scholarly journals A loop in theN-lobe of human serum transferrin is critical for binding to the transferrin receptor as revealed by mutagenesis, isothermal titration calorimetry, and epitope mapping

2009 ◽  
Vol 22 (6) ◽  
pp. 521-529 ◽  
Author(s):  
Anne B. Mason ◽  
Shaina L. Byrne ◽  
Stephen J. Everse ◽  
Samantha E. Roberts ◽  
N. Dennis Chasteen ◽  
...  
Keyword(s):  
Human Serum ◽  
Isothermal Titration Calorimetry ◽  
Transferrin Receptor ◽  
Epitope Mapping ◽  
Titration Calorimetry ◽  
Serum Transferrin ◽  
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

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

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.

scholarly journals A first-principles study on potential chelation agents and indicators of Alzheimer's disease

RSC Advances ◽  
2020 ◽  
Vol 10 (58) ◽  
pp. 35574-35581
Author(s):  
Bryan Wang ◽  
Xuan Luo
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Human Serum ◽  
Blood Brain Barrier ◽  
First Principles ◽  
Brain Barrier ◽  
Serum Transferrin ◽  
Human Serum Transferrin ◽  
First Principles Study ◽  
Blood Brain

Human-serum transferrin is involved in the transportation of aluminum across the blood–brain barrier.

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