil granulocyte migration to sites of apoptosis, when secreted by apoptotic cells. Stimulates VEGFA-mediated endothelial cell migration and proliferation. Binds heparin, chondroitin sulfate and possibly other glycosaminoglycans (GAGs). Also binds specifically to pneumococcal surface protein A (pspA), the lipid A portion of bacterial lipopolysaccharide (LPS), lysozyme and DNA.Lactoferricin binds to the bacterial surface and is crucial for the bactericidal functions. Has some antiviral activity against papillomavirus infection. N-terminal region shows strong antifungal activity against C.albicans. Contains two BBXB heparin-binding consensus sequences that appear to form the predominate functional GAG-binding site.Kaliocin-1 has antimicrobial activity and is able to permeabilize different ions through liposomal membranes.Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors.The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity.Isoform DeltaLf: transcription factor with antiproliferative properties and ability to induce cell cycle arrest. Binds to the DeltaLf response element found in the SKP1, BAX, DCPS, and SELH promoters.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID34416
UniProtKB IDP02788
UniProtKB Entry NameTRFL_HUMAN
Cellular LocationSecreted
Gene sequence
>lcl|BSEQ0020499|Lactotransferrin (LTF)
ATGAGAAAAGTGCGTGGCCCTCCTGTCAGCTGCATAAAGAGAGACTCCCCCATCCAGTGT
ATCCAGGCCATTGCGGAAAACAGGGCCGATGCTGTGACCCTTGATGGTGGTTTCATATAC
GAGGCAGGCCTGGCCCCCTACAAACTGCGACCTGTAGCGGCGGAAGTCTACGGGACCGAA
AGACAGCCACGAACTCACTATTATGCCGTGGCTGTGGTGAAGAAGGGCGGCAGCTTTCAG
CTGAACGAACTGCAAGGTCTGAAGTCCTGCCACACAGGCCTTCGCAGGACCGCTGGATGG
AATGTCCCTATAGGGACACTTCGTCCATTCTTGAATTGGACGGGTCCACCTGAGCCCATT
GAGGCAGCTGTGGCCAGGTTCTTCTCAGCCAGCTGTGTTCCCGGTGCAGATAAAGGACAG
TTCCCCAACCTGTGTCGCCTGTGTGCGGGGACAGGGGAAAACAAATGTGCCTTCTCCTCC
CAGGAACCGTACTTCAGCTACTCTGGTGCCTTCAAGTGTCTGAGAGACGGGGCTGGAGAC
GTGGCTTTTATCAGAGAGAGCACAGTGTTTGAGGACCTGTCAGACGAGGCTGAAAGGGAC
GAGTATGAGTTACTCTGCCCAGACAACACTCGGAAGCCAGTGGACAAGTTCAAAGACTGC
CATCTGGCCCGGGTCCCTTCTCATGCCGTTGTGGCACGAAGTGTGAATGGCAAGGAGGAT
GCCATCTGGAATCTTCTCCGCCAGGCACAGGAAAAGTTTGGAAAGGACAAGTCACCGAAA
TTCCAGCTCTTTGGCTCCCCTAGTGGGCAGAAAGATCTGCTGTTCAAGGACTCTGCCATT
GGGTTTTCGAGGGTGCCCCCGAGGATAGATTCTGGGCTGTACCTTGGCTCCGGCTACTTC
ACTGCCATCCAGAACTTGAGGAAAAGTGAGGAGGAAGTGGCTGCCCGGCGTGCGCGGGTC
GTGTGGTGTGCGGTGGGCGAGCAGGAGCTGCGCAAGTGTAACCAGTGGAGTGGCTTGAGC
GAAGGCAGCGTGACCTGCTCCTCGGCCTCCACCACAGAGGACTGCATCGCCCTGGTGCTG
AAAGGAGAAGCTGATGCCATGAGTTTGGATGGAGGATATGTGTACACTGCAGGCAAATGT
GGTTTGGTGCCTGTCCTGGCAGAGAACTACAAATCCCAACAAAGCAGTGACCCTGATCCT
AACTGTGTGGATAGACCTGTGGAAGGATATCTTGCTGTGGCGGTGGTTAGGAGATCAGAC
ACTAGCCTTACCTGGAACTCTGTGAAAGGCAAGAAGTCCTGCCACACCGCCGTGGACAGG
ACTGCAGGCTGGAATATCCCCATGGGCCTGCTCTTCAACCAGACGGGCTCCTGCAAATTT
GATGAATATTTCAGTCAAAGCTGTGCCCCTGGGTCTGACCCGAGATCTAATCTCTGTGCT
CTGTGTATTGGCGACGAGCAGGGTGAGAATAAGTGCGTGCCCAACAGCAACGAGAGATAC
TACGGCTACACTGGGGCTTTCCGGTGCCTGGCTGAGAATGCTGGAGACGTTGCATTTGTG
AAAGATGTCACTGTCTTGCAGAACACTGATGGAAATAACAATGAGGCATGGGCTAAGGAT
TTGAAGCTGGCAGACTTTGCGCTGCTGTGCCTCGATGGCAAACGGAAGCCTGTGACTGAG
GCTAGAAGCTGCCATCTTGCCATGGCCCCGAATCATGCCGTGGTGTCTCGGATGGATAAG
