Research Topics
Genomes and Genes | Anne MasonSummaryAffiliation: University of Vermont Country: USA Publications
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Publications
Structural and functional consequences of the substitution of glycine 65 with arginine in the N-lobe of human transferrinAnne B Mason
Department of Biochemistry, University of Vermont College of Medicine, Burlington, Vermont 05405, USA
Biochemistry 48:1945-53. 2009....
Mutational analysis of C-lobe ligands of human serum transferrin: insights into the mechanism of iron releaseAnne B Mason
Department of Biochemistry, University of Vermont College of Medicine, Burlington, Vermont 05405 0068, USA
Biochemistry 44:8013-21. 2005....
A loop in the N-lobe of human serum transferrin is critical for binding to the transferrin receptor as revealed by mutagenesis, isothermal titration calorimetry, and epitope mappingAnne B Mason
Department of Biochemistry, College of Medicine, University of Vermont, 89 Beaumont Avenue, Burlington, VT 05405, USA
J Mol Recognit 22:521-9. 2009....- Expression, purification, and characterization of authentic monoferric and apo-human serum transferrinsAnne B Mason
Department of Biochemistry, University of Vermont, College of Medicine, 89 Beaumont Avenue, Burlington, VT 05405, USA
Protein Expr Purif 36:318-26. 2004..These improvements should be applicable to expression of other recombinant proteins in mammalian cells... - Evolution reversed: the ability to bind iron restored to the N-lobe of the murine inhibitor of carbonic anhydrase by strategic mutagenesisAnne B Mason
Department of Biochemistry, College of Medicine, University of Vermont, Burlington, Vermont 05405, USA
Biochemistry 47:9847-55. 2008..Proof of this assignment is provided by limited trypsin proteolysis of porcine ICA... - The oxalate effect on release of iron from human serum transferrin explainedPeter J Halbrooks
Department of Biochemistry, College of Medicine, University of Vermont, 89 Beaumont Avenue, Burlington, VT 05405, USA
J Mol Biol 339:217-26. 2004..In the context of iron uptake by cells, substitution of carbonate by oxalate effectively locks the iron into each lobe of hTF, thereby interfering with normal iron metabolism... - The position of arginine 124 controls the rate of iron release from the N-lobe of human serum transferrin. A structural studyTy E Adams
Department of Biochemistry, University of Vermont, College of Medicine, Burlington, Vermont 05405, USA
J Biol Chem 278:6027-33. 2003..Access to the carbonate via a water channel allows entry of protons and anions, enabling the attack on the iron... - Investigation of the mechanism of iron release from the C-lobe of human serum transferrin: mutational analysis of the role of a pH sensitive triadPeter J Halbrooks
Department of Biochemistry, University of Vermont, College of Medicine, 89 Beaumont Avenue, Burlington, Vermont 05405, USA
Biochemistry 42:3701-7. 2003..In addition, the striking difference in the effect of increasing salt concentrations on iron release from the two lobes of hTF is further documented in the present work... - The unique kinetics of iron release from transferrin: the role of receptor, lobe-lobe interactions, and salt at endosomal pHShaina L Byrne
Department of Biochemistry, College of Medicine, University of Vermont, 89 Beaumont Avenue, Burlington, VT 05405, USA
J Mol Biol 396:130-40. 2010..Accurate rate constants for the pH and salt-induced conformational changes in each lobe precisely delineate how delivery of iron within the physiologically relevant time frame of 2 min might be accomplished... - Human serum transferrin: a tale of two lobes. Urea gel and steady state fluorescence analysis of recombinant transferrins as a function of pH, time, and the soluble portion of the transferrin receptorShaina L Byrne
Department of Biochemistry, University of Vermont College of Medicine, Burlington, VT 05405 0068, USA
J Biol Inorg Chem 14:771-81. 2009..Iron release from the C-lobe is most affected by the presence of the sTFR and changes in pH, but is unaffected by the conformation of the N-lobe. A model for iron release from diferric hTF is provided to delineate our findings... - Effect of glycosylation on the function of a soluble, recombinant form of the transferrin receptorShaina L Byrne
Department of Biochemistry, University of Vermont College of Medicine, Burlington, Vermont 05405-0068, USA
