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| Wayne Albers, Ph.D., Senior Investigator |
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Dr. Albers received a B.S. degree in chemistry at the University of Nebraska and a Ph.D. in pharmacology under Dr. Oliver Lowry, working on the development and applications of quantitative biochemical techniques. In 1954 he joined the National Institute of Neurological Diseases in the Section on Neurocytology under Dr. Sanford Palay, during which time he began studies of the metabolism and distribution of the GABA enzymes in brain. After joining the Laboratory of Neurochemistry under Dr. Donald Tower he began work on the mechanism of sodium transport, which continues to be his principle scientific interest. After teaching neurochemistry at George Washington Medical School and at FAES, he and three colleagues organized the collaborative textbook, Basic Neurochemistry which continues under the sponsorship of the American Society for Neurochemistry.w
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Research Interests:
The major research effort of this section is to extend our knowledge of the molecular events underlying ion transport. The "biomachines" that perform these functions belong principally to the P-type ATP-dependent transporter family. A major ion transport system of most animal cells is the ATP-dependent sodium pump, which occurs in plasma membranes and couples the metabolic energy of ATP to the extrusion of 3 Na+ and uptake of 2 K+. Many cell processes depend on the resultant transmembrane concentration gradients of Na+ and K+ as a source of free energy. In the nervous system, most neurotransmitter uptake systems are powered by the Na+ gradient. The K+ gradient is the primary determinant of the "resting" membrane potential of most neurons and the Na+ gradient is the driving force for their principal depolarizing currents. The energy used by sodium pumps to maintain these gradients in brain is estimated to require about 50% of the total cerebral energy production.
The principal questions currently under investigation are:
1.Do subunit interactions participate in energy transduction of P-type pumps?
2.Do hydration forces play a prominent role in pump conformational transitions?
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Selected Recent Publications:
Zheng YL Li BS Amin ND Albers W Pant HC (2002) A peptide derived from cyclin-dependent kinase activator (p35) specifically inhibits Cdk5 activity and phosphorylation of tau protein in transfected cells, Eur J Biochem 269, 4427-34.
Full Text/Abstract
Contact Information:
Dr. Wayne Albers
Enzyme Chemistry Section
Laboratory of Neurochemistry, NINDS
Building 49, Room 3A82
49 Convent Drive MSC 4479
Bethesda, MD 20892-4479
Telephone: (301) 496-1673 (office),
(301) 496-1673 (laboratory),
(301) 496-1339 (fax)
Email: rwalbers@helix.nih.gov
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