GTGGAACGCCTGAAACAGGTGTTGCTCCACCAACAGGCTAAATTTGGGAGAAATGGATCT
GACTGCCCGGACAAGTTTTGCTTATTCCAGTCTGAAACCAAAAACCTTCTGTTCAATGAC
AACACTGAGTGTCTGGCCAGACTCCATGGCAAAACAACATATGAAAAATATTTGGGACCA
CAGTATGTCGCAGGCATTACTAATCTGAAAAAGTGCTCAACCTCCCCCCTCCTGGAAGCC
TGTGAATTCCTCAGGAAGTAA
GenBank Gene IDX53961
GeneCard IDNot Available
GenAtlas IDLTF
HGNC IDHGNC:6720
Chromosome Location3
Locus3q21-q23
References
  1. Rey MW, Woloshuk SL, deBoer HA, Pieper FR: Complete nucleotide sequence of human mammary gland lactoferrin. Nucleic Acids Res. 1990 Sep 11;18(17):5288. 2402455
  2. Siebert PD, Huang BC: Identification of an alternative form of human lactoferrin mRNA that is expressed differentially in normal tissues and tumor-derived cell lines. Proc Natl Acad Sci U S A. 1997 Mar 18;94(6):2198-203. 9122171
  3. Cheng H, Chen XZ, Huan LD: [cDNA cloning and sequence analysis of human lactoferrin]. Sheng Wu Gong Cheng Xue Bao. 2001 Jul;17(4):385-7. 11702692
  4. Kumar J, Weber W, Munchau S, Yadav S, Singh SB, Saravanan K, Paramasivam M, Sharma S, Kaur P, Bhushan A, Srinivasan A, Betzel C, Singh TP: Crystal structure of human seminal diferric lactoferrin at 3.4 Angstrom resolution. Indian J Biochem Biophys. 2003 Feb;40(1):14-21. 22900286
  5. Velliyagounder K, Kaplan JB, Furgang D, Legarda D, Diamond G, Parkin RE, Fine DH: One of two human lactoferrin variants exhibits increased antibacterial and transcriptional activation activities and is associated with localized juvenile periodontitis. Infect Immun. 2003 Nov;71(11):6141-7. 14573629
  6. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. 14702039
  7. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. 16641997
  8. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. 15489334
  9. Teng CT, Liu Y, Yang N, Walmer D, Panella T: Differential molecular mechanism of the estrogen action that regulates lactoferrin gene in human and mouse. Mol Endocrinol. 1992 Nov;6(11):1969-81. 1480183
  10. Powell MJ, Ogden JE: Nucleotide sequence of human lactoferrin cDNA. Nucleic Acids Res. 1990 Jul 11;18(13):4013. 2374734
  11. Metz-Boutigue MH, Jolles J, Mazurier J, Schoentgen F, Legrand D, Spik G, Montreuil J, Jolles P: Human lactotransferrin: amino acid sequence and structural comparisons with other transferrins. Eur J Biochem. 1984 Dec 17;145(3):659-76. 6510420
  12. Metz-Boutigue MH, Mazurier J, Jolles J, Spik G, Montreuil J, Jolles P: The present state of the human lactotransferrin sequence. Study and alignment of the cyanogen bromide fragments and characterization of N- and C-terminal domains. Biochim Biophys Acta. 1981 Sep 29;670(2):243-54. 6794640
  13. Bellamy W, Takase M, Yamauchi K, Wakabayashi H, Kawase K, Tomita M: Identification of the bactericidal domain of lactoferrin. Biochim Biophys Acta. 1992 May 22;1121(1-2):130-6. 1599934
  14. Mann DM, Romm E, Migliorini M: Delineation of the glycosaminoglycan-binding site in the human inflammatory response protein lactoferrin. J Biol Chem. 1994 Sep 23;269(38):23661-7. 8089135
  15. Sato I: Characterization of the 84-kDa protein with ABH activity in human seminal plasma. Nihon Hoigaku Zasshi. 1995 Oct;49(5):281-93. 8551695
