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jennings.jpg (41358 bytes)Michael L. Jennings
Professor and Chair
Ph.D., Harvard University
Office: (501) 296-1438
Lab: (501) 296-1439
Email: JenningsMichaelL@uams.edu

My research is focused on the structure, function, and regulation of ion transport proteins. The present focus is on sulfate transporters and the regulation of the pathway for sulfation of macromolecules.  Mutations in a specific sulfate transporter known as DTDST (diastrophic dysplasia sulfate transporter) are known to cause abnormalities in bone and cartilage formation in humans.  It is believed that the abnormalities are caused by undersulfation of glycosaminoglycan produced by chondrocytes and osteoblasts under conditions of low sulfate transport activity by DTDST.  We are in the process of determining the mechanisms by which mammalian chondrocytic and osteoblastic cells regulate the sulfation pathway in response to transport inhibition or of low extracellular sulfate.  A separate project is focused on a closely related protein (Sul2p) in yeast; this protein is tightly regulated by sulfur-containing compounds in the growth medium.  An understanding of this regulation can potentially lead to the discovery of the mechanisms by which eukaryotic cells can sense sulfate and other anions.

Dr. Jennings' Laboratory Homepage

Representative Publications

Jennings, M.L. (2005) Evidence for a second binding/transport site for chloride in erythrocyte anion transporter AE1 modified at Glutamate 681.  Biophys. J. 88: 2681-2691.

Mardach, R., J. Zempleni, B. Wolf, M.J. Cannon, M.L Jennings, S. Cress, J. Boylan, S. Roth, S.  Cederbaum, and D.M. Mock (2002)  Biotin dependency due to a defect in biotin transport.  J. Clin. Invest. 109: 1617-1623.

Kuma, H., A.A. Shinde, T.R. Howren, and M.L. Jennings (2002) Topology of the anion exchange protein AE1: the controversial sidedness of Lysine 743. Biochemistry 41: 3380-3388.

Deen, P.M.T., B.W.M. van Balkom, P.J.M. Savelkoul, E.-J. Kamsteeg, M. van Raak, M.L Jennings, T.R. Muth, V. Rajendran, and M.J. Caplan. (2002). The C-terminus of Aquaporin-2 COOH terminus is necessary, but not sufficient, for routing to the apical membrane. Am. J. Physiol. Renal, 282:F330-F340.

Jennings, M.L. and M.F. Adame (2001) Direct estimate of 1:1 stoichiometry of the erythrocyte K+-Cl- cotransporter. Am. J. Physiol. (Cell Physiol.) 281:C825-C832.

Link to Dr. Jennings at PubMed

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