scholarly journals Ionic Residues of Human Serum Transferrin Affect Binding to the Transferrin Receptor and Iron Release

Biochemistry ◽  
2012 ◽  
Vol 51 (2) ◽  
pp. 686-694 ◽  
Author(s):  
Ashley N. Steere ◽  
Brendan F. Miller ◽  
Samantha E. Roberts ◽  
Shaina L. Byrne ◽  
N. Dennis Chasteen ◽  
...  
Keyword(s):  
Human Serum ◽  
Transferrin Receptor ◽  
Serum Transferrin ◽  
Iron Release ◽  
Human Serum Transferrin

Tertiary structural changes and iron release from human serum transferrin

1997 ◽  
Vol 270 (5) ◽  
pp. 739-750 ◽  
Author(s):  
Sandra L Mecklenburg ◽  
Robert J Donohoe ◽  
Glenn A Olah
Keyword(s):  
Human Serum ◽  
Structural Changes ◽  
Serum Transferrin ◽  
Iron Release ◽  
Human Serum Transferrin

Mutational Analysis of C-Lobe Ligands of Human Serum Transferrin:  Insights into the Mechanism of Iron Release†

Biochemistry ◽  
2005 ◽  
Vol 44 (22) ◽  
pp. 8013-8021 ◽  
Author(s):  
Anne B. Mason ◽  
Peter J. Halbrooks ◽  
Nicholas G. James ◽  
Susan A. Connolly ◽  
Julia R. Larouche ◽  
...  
Keyword(s):  
Human Serum ◽  
Mutational Analysis ◽  
Serum Transferrin ◽  
Iron Release ◽  
Human Serum Transferrin

scholarly journals The Position of Arginine 124 Controls the Rate of Iron Release from the N-lobe of Human Serum Transferrin

2002 ◽  
Vol 278 (8) ◽  
pp. 6027-6033 ◽  
Author(s):  
Ty E. Adams ◽  
Anne B. Mason ◽  
Qing-Yu He ◽  
Peter J. Halbrooks ◽  
Sara K. Briggs ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Transferrin ◽  
Iron Release ◽  
Human Serum Transferrin

Investigation of the Mechanism of Iron Release from the C-Lobe of Human Serum Transferrin:  Mutational Analysis of the Role of a pH Sensitive Triad†

Biochemistry ◽  
2003 ◽  
Vol 42 (13) ◽  
pp. 3701-3707 ◽  
Author(s):  
Peter J. Halbrooks ◽  
Qing-Yu He ◽  
Sara K. Briggs ◽  
Stephen J. Everse ◽  
Valerie C. Smith ◽  
...  
Keyword(s):  
Human Serum ◽  
Mutational Analysis ◽  
Ph Sensitive ◽  
Serum Transferrin ◽  
Iron Release ◽  
Human Serum Transferrin

scholarly journals Structure-Based Mutagenesis Reveals Critical Residues in the Transferrin Receptor Participating in the Mechanism of pH-Induced Release of Iron from Human Serum Transferrin

Biochemistry ◽  
2012 ◽  
Vol 51 (10) ◽  
pp. 2113-2121 ◽  
Author(s):  
Ashley N. Steere ◽  
N. Dennis Chasteen ◽  
Brendan F. Miller ◽  
Valerie C. Smith ◽  
Ross T. A. MacGillivray ◽  
...  
Keyword(s):  
Human Serum ◽  
Transferrin Receptor ◽  
Serum Transferrin ◽  
Human Serum Transferrin ◽  
Critical Residues

Aluminum Exchange between Citrate and Human Serum Transferrin and Interaction with Transferrin Receptor 1

Biochemistry ◽  
2003 ◽  
Vol 42 (10) ◽  
pp. 3120-3130 ◽  
Author(s):  
Miryana Hémadi ◽  
Geneviève Miquel ◽  
Philippe H. Kahn ◽  
Jean-Michel El Hage Chahine
Keyword(s):  
Human Serum ◽  
Transferrin Receptor ◽  
Serum Transferrin ◽  
Human Serum Transferrin ◽  
Transferrin Receptor 1

A Density Functional Theory Study of the Iron-Binding Site of Human Serum Transferrin