  16. Hunter HN, Demcoe AR, Jenssen H, Gutteberg TJ, Vogel HJ: Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent. Antimicrob Agents Chemother. 2005 Aug;49(8):3387-95. 16048952
  17. Azkargorta M, Soria J, Ojeda C, Guzman F, Acera A, Iloro I, Suarez T, Elortza F: Human Basal Tear Peptidome Characterization by CID, HCD, and ETD Followed by in Silico and in Vitro Analyses for Antimicrobial Peptide Identification. J Proteome Res. 2015 Jun 5;14(6):2649-58. doi: 10.1021/acs.jproteome.5b00179. Epub 2015 May 20. 25946035
  18. Rado TA, Wei XP, Benz EJ Jr: Isolation of lactoferrin cDNA from a human myeloid library and expression of mRNA during normal and leukemic myelopoiesis. Blood. 1987 Oct;70(4):989-93. 3477300
  19. Metz-Boutigue MH, Jolles J, Mazurier J, Spik G, Montreuil J, Jolles P: An 88 amino acid long C-terminal sequence of human lactotransferrin. FEBS Lett. 1982 Jun 1;142(1):107-10. 7049727
  20. Arnold RR, Russell JE, Champion WJ, Brewer M, Gauthier JJ: Bactericidal activity of human lactoferrin: differentiation from the stasis of iron deprivation. Infect Immun. 1982 Mar;35(3):792-9. 6802759
  21. Cramer E, Pryzwansky KB, Villeval JL, Testa U, Breton-Gorius J: Ultrastructural localization of lactoferrin and myeloperoxidase in human neutrophils by immunogold. Blood. 1985 Feb;65(2):423-32. 2981589
  22. Ellison RT 3rd, Giehl TJ, LaForce FM: Damage of the outer membrane of enteric gram-negative bacteria by lactoferrin and transferrin. Infect Immun. 1988 Nov;56(11):2774-81. 3169987
  23. Tani F, Iio K, Chiba H, Yoshikawa M: Isolation and characterization of opioid antagonist peptides derived from human lactoferrin. Agric Biol Chem. 1990 Jul;54(7):1803-10. 1369293
  24. van Berkel PH, Geerts ME, van Veen HA, Mericskay M, de Boer HA, Nuijens JH: N-terminal stretch Arg2, Arg3, Arg4 and Arg5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNA. Biochem J. 1997 Nov 15;328 ( Pt 1):145-51. 9359845
  25. Lupetti A, Paulusma-Annema A, Welling MM, Senesi S, van Dissel JT, Nibbering PH: Candidacidal activities of human lactoferrin peptides derived from the N terminus. Antimicrob Agents Chemother. 2000 Dec;44(12):3257-63. 11083624
  26. Abrink M, Larsson E, Gobl A, Hellman L: Expression of lactoferrin in the kidney: implications for innate immunity and iron metabolism. Kidney Int. 2000 May;57(5):2004-10. 10792619
  27. Nibbering PH, Ravensbergen E, Welling MM, van Berkel LA, van Berkel PH, Pauwels EK, Nuijens JH: Human lactoferrin and peptides derived from its N terminus are highly effective against infections with antibiotic-resistant bacteria. Infect Immun. 2001 Mar;69(3):1469-76. 11179314
  28. Singh PK, Parsek MR, Greenberg EP, Welsh MJ: A component of innate immunity prevents bacterial biofilm development. Nature. 2002 May 30;417(6888):552-5. 12037568
  29. Liu D, Wang X, Zhang Z, Teng CT: An intronic alternative promoter of the human lactoferrin gene is activated by Ets. Biochem Biophys Res Commun. 2003 Feb 7;301(2):472-9. 12565886
