The transfer of iron between ceruloplasmin and transferrins
White, K. N. ; Conesa, C. ; S·nchez, L. ; Amini, M. ; Farnaud, S. ; Lorvoralak, C. ; Evans, R. W.
Resumen: Background
It is over 60 years since the discovery and isolation of the serum ferroxidase ceruloplasmin. In that time much basic information about the protein has been elucidated including its catalytic and kinetic properties as an enzyme, expression, sequence and structure. The importance of its biological role is indicated in genetic diseases such as aceruloplasminemia where its function is lost through mutation. Despite this wealth of data, fundamental questions about its action remain unanswered and in this article we address the question of how ferric iron produced by the ferroxidase activity of ceruloplasmin could be taken up by transferrins or lactoferrins.
Methods
Overlapping peptide libraries for human ceruloplasmin have been probed with a number of different lactoferrins to identify putative lactoferrin-binding regions on human ceruloplasmin. Docking software, 3D-Garden, has been used to model the binding of human lactoferrin to human ceruloplasmin.
Results
Upon probing the human ceruloplasmin library with human lactoferrin, three predominantly acidic lactoferrin-binding peptides, located in domains 2, 5 and 6 of human ceruloplasmin, were identified. The docking software identified a complex such that the N-lobe of human apo-lactoferrin interacts with the catalytic ferroxidase centre on human ceruloplasmin.
Idioma: Inglés
DOI: 10.1016/j.bbagen.2011.10.006
Año: 2012
Publicado en: Biochimica et Biophysica Acta - General Subjects 1820, 3 (2012), 411-416
ISSN: 0304-4165
Factor impacto JCR: 3.848 (2012)
Categ. JCR: BIOPHYSICS rank: 15 / 71 = 0.211 (2012) - Q1 - T1
Categ. JCR: BIOCHEMISTRY & MOLECULAR BIOLOGY rank: 89 / 288 = 0.309 (2012) - Q2 - T1
Tipo y forma: Article (PostPrint)
You must give appropriate credit, provide a link to the license, and indicate if changes were made. You may do so in any reasonable manner, but not in any way that suggests the licensor endorses you or your use. You may not use the material for commercial purposes. If you remix, transform, or build upon the material, you may not distribute the modified material.
Exportado de SIDERAL (2026-02-04-13:18:10)
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It is over 60 years since the discovery and isolation of the serum ferroxidase ceruloplasmin. In that time much basic information about the protein has been elucidated including its catalytic and kinetic properties as an enzyme, expression, sequence and structure. The importance of its biological role is indicated in genetic diseases such as aceruloplasminemia where its function is lost through mutation. Despite this wealth of data, fundamental questions about its action remain unanswered and in this article we address the question of how ferric iron produced by the ferroxidase activity of ceruloplasmin could be taken up by transferrins or lactoferrins.
Methods
Overlapping peptide libraries for human ceruloplasmin have been probed with a number of different lactoferrins to identify putative lactoferrin-binding regions on human ceruloplasmin. Docking software, 3D-Garden, has been used to model the binding of human lactoferrin to human ceruloplasmin.
Results
Upon probing the human ceruloplasmin library with human lactoferrin, three predominantly acidic lactoferrin-binding peptides, located in domains 2, 5 and 6 of human ceruloplasmin, were identified. The docking software identified a complex such that the N-lobe of human apo-lactoferrin interacts with the catalytic ferroxidase centre on human ceruloplasmin.
Idioma: Inglés
DOI: 10.1016/j.bbagen.2011.10.006
Año: 2012
Publicado en: Biochimica et Biophysica Acta - General Subjects 1820, 3 (2012), 411-416
ISSN: 0304-4165
Factor impacto JCR: 3.848 (2012)
Categ. JCR: BIOPHYSICS rank: 15 / 71 = 0.211 (2012) - Q1 - T1
Categ. JCR: BIOCHEMISTRY & MOLECULAR BIOLOGY rank: 89 / 288 = 0.309 (2012) - Q2 - T1
Tipo y forma: Article (PostPrint)
You must give appropriate credit, provide a link to the license, and indicate if changes were made. You may do so in any reasonable manner, but not in any way that suggests the licensor endorses you or your use. You may not use the material for commercial purposes. If you remix, transform, or build upon the material, you may not distribute the modified material. Exportado de SIDERAL (2026-02-04-13:18:10)
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Record created 2026-01-16, last modified 2026-02-04