B.S., University of Hartford (1972)
Ph.D., Syracuse University (1977)
003 Winston Hall
(336) 758-5318
browne@wfu.edu
Go to my personal page
Areas of Interest
Cell and Developmental Biology, Cytoskeleton, Cell Cycle
| Carole L. Browne | |
| Professor
of Biology B.S., University of Hartford (1972) Go to my personal page |
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Areas of Interest Cell and Developmental Biology, Cytoskeleton, Cell Cycle |
Research
The role of estrogen in the regulation of the leptin receptor
The hormone leptin is produced by adipocytes (fat cells) and acts on receptors in the hypothalamus to reduce food consumption and increase energy expenditure.
There is considerable interest in leptin because mutations in the leptin gene are associated with obesity in rodents and humans. Leptin has also been shown to
play a role in reproduction through regulation of the release of gonadotropin-releasing hormone. The receptor for leptin is found in a variety of tissues and exists in a number of isoforms, membrane bound and soluble.
The membrane bound, or long form, of the receptor triggers an intracellular signaling pathway upon binding of leptin. The functions of the short and soluble forms of the receptor are not clear.
Blood leptin levels are higher in women than in men, and evidence suggests that leptin receptor
expression and/or soluble leptin receptor secretion are regulated by changing levels of estrogen or reproductive state.
Working with Dr. Gloria Muday, also of the Biology Department, I am investigating the role of estrogens in regulation of the
isoforms of the leptin receptor, using cultured mouse 3T3 LI adipocytes and HEK cells that have been transfected with a leptin receptor-GFP construct.
When a cell is injured or subjected to potentially harmful changes in its environment, it expresses genes that code for proteins that prevent and repair damage to other cellular proteins. Among these proteins is heat shock protein Hsp70. Working with Dr. Michael Tytell in the Department of Neuroanatomy, I am studying the ability of exogenously applied Hsp70 to protect rat embryonic spinal cord motor neurons against oxidative damage. Cell health is assessed by assays of programmed cell death or apoptosis, measures of mitochondrial function, and observations of axonal transport. In addition, we are comparing the efficacy of two different forms of Hsp70, one a human recombinant form and the other derived from alfalfa.
Hsp proteins are highly conserved, and alfalfa Hsp70 offers an alternative form of the protein for the development of clinical applications.
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Selected Publications Browne, C.L. Tobin, J.R. and, Voytko, M L (2009) Effects of two years of conjugated equine estrogens on cholinergic neurons in young and middle-aged monkeys. Brain Research. (in press) Browne, C.L., Swan, J.B., Rankin, E.E., Calvert, H. Griffiths, S. and Tytell, M. (2007) Extracellular heat shock protein 70 has novel functional effects on sea urchin eggs and coelomocytes. J. Exp. Biol. 210:1275-1287 Silver, W.L. and Browne, C.L. (2000) Integration of laboratory exercises in development and neurobiology courses using the Xenopus oocyte expression xsystem. J. Industrial Microbiol. Biotech. 24:353-358. Browne, C.L., Creton R., Karplus, E., Mohler, P.M., Palazzo, R.E., and Miller A.L. 1996. Analysis of the Calcium Transient at NEB During the First Cell Cycle in Dividing Sea Urchin Eggs. Biol. Bull. 191:5-16. Browne, C.L., Miller, A.L., Palazzo, R.E., and Jaffe, L.F. 1992. On the calcium pulse during nuclear envelope breakdown (NEB) in sea urchin eggs. Biol. Bull. 183:370-372. Browne, C.L., Bower, W.A., Palazzo, R.E. and Rebhun, L.I. 1990. Inhibition of mitosis in fertilized sea urchin eggs by inhibition of the cAMP-dependent protein kinase. Exp. Cell Res. 188:122-128. |
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