  30. Viejo-Diaz M, Andres MT, Perez-Gil J, Sanchez M, Fierro JF: Potassium efflux induced by a new lactoferrin-derived peptide mimicking the effect of native human lactoferrin on the bacterial cytoplasmic membrane. Biochemistry (Mosc). 2003 Feb;68(2):217-27. 12693969
  31. Hendrixson DR, Qiu J, Shewry SC, Fink DL, Petty S, Baker EN, Plaut AG, St Geme JW 3rd: Human milk lactoferrin is a serine protease that cleaves Haemophilus surface proteins at arginine-rich sites. Mol Microbiol. 2003 Feb;47(3):607-17. 12535064
  32. Breton M, Mariller C, Benaissa M, Caillaux K, Browaeys E, Masson M, Vilain JP, Mazurier J, Pierce A: Expression of delta-lactoferrin induces cell cycle arrest. Biometals. 2004 Jun;17(3):325-9. 15222485
  33. Cornish J, Callon KE, Naot D, Palmano KP, Banovic T, Bava U, Watson M, Lin JM, Tong PC, Chen Q, Chan VA, Reid HE, Fazzalari N, Baker HM, Baker EN, Haggarty NW, Grey AB, Reid IR: Lactoferrin is a potent regulator of bone cell activity and increases bone formation in vivo. Endocrinology. 2004 Sep;145(9):4366-74. Epub 2004 May 27. 15166119
  34. Kim CW, Son KN, Choi SY, Kim J: Human lactoferrin upregulates expression of KDR/Flk-1 and stimulates VEGF-A-mediated endothelial cell proliferation and migration. FEBS Lett. 2006 Aug 7;580(18):4332-6. Epub 2006 Jul 7. 16842782
  35. Mistry N, Drobni P, Naslund J, Sunkari VG, Jenssen H, Evander M: The anti-papillomavirus activity of human and bovine lactoferricin. Antiviral Res. 2007 Sep;75(3):258-65. Epub 2007 Apr 20. 17481742
  36. Wang Z, Widgren EE, Richardson RT, O'Rand MG: Characterization of an eppin protein complex from human semen and spermatozoa. Biol Reprod. 2007 Sep;77(3):476-84. Epub 2007 Jun 13. 17567961
  37. Johansson C, Jonsson M, Marttila M, Persson D, Fan XL, Skog J, Frangsmyr L, Wadell G, Arnberg N: Adenoviruses use lactoferrin as a bridge for CAR-independent binding to and infection of epithelial cells. J Virol. 2007 Jan;81(2):954-63. Epub 2006 Nov 1. 17079302
  38. Picariello G, Ferranti P, Mamone G, Roepstorff P, Addeo F: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics. 2008 Sep;8(18):3833-47. doi: 10.1002/pmic.200701057. 18780401
  39. Bournazou I, Pound JD, Duffin R, Bournazos S, Melville LA, Brown SB, Rossi AG, Gregory CD: Apoptotic human cells inhibit migration of granulocytes via release of lactoferrin. J Clin Invest. 2009 Jan;119(1):20-32. doi: 10.1172/JCI36226. Epub 2008 Dec 1. 19033648
  40. Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. doi: 10.1021/pr8008012. 19159218
  41. Ando K, Hasegawa K, Shindo K, Furusawa T, Fujino T, Kikugawa K, Nakano H, Takeuchi O, Akira S, Akiyama T, Gohda J, Inoue J, Hayakawa M: Human lactoferrin activates NF-kappaB through the Toll-like receptor 4 pathway while it interferes with the lipopolysaccharide-stimulated TLR4 signaling. FEBS J. 2010 May;277(9):2051-66. doi: 10.1111/j.1742-4658.2010.07620.x. Epub 2010 Mar 19. 20345905
  42. Hardiville S, Hoedt E, Mariller C, Benaissa M, Pierce A: O-GlcNAcylation/phosphorylation cycling at Ser10 controls both transcriptional activity and stability of delta-lactoferrin. J Biol Chem. 2010 Jun 18;285(25):19205-18. doi: 10.1074/jbc.M109.080572. Epub 2010 Apr 19. 20404350