Biochemistry 45:6663-73. 2006..6 reveals that only the N317D mutant has a significant effect. The carbohydrate at position 317 lies close to a region of the TFR previously shown to interact with hTF... - Inequivalent contribution of the five tryptophan residues in the C-lobe of human serum transferrin to the fluorescence increase when iron is releasedNicholas G James
Department of Biochemistry, College of Medicine, University of Vermont, 89 Beaumont Avenue, Burlington 05405, Vermont, USA
Biochemistry 48:2858-67. 2009..Excitation at 295 nm (Trp only) and at 280 nm (Trp and Tyr) reveals interesting and significant differences in the rate constants for the complex... - 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 releasePeter J Halbrooks
Department of Biochemistry, University of Vermont, College of Medicine, Burlington, Vermont 05405, USA
Biochemistry 44:15451-60. 2005..The studies collectively highlight important features common to both the N- and C-lobes of TF and the critical role of the receptor in iron release... - Intrinsic fluorescence reports a global conformational change in the N-lobe of human serum transferrin following iron releaseNicholas G James
Department of Biochemistry, University of Vermont, Burlington, Vermont 05405, USA
Biochemistry 46:10603-11. 2007.... - Incorporation of 5-hydroxytryptophan into transferrin and its receptor allows assignment of the pH induced changes in intrinsic fluorescence when iron is releasedNicholas G James
Department of Biochemistry, University of Vermont College of Medicine, 89 Beaumont Avenue, Burlington, VT 05405 0068, USA
Biochim Biophys Acta 1794:532-40. 2009..Quantum yield determinations of TFR, Fe(C) hTF and the Fe(C) hTF/TFR complex strongly support our interpretation of the kinetic data... - Properties of a homogeneous C-lobe prepared by introduction of a TEV cleavage site between the lobes of human transferrinAshley N Steere
Department of Biochemistry, University of Vermont, College of Medicine, 89 Beaumont Avenue, Burlington, VT 05405, USA
Protein Expr Purif 72:32-41. 2010..The spectral and kinetic properties of the isolated C-lobe differ significantly from those of the isolated N-lobe... - Differential effect of a his tag at the N- and C-termini: functional studies with recombinant human serum transferrinAnne B Mason
Department of Biochemistry, University of Vermont, College of Medicine, Burlington, Vermont 05405, USA
Biochemistry 41:9448-54. 2002..Thus, the presence of a His tag at either the N- or C-terminus of hTF-NG has no apparent effect on the ability of these hTF species to bind to transferrin receptors... - Identification of a kinetically significant anion binding (KISAB) site in the N-lobe of human serum transferrinShaina L Byrne
Department of Biochemistry, University of Vermont College of Medicine, 89 Beaumont Avenue, Burlington, Vermont 05405, USA
Biochemistry 49:4200-7. 2010..This is the first identification of an authentic KISAB site in the N-lobe of hTF. The effect of the single R143A mutation on the kinetic profile of iron release provides a dramatic illustration of the dynamic nature of hTF... - Excited-state lifetime studies of the three tryptophan residues in the N-lobe of human serum transferrinNicholas G James
Department of Biochemistry, University of Vermont, College of Medicine, Burlington, Vermont 05405, USA
Protein Sci 19:99-110. 2010..e., static quenching. The results of these experiments provide quantitative data strongly suggesting that Förster resonance energy transfer is not the sole source of Trp quenching in the N-lobe of hTF... - Protocol to determine accurate absorption coefficients for iron-containing transferrinsNicholas G James
Department of Biochemistry, College of Medicine, University of Vermont, Burlington, VT 05405, USA
Anal Biochem 378:202-7. 2008.... - The low pKa value of iron-binding ligand Tyr188 and its implication in iron release and anion binding of human transferrinXuesong Sun
Department of Chemistry, University of Hong Kong, Hong Kong, China
FEBS Lett 573:181-5. 2004..These data indicate that Tyr188 is a critical residue not only for iron binding but also for chelator binding and iron release in transferrin... - Structural and functional consequences of binding site mutations in transferrin: crystal structures of the Asp63Glu and Arg124Ala mutants of the N-lobe of human transferrinHeather M Baker
School of Biological Sciences, University of Auckland, Private Bag 92019, Auckland, New Zealand
Biochemistry 42:7084-9. 2003..In both cases, the weakened Fe-N(His) bond may also contribute, consistent with protonation of the His ligand being an early intermediate step in iron release, following the protonation of the carbonate ion... - Interlobe communication in human serum transferrin: metal binding and conformational dynamics investigated by electrospray ionization mass spectrometryDmitry R Gumerov
Department of Chemistry, University of Massachusetts, 710 North Pleasant Street, Amherst, Massachusetts, 01003, USA
Biochemistry 42:5421-8. 2003..The experimental results provide strong support for the earlier suggestion that hTF interacts with its receptor (TFR) primarily through the C-lobe both at the cell surface and inside the endosome... - The molecular mechanism for receptor-stimulated iron release from the plasma iron transport protein transferrinAnthony M Giannetti
Division of Biology 114-96, California Institute of Technology, Pasadena, California 91125, USA
Structure 13:1613-23. 2005.... - Identification of the epitope of a monoclonal antibody that disrupts binding of human transferrin to the human transferrin receptorEvelyn M Teh
Department of Biochemistry and Molecular Biology and Centre for Blood Research, University of British Columbia, Vancouver, Canada
FEBS J 272:6344-53. 2005..In agreement with other studies, these epitope mapping studies support a role for residues in the C1 domain of hTF in receptor binding... - Inhibition of transferrin iron release increases in vitro drug carrier efficacyBert J Lao
Department of Bioengineering, University of California, Los Angeles, CA 90095, USA
J Control Release 117:403-12. 2007..06 nM for the oxalate Tf conjugate vs. 0.22 nM for the native Tf conjugate. Thus, we show that inhibition of Tf iron release improves the efficacy of Tf as a drug carrier through increased association with cells expressing TfR... - A novel murine protein with no effect on iron homoeostasis is homologous with transferrin and is the putative inhibitor of carbonic anhydraseFudi Wang
Division of Hematology Oncology, Children s Hospital Boston, and Harvard Medical School, Boston, MA 02115, USA
Biochem J 406:85-95. 2007..Lastly, we note that this member of the TF superfamily is a relatively recent addition resulting from a tandem duplication event... - The crystal structure of iron-free human serum transferrin provides insight into inter-lobe communication and receptor bindingJeremy Wally
NIDDK, National Institutes of Health, Bethesda, Maryland 20892, USA
J Biol Chem 281:24934-44. 2006..In addition, we evaluate potential interactions between apo-hTF and the human transferrin receptor... - Indirect detection of protein-metal binding: interaction of serum transferrin with In3+ and Bi3+Mingxuan Zhang
Department of Chemistry, University of Massachusetts at Amherst, Amherst, Massachusetts 01003, USA
J Am Soc Mass Spectrom 15:1658-64. 2004.... - Evolution of the transferrin family: conservation of residues associated with iron and anion bindingLisa A Lambert
Department of Biology, Chatham College, Woodland Road, Pittsburgh, PA 15232, USA
Comp Biochem Physiol B Biochem Mol Biol 142:129-41. 2005.... - Structures of two mutants that probe the role in iron release of the dilysine pair in the N-lobe of human transferrinHeather M Baker
School of Biological Sciences, University of Auckland, Private Bag 92019, Auckland, New Zealand
Acta Crystallogr D Biol Crystallogr 63:408-14. 2007....
Research Grants
- IRON DELIVERY VIA BLOOD--STRUCTURAL ROLE OF TRANSFERRINAnne Mason; Fiscal Year: 2001..The fundamentals of structure-function relationships in transferrin are essential to understanding the molecular basis of certain defects in iron delivery and to the design of rational interventions in the delivery of iron to neoplasms. ..
- Iron Delivery via Blood; Structure Role of TransferrinAnne B Mason; Fiscal Year: 2010..Owing to the fact that iron deficiency and excess are directly related to specific human diseases, understanding this process at the molecular level is essential to a global understanding of iron metabolism. ..
- Iron Delivery via Blood; Structure Role of TransferrinAnne Mason; Fiscal Year: 2009..Owing to the fact that iron deficiency and excess are directly related to specific human diseases, understanding this process at the molecular level is essential to a global understanding of iron metabolism. ..
- IRON DELIVERY VIA BLOOD; STRUCTURAL ROLE OF TRANSFERRINAnne Mason; Fiscal Year: 2005..abstract_text> ..
- Iron Delivery via Blood; Structure Role of TransferrinAnne Mason; Fiscal Year: 2009..Owing to the fact that iron deficiency and excess are directly related to specific human diseases, understanding this process at the molecular level is essential to a global understanding of iron metabolism. ..