Biology Department |
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Dr. Lee WeberProfessorMolecular Biology; structure and expression of human stress protein genes, function of the heat shock proteins in stress resistance. |
Montclair State College, Montclair, NJ
1968, B.A. Biology
University of Connecticut, Storrs, CT
1970, M.S. Genetics
1975, Ph.D. Cell Biology
State University of New York at Albany, Albany, NY
1974 - 1977, Postdoctoral Training
Cells of all known organisms respond to
physiological stress by increased synthesis of heat shock or
stress proteins. Accumulation of stress proteins induced by
exposure to mild stress results in a transient state of stress
resistance. The goal of our laboratory is to understand how heat
shock proteins function in normal cell physiology and in the
development of cellular stress resistance. Our approach has been
to construct cell lines that over express individual heat shock
protein genes. Most of our work has focused on the low molecular
weight heat shock protein, hsp27. Stable transfected rodent cells
that over express human hsp27 in the absence of other stress
proteins exhibit enhanced stress resistance. Recent evidence
suggests that phosphorylation of hsp27 mediates heat resistance
by stabilizing cytoplasmic F-actin filaments. Directed
mutagenesis is now being used to define the role of the stress
protein in this process.
We have recently become interested in using stress protein gene
expression as a biomarker for environmental stress. We have
cloned several salmon heat shock protein cDNAs, expressed the
recombinant proteins, and prepared specific antibodies. These
reagents are being used to monitor stress levels in Lahonton
Cutthroat trout and in Chinook salmon exposed to thermal
pollution.
Lavoie, J.N., E. Hickey, L.A. Weber and J.L. Landry. 1993.
Involvement of heat shock protein 27 in microfilament dynamics
and growth factor signal transduction. J. Biol. Chem. 268:24210.
Lavoie, J.N., H. Lambert, E. Hickey, L.A. Weber and J. Landry.
1995. Regulation of cellular
thermoresistance and actin polymerization activity by
phosphorylation-induced changes in
the oligomeric structure of heat shock protein 27. Mol. Cell
Biol. 15:505.
Piotrowicz, R.S., L.A. Weber, E. Hickey and E.G. Levin. 1995.
Accelerated growth and senescence of arterial endothelial cells
expressing the small molecular weight heat shock protein, hsp27.
FASEB J. 9:1079.
Larsen, J. K., W.T. Gerthoffer, E. Hickey and L.A. Weber. 1995.
Cloning and sequencing of a cDNA encoding the canine HSP27
protein. Gene 161:305.
Richards, E.H., Hickey, E., Weber, L.A., and Masters, J.R.