  43. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. 21269460
  44. Mariller C, Hardiville S, Hoedt E, Huvent I, Pina-Canseco S, Pierce A: Delta-lactoferrin, an intracellular lactoferrin isoform that acts as a transcription factor. Biochem Cell Biol. 2012 Jun;90(3):307-19. doi: 10.1139/o11-070. Epub 2012 Feb 9. 22320386
  45. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. 24275569
  46. Anderson BF, Baker HM, Norris GE, Rice DW, Baker EN: Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8 A resolution. J Mol Biol. 1989 Oct 20;209(4):711-34. 2585506
  47. Norris GE, Anderson BF, Baker EN: Molecular replacement solution of the structure of apolactoferrin, a protein displaying large-scale conformational change. Acta Crystallogr B. 1991 Dec 1;47 ( Pt 6):998-1004. 1772635
  48. Smith CA, Anderson BF, Baker HM, Baker EN: Metal substitution in transferrins: the crystal structure of human copper-lactoferrin at 2.1-A resolution. Biochemistry. 1992 May 12;31(18):4527-33. 1581307
  49. Day CL, Anderson BF, Tweedie JW, Baker EN: Structure of the recombinant N-terminal lobe of human lactoferrin at 2.0 A resolution. J Mol Biol. 1993 Aug 20;232(4):1084-100. 8371268
  50. Smith CA, Anderson BF, Baker HM, Baker EN: Structure of copper- and oxalate-substituted human lactoferrin at 2.0 A resolution. Acta Crystallogr D Biol Crystallogr. 1994 May 1;50(Pt 3):302-16. 15299444
  51. Bourne Y, Mazurier J, Legrand D, Rouge P, Montreuil J, Spik G, Cambillau C: Structures of a legume lectin complexed with the human lactotransferrin N2 fragment, and with an isolated biantennary glycopeptide: role of the fucose moiety. Structure. 1994 Mar 15;2(3):209-19. 8069634
  52. Haridas M, Anderson BF, Baker EN: Structure of human diferric lactoferrin refined at 2.2 A resolution. Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):629-46. 15299793
  53. Baker HM, Anderson BF, Brodie AM, Shongwe MS, Smith CA, Baker EN: Anion binding by transferrins: importance of second-shell effects revealed by the crystal structure of oxalate-substituted diferric lactoferrin. Biochemistry. 1996 Jul 16;35(28):9007-13. 8703903
  54. Faber HR, Baker CJ, Day CL, Tweedie JW, Baker EN: Mutation of arginine 121 in lactoferrin destabilizes iron binding by disruption of anion binding: crystal structures of R121S and R121E mutants. Biochemistry. 1996 Nov 19;35(46):14473-9. 8931543
  55. Faber HR, Bland T, Day CL, Norris GE, Tweedie JW, Baker EN: Altered domain closure and iron binding in transferrins: the crystal structure of the Asp60Ser mutant of the amino-terminal half-molecule of human lactoferrin. J Mol Biol. 1996 Feb 23;256(2):352-63. 8594202
  56. Nicholson H, Anderson BF, Bland T, Shewry SC, Tweedie JW, Baker EN: Mutagenesis of the histidine ligand in human lactoferrin: iron binding properties and crystal structure of the histidine-253-->methionine mutant. Biochemistry. 1997 Jan 14;36(2):341-6. 9003186
  57. Jameson GB, Anderson BF, Norris GE, Thomas DH, Baker EN: Structure of human apolactoferrin at 2.0 A resolution. Refinement and analysis of ligand-induced conformational change. Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1319-35. 10089508
