2nd Floor, Room # 282
- Cardiovascular & Metabolic Diseases Graduate Program Track (CVMD)
- CeDER - Center for Diabetes and Endocrine Research
Health Science Campus
Block Health Science Building
2nd Floor, Room # 282
|Professor and Education Director
Phone: (419) 383-4182, 383-4125
FAX: (419) 383-2871
- B.Sc., Biochemistry, 1974, University of Bristol, Bristol, Avon, England
- Ph.D., Biochemistry, 1977, University of Bristol, Bristol, Avon, England
- Research Associate, Pharmacology, Medical University of Ohio,1982-1984
- Assistant Professor of Pharmacology, Medical University of Ohio, 1984-1991
- Associate Professor Department of Physiology and Pharmacology, University of Toledo College of Medicine, Health Science Campus, 1991-2010
- Professor Department of Physiology and Pharmacology, University of Toledo College of Medicine, Health Science Campus, 2011-present
- Director of the Cardiovascular and Metabolic Diseases (CVMD) Track of Biomedical Sciences Graduate Program, 2007-present
- Mitochondrial bioenergetics and transport processes.
Mitochondria are cellular organelles responsible for the synthesis of ATP. The coupling mechanism of oxidative phosphorylation involves the generation of a large protonmotive force across the inner membrane by the H+ pumps of the respiratory chain. In addition to being the immediate source of energy for ATP synthesis, the protonmotive force has a great influence on the transport of anions and cations across the inner membrane, and in a number of cases the membrane potential itself is used to drive transport. Most of my research has been devoted to the study of these electrophoretic transport processes. I have studied two transport pathways, an anion uniporter which is also called the inner membrane anion channel (IMAC) and a cation uniporter which transports K+ and other cations. The anion uniporter enables mitochondria to pump out salts and the K+ uniporter allows salts to be pumped in. Controlling the balance between these processes is the essence of mitochondrial volume homeostasis. I have carried out studies with intact mitochondria investigating the effects of physiological and pharmacological regulators and chemical modification on the properties of IMAC. We have used electrophysiological methods to examine the properties of channels extracted from mitochondria and reconstituted into planar lipid bilayers.Representative Publications:
- Beavis, A.D. and Powers, M.F. (1989): On the regulation of the mitochondrial inner membrane anion channel by magnesium and protons. J. Biol. Chem. 264:17148-17155.
- Beavis, A.D. (1989): The mitochondrial inner membrane anion channel possesses two mercurial-reactive regulatory sites. Eur. J. Biochem. 185:511-519.
- Powers, M.F. and Beavis, A.D. (1991): Triorganotins inhibit the mitochondrial inner membrane anion channel. J. Biol. Chem. 266:17250-17256.
- Beavis, A.D. (1992): Properties of the inner membrane anion channel in intact mitochondria (Review). J. Bioenerg. Biomembr. 24:77-90.
- Beavis, A.D. and Vercesi, A.E. (1992): Anion uniport in plant mitochondria is mediated by a Mg2+-insensitive inner membrane anion channel. J. Biol. Chem. 267:3079-3087.
- Beavis, A.D., Lu, Y. and Garlid, K.D. (1993): On the regulation of K+ uniport in intact mitochondria by adenine nucleotides and nucleotide analogs. J. Biol. Chem. 268:997-1004.
- Powers, M.F., Smith, L.L. and Beavis, A.D. (1994): On the relationship between the mitochondrial inner membrane anion channel and the adenine nucleotide translocase. J. Biol. Chem. 269: 10614-10620.
- Welihinda, A. A., Beavis, A. D., and Trumbly, R. J. (1994): Mutations in LISI (ERG6) gene confer increased sodium and lithium uptake in saccharomyces cerevisiae. Biochim. Biophys. Acta 1193: 107-117.
- Beavis, A. D. (1994): A Channel Model to Explain Regulation of the Mitochondrial Inner Membrane Anion Channel. In "Molecular Biology of Mitochondrial Transport Systems" (Eds., M. Forte and M. Colombini), Springer- Verlag, Berlin Heidelberg, pp. 137-151.
- Beavis, A.D. and Davatol-Hag, H. (1996): The Mitochondrial Inner Membrane Anion Channel is Inhibited by DIDS. J. Bioenerg. Biomembr. 28: 207- 214.
- Liu, G., Hinch, B., Davatol-Hag, H., Lu, Y., Powers, M., and Beavis, A. D. (1996): Temperature Dependence of the Mitochondrial Inner Membrane Anion Channel: The Relationship Between Temperature and Inhibition by Protons. J. Biol. Chem. 271: 19717-19723.
- Liu, G., Hinch, B., and Beavis, A. D. (1996): Mechanisms for the Transport of alpha,omega Dicarboxylates Through the Mitochondrial Inner Membrane. J. Biol. Chem. 271: 25338-25344.
- Lu, Y. and Beavis, A. D. (1997): Effect of Leader Peptides on the Permeability of Mitochondria. J. Biol. Chem. 272: 13555-13561.
- Beavis, A.D. and Powers, M. (2004) Temperature dependence of the mitochondrial inner membrane anion channel: The relationship between temperature and inhibition by magnesium. J. Biol. Chem. 279:4045-4050.