PL EN


Preferences help
enabled [disable] Abstract
Number of results
2007 | 54 | 1 | 175-182
Article title

Isolation and characterisation of crocodile and python ovotransferrins

Content
Title variants
Languages of publication
EN
Abstracts
EN
Transferrins play a major role in iron homeostasis and metabolism. In vertebrates, these proteins are synthesised in the liver and dispersed within the organism by the bloodstream. In oviparous vertebrates additional expression is observed in the oviduct and the synthesised protein is deposited in egg white as ovotransferrin. Most research on ovotransferrin has been performed on the chicken protein. There is a limited amount of information on other bird transferrins, and until our previous paper on red-eared turtle protein there was no data on the isolation, sequencing and biochemical properties of reptilian ovotransferrins. Recently our laboratory deposited ten new sequences of reptilian transferrins in the EMBL database. A comparative analysis of these sequences indicates a possibility of different mechanisms of iron release among crocodile and snake transferrin. In the present paper we follow with the purification and analysis of the basic biochemical properties of two crocodile (Crocodilus niloticus, C. rhombifer) and one snake (Python molurus bivittatus) ovotransferrins. The proteins were purified by anion exchange and hydrophobic chromatography, and their N-terminal amino-acid sequences, molecular mass and isoelectric points were determined. All three proteins are glycosylated and their N-glycan chromatographic profiles show the largest contribution of neutral oligosaccharides in crocodile and disialylated glycans in python ovotransferrin. The absorption spectra of iron-saturated transferrins were analysed. Iron release from these proteins is pH-dependent, showing a biphasic character in crocodile ovotransferrins and a monophasic type in the python protein. The reason for the different types of iron release is discussed.
Publisher