  58. Sun XL, Baker HM, Shewry SC, Jameson GB, Baker EN: Structure of recombinant human lactoferrin expressed in Aspergillus awamori. Acta Crystallogr D Biol Crystallogr. 1999 Feb;55(Pt 2):403-7. 10089347
  59. Peterson NA, Anderson BF, Jameson GB, Tweedie JW, Baker EN: Crystal structure and iron-binding properties of the R210K mutant of the N-lobe of human lactoferrin: implications for iron release from transferrins. Biochemistry. 2000 Jun 6;39(22):6625-33. 10828980
  60. Baker HM, Baker CJ, Smith CA, Baker EN: Metal substitution in transferrins: specific binding of cerium(IV) revealed by the crystal structure of cerium-substituted human lactoferrin. J Biol Inorg Chem. 2000 Dec;5(6):692-8. 11128996
  61. Jameson GB, Anderson BF, Breyer WA, Day CL, Tweedie JW, Baker EN: Structure of a domain-opened mutant (R121D) of the human lactoferrin N-lobe refined from a merohedrally twinned crystal form. Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):955-62. Epub 2002 May 29. 12037297
  62. Peterson NA, Arcus VL, Anderson BF, Tweedie JW, Jameson GB, Baker EN: "Dilysine trigger" in transferrins probed by mutagenesis of lactoferrin: crystal structures of the R210G, R210E, and R210L mutants of human lactoferrin. Biochemistry. 2002 Dec 3;41(48):14167-75. 12450380
  63. Japelj B, Pristovsek P, Majerle A, Jerala R: Structural origin of endotoxin neutralization and antimicrobial activity of a lactoferrin-based peptide. J Biol Chem. 2005 Apr 29;280(17):16955-61. Epub 2005 Feb 1. 15687491
  64. Thomassen EA, van Veen HA, van Berkel PH, Nuijens JH, Abrahams JP: The protein structure of recombinant human lactoferrin produced in the milk of transgenic cows closely matches the structure of human milk-derived lactoferrin. Transgenic Res. 2005 Aug;14(4):397-405. 16201406
  65. Japelj B, Zorko M, Majerle A, Pristovsek P, Sanchez-Gomez S, Martinez de Tejada G, Moriyon I, Blondelle SE, Brandenburg K, Andra J, Lohner K, Jerala R: The acyl group as the central element of the structural organization of antimicrobial lipopeptide. J Am Chem Soc. 2007 Feb 7;129(5):1022-3. 17263370
  66. Senkovich O, Cook WJ, Mirza S, Hollingshead SK, Protasevich II, Briles DE, Chattopadhyay D: Structure of a complex of human lactoferrin N-lobe with pneumococcal surface protein a provides insight into microbial defense mechanism. J Mol Biol. 2007 Jul 20;370(4):701-13. Epub 2007 May 10. 17543335
  67. Klintworth GK, Sommer JR, Obrian G, Han L, Ahmed MN, Qumsiyeh MB, Lin PY, Basti S, Reddy MK, Kanai A, Hotta Y, Sugar J, Kumaramanickavel G, Munier F, Schorderet DF, El Matri L, Iwata F, Kaiser-Kupfer M, Nagata M, Nakayasu K, Hejtmancik JF, Teng CT: Familial subepithelial corneal amyloidosis (gelatinous drop-like corneal dystrophy): exclusion of linkage to lactoferrin gene. Mol Vis. 1998 Dec 31;4:31. 9873069
  68. Videm V, Dahl H, Walberg LE, Wiseth R: Functional polymorphisms in the LTF gene and risk of coronary artery stenosis. Hum Immunol. 2012 May;73(5):554-9. doi: 10.1016/j.humimm.2012.02.014. Epub 2012 Feb 26. 22406253