You are here

Dr. Douglas D. McAbee

Brief Biosketch

  • PhD, University of Texas Southwestern Medical School (Dallas); Cell Biology; Advisor, Dr. Fred Grinnell (1984)
  • Post-doctoral fellow, Department of Human Biological Chemistry & Genetics, University of Texas Medical Branch (Galveston); Advisor, Dr. Paul H. Weigel (1989)
  • Assistant Professor, Department of Biological Sciences, University of Notre Dame, 1997

Teaching Interests

  • CHEM 441A/B, Introductory Biochemistry lecture courses
  • CHEM 443, Biochemistry Laboratory course
  • CHEM 541, core course for biochemistry graduate students
  • CHEM 548, Cell Membranes

Research Interests

I have had a long-standing interest in hepatic iron metabolism, cell membranes, and endocytosis. My work has focused on hepatic metabolism of the iron-binding protein lactoferrin and the lactoferrin receptor on hepatocytes, the C-type rat hepatic lectin (RHL; aka, the asialoglycoprotein receptor or galactosyl receptor). We have found that lactoferrin interacts with the major subunit of RHL independent of lactoferrins carbohydrates yet which requires the lectin activity of RHL. We have also found that binding determinants on lactoferrin that mimic a RHL-recognized carbohydrate are present in both N- and C-lobes of lactoferrin. The molecular structure recognized by RHL on lactoferrin remains to be identified. We have also found that acute iron overload induces up-regulates RHL protein expression. Overload of hepatocytes with Fe3+, Cu+ or Zn2+ interferes with normal recycling and ligand-binding activity of RHL.

Recent Publications

  • McAbee, D.D. 2001 "Lactoferrin" in Wiley Encylopedia of Molecular Medicine, Wiley & Sons, New York (ISBN 0-471-37494-6), pp 1894-1897.
  • McAbee, D.D., Jiang, X., and Walsh, K.B. 2000 Lactoferrin binding to the rat asialoglycoprotein receptor requires the receptor's lectin properties. Biochem. J. 348:113-117.
  • McAbee, D.D. and Jiang, X. 1999 Copper and zinc ions differentially block asialoglycoprotein receptor-mediated endocytosis in isolated rat hepatocytes. J. Biol. Chem. 274:14750-14758.
  • McAbee, D.D., Bennatt, D.J., and Ling, Y.Y. 1998 Isolated rat hepatocytes bind and internalize lactoferrins via the asialoglycoprotein receptor by a galactose-independent mechanism. Adv. Exper. Med. Biol. 443:113-121.
  • Sitaram, M., Moloney, B, and McAbee, D.D. 1998 Prokaryotic expression of bovine lactoferrin deletion mutants that bind to the Ca2+-dependent lactoferrin receptor on isolated rat hepatocytes. Prot. Expr. Purif.14:229-236.
  • McAbee, D.D., Ling, Y.Y., and Stich, C. 1998 Iron loading of isolated rat hepatocytes inhibits asialoglycoprotein receptor dynamics and induces formation of rat hepatic lectin-1 (RHL-1) oligomers. Biochem. J.331:719-726.
  • Bennatt, D.J., Ling, Y.Y., and McAbee, D.D. 1997 Isolated rat hepatocytes bind lactoferrins by the RHL-1 subunit of the asialoglycoprotein receptor in a galactose-independent manner. Biochemistry 36:8367-8376.
  • Bennatt, D.J., and McAbee, D.D. 1997 Identification and isolation of a 45 kDa calcium-dependent lactoferrin receptor from rat hepatocytes. Biochemistry 36:8359-8366.
  • Sitaram, M.P., and McAbee, D.D. 1997 Isolated rat hepatocytes bind and endocytose differentially the N- and C-lobes of bovine lactoferrin. Biochem. J. 323:815-822.
  • McAbee, D.D. and Ling, Y.Y. 1997 Iron loading of cultured adult rat hepatocytes reversibly enhances lactoferrin binding and endocytosis. J. Cell. Physiol. 171:75-86.