2004 ◽  
Vol 57 (12) ◽  
pp. 1219 ◽  
Author(s):  
David Rinaldo ◽  
Martin J. Field
Keyword(s):  
Human Serum ◽  
Binding Site ◽  
Conformational Changes ◽  
Metal Binding ◽  
Density Functional ◽  
Release Mechanism ◽  
Serum Transferrin ◽  
Iron Binding ◽  
Iron Release ◽  
Human Serum Transferrin

Human serum transferrin binds ferric ions with high affinity in the blood stream and releases them into cells by a process involving receptor-mediated endocytosis and a decrease in pH. The iron-release mechanism is unclear but protonation events and conformational changes are known to be important. In this study, we investigate properties of the iron-binding site theoretically. Our results suggest that an equatorial histidine could be in its histidinate form when bound to iron at neutral and high pH and that protonation of an axial tyrosine is a key event in iron release. Support for this mechanism from other metal-binding enzymes is also presented.

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 ◽  
2005 ◽  
Vol 44 (47) ◽  
pp. 15451-15460 ◽  
Author(s):  
Peter J. Halbrooks ◽  
Anthony M. Giannetti ◽  
Joshua S. Klein ◽  
Pamela J. Björkman ◽  
Julia R. Larouche ◽  
...  
Keyword(s):  
Human Serum ◽  
Ph Sensitive ◽  
Serum Transferrin ◽  
Iron Release ◽  
Human Serum Transferrin ◽  
Functional Differences ◽  
Insight Into

Intrinsic Fluorescence Reports a Global Conformational Change in the N-Lobe of Human Serum Transferrin following Iron Release†

Biochemistry ◽  
2007 ◽  
Vol 46 (37) ◽  
pp. 10603-10611 ◽  
Author(s):  
Nicholas G. James ◽  
Christopher L. Berger ◽  
Shaina L. Byrne ◽  
Valerie C. Smith ◽  
Ross T. A. MacGillivray ◽  
...  
Keyword(s):  
Human Serum ◽  
Conformational Change ◽  
Intrinsic Fluorescence ◽  
Serum Transferrin ◽  
Iron Release ◽  
Human Serum Transferrin

scholarly journals Receptor recognition sites reside in both lobes of human serum transferrin

1997 ◽  
Vol 326 (1) ◽  
pp. 77-85 ◽  
Author(s):  
Anne B. MASON ◽  
Beatrice M. TAM ◽  
Robert C. WOODWORTH ◽  
Ronald W. A. OLIVER ◽  
Brian N. GREEN ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Human Serum ◽  
Transferrin Receptor ◽  
Expression System ◽  
Cell System ◽  
Serum Transferrin ◽  
Human Serum Transferrin ◽  
Human Transferrin ◽  
Domain Specific ◽  
Mammalian Expression

The binding of iron by transferrin leads to a significant conformational change in each lobe of the protein. Numerous studies have shown that the transferrin receptor discriminates between iron-saturated and iron-free transferrin and that it modulates the release of iron. Given these observations, it seems likely that there is contact between each lobe of transferrin and the receptor. This is the case with chicken transferrin, in which it has been demonstrated unambiguously that both lobes are required for binding and iron donation to occur [Brown-Mason and Woodworth (1984) J. Biol. Chem. 259, 1866–1873]. Further support to this contention is added by the ability of both N- and C-domain-specific monoclonal antibodies to block the binding of a solution containing both lobes [Mason, Brown and Church (1987) J. Biol. Chem. 262, 9011–9015]. In the present study a similar conclusion is reached for the binding of human serum transferrin to the transferrin receptor. With the use of recombinant N- and C-lobes of human transferrin produced in a mammalian expression system, we show that both lobes are required to achieve full binding. (Production of recombinant C-lobe in the baby hamster kidney cell system is reported here for the first time.) Each lobe is able to donate iron to transferrin receptors on HeLa S3 cells in the presence of the contralateral lobe. The results are not identical with the chicken system, because the C-lobe alone shows a limited ability to bind to receptors and to donate iron. Further complications arise from the relatively weak re-association between the two lobes of human transferrin compared with the re-association of the ovotransferrin lobes. However, domain-specific monoclonal antibodies to either lobe block the binding of N- and C-lobe mixtures in the human system, thus substantiating the need for both.

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