Year
Volume
54
Issue
1
Pages
175-182
Physical description
Dates
published
2007
received
2006-11-28
revised
2007-02-12
accepted
2007-02-16
(unknown)
2007-03-09
Contributors
  • Laboratory of Biochemistry, Faculty of Biotechnology, University of Wroclaw, Wrocław, Poland
  • Laboratory of Biochemistry, Faculty of Biotechnology, University of Wroclaw, Wrocław, Poland
  • Laboratory of Biochemistry, Faculty of Biotechnology, University of Wroclaw, Wrocław, Poland
References
  • Aisen P, Enns C, Wessling-Resnick M (2001) Chemistry and biology of eukaryotic iron metabolism. Int J Biochem Cell Biol 33: 940-959.
  • Bailey S, Evans RW, Garratt RC, Gorinsky B, Hasnain S, Horsburgh C, Jhoti H, Lindley PF, Mydin A, Sarra R, Watson JL (1988) Molecular structure of serum transferrin at 3.3 Å resolution. Biochemistry 27: 5804-5812.
  • Baker HM, Mason AB, He QY, Baker EN (2001) Ligand variation in the transferrin family: the crystal structure of H249Q mutant of the human transferrin N-lobe as a model for iron binding in insect transferrins. Biochemistry 40: 11670-11675.
  • Baker EN, Baker HM, Kidd RD (2002) Lactoferrin and transferrin: functional variations on a common structural framework. Biochem Cell Biol 80: 27-34.
  • Baker HM, Anderson BF, Baker EN (2003) Dealing with iron: common structural principles in proteins that transport iron and heme. Proc Natl Acad Sci USA 100: 3579-3583.
  • Bali PK, Zak O, Aisen P (2001) A new role for the transferrin receptor in the release of iron from transferrin. Biochemistry 30: 324-328.
  • Bigge JC, Patel TP, Bruce JA, Goulding PN, Charles SM, Parekh RB (1995) Nonselective and efficient fluorescent labeling of glycans using 2-amino benzamide and anthranilic acid. Anal Biochem 230: 229-238.
  • Ciuraszkiewicz J, Olczak M, Watorek W (2006) Isolation, cloning and sequencing of transferrins from red-eared turtle, African ostrich, and turkey. Comp Biochem Physiol B Biochem Mol Biol 144: 301-310.
  • Dewan JC, Mikami B, Hirose M, Sacchettini JC (1993) Structural evidence for a pH-sensitive dilysine trigger in the hen ovotransferrin N-lobe: implications for transferrin release. Biochemistry 32: 11963-11968.
  • Gianetti AM, Halbrooks PJ, Mason AB, Vogt TM, Enns CA, Björkman PJ (2005) The molecular mechanism for receptor-stimulated iron release from the plasma iron transport protein transferrin. Structure 13: 1613-1623.
  • Gomme PT, McCann KB (2005) Transferrins: structure, function and potential therapeutic actions. Drug Discov Today 10: 267-273.
  • Halbrooks PJ, Giannetti AM, Klein JS, Björkman PJ, Larouche JR, Smith VC, MacGillivray RTA, Everse SJ, Mason AB (2005) Composition of pH-sensitive triad in C-lobe of human serum transferrin. Comparison to sequences of ovotransferrin and lactoferrin provides insight into functional differences in iron release. Biochemistry 44: 15451-15460.
  • He QY, Mason AB, Tam BM, MacGillivray RTA, Woodworth RC (1999) Dual role of Lys206-Lys296 interaction in human transferrin N-lobe: iron release trigger and anion-binding site. Biochemistry 38: 9704-9711.
  • Hentze MW, Kühn LC (1996) Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc Natl Acad Sci USA 93: 8175-8182.
  • Kim H, Nakai S (1996) Immunoglobulin separation from egg yolk: a serial filtration system. J Food Sci 61: 510-513.
  • Lambert LA, Perri H, Meehan TJ (2005a) Evolution of duplications in the transferrin family of proteins. Comp Biochem Physiol B Biochem Mol Biol 140: 11-25.
  • Lambert LA, Perri H, Halbrooks PJ, Mason AB (2005b) Evolution of transferrin family: conservation of residues associated with iron and anion binding. Comp Biochem Physiol B Biochem Mol Biol 142: 129-141.
  • Lee DC, McKnight S, Palmiter RD (1980) The chicken transferrin gene. Restriction endonuclease analysis of gene sequences in liver and oviduct DNA. J Biol Chem 255: 1442-1450.
  • Mason AB, Halbrooks PJ, James NG, Conolly SA, Larouche JR, Smith VC, MacGillivray RTA, Chasteen ND (2005) Mutational analysis of C-lobe ligands of human serum transferrin: insights into the mechanism of iron release. Biochemistry 44: 8013-8021.
  • 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.
  • Park I, Schaeffer E, Sidoli A, Barralle FE, Cohen GN, Zakin MM (1985) Organization of the human transferrin gene: direct evidence that it originated by gene duplication. Proc Natl Acad Sci USA 82: 3149-3153.
  • Schägger H, von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166: 368-379.
  • Valenti P, Antonini G (2005) Lactoferrin: an important host defence against microbial and viral attack. Cell Mol Life Sci 62: 2576-2587.
  • van Renswoude J, Bridges KR, Harford JB, Klausner RD (1982) Receptor-mediated endocytosis of transferrin and the uptake of Fe in K562 cells: identification of nonlysosomal acidic compartment. Proc Natl Acad Sci USA 79: 6186-6190.
  • Ward PP, Zhou X, Conneely OM (1996) Cooperative interactions between the amino- and carboxy-terminal lobes contribute to the unique iron-binding stability of lactoferrin. J Biol Chem 271: 12790-12794.
  • Welch S (1990) A comparison of the structure and properties of serum transferrin from 17 animal species. Comp Biochem Physiol B 97: 417-427.
  • Zak O, Ikuta K, Aisen P (2002) The synergistic anion-binding sites of human transferrin: chemical and physiological effects of site-directed mutagenesis. Biochemistry 41: 7416-7423.
  • Zak O, Aisen P (2003) Iron release from transferrin, its C-lobe and their complexes with transferrin receptor: presence of N-lobe accelerates release from C-lobe at endosomal pH. Biochemistry 42: 12330-12334.
  • Zor T, Selinger Z (1996) Linearization of the Bradford protein assay increases its sensitivity: theoretical and experimental studies. Anal Biochem 236: 302-308.
Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv54p175kz
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.