Anne B. Mason, PhD, University of Vermont

Anne B. Mason, PhD

Anne B. Mason, Ph.D.

The Mason lab's research seeks to mechanistically understand iron release from the individual lobes of human serum transferrin and ovotransferrin, especially in a complex with their respective receptors. The Mason research group believes that both lobes of transferrin interact with each other and with the receptor to bring about release of this vital metal. The lab focuses on making site-directed mutants for which spectral properties (UV-vis and EPR) and the rate constants for iron release in the presence and absence of recombinant soluble transferrin receptor (as a function of pH and anion concentration) can be measured. Authentic monoferric and apo-transferrins provide essential controls.

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References

  1. Byrne, S. L., R. Leverence, J.S. Klein, A.M. Giannetti, V.C. Smith, R.T.A. MacGillivray, I.A. Kaltashov, and A.B. Mason, â??Effect of glycosylation on the function of a soluble, recombinant form of the transferrin receptor, Biochemistry 45, 6663-6673 (2006).
  2. Byrne, S.L., N. D. Chasteen, A. N. Steere and A.B. Mason, 'The unique kinetics of iron release from transferrin: The role of receptor, lobe-lobe interactions, and salt at endosomal pH â??.J. Mol Biol 396, 130-140 (2010).
  3. Eckenroth, B.E., A.N. Steere, N. Dennis Chasteen and S. J. Everse, and A.B. Mason, 'How the binding of human transferrin primes the transferrin receptor potentiating iron release at endosomal pH', Proc. Natl. Acad. Sci, USA, 108, 13089-13094 (2011).
  4. Steere, A.N., B.F. Miller, S.E. Roberts, S.L. Byrne, N. D. Chasteen, V.C. Smith, R.T.A. MacGillivray and A.B. Mason, 'Ionic residues of human serum transferrin affect binding to the transferrin receptor and iron release', Biochemistry, 51, 686-694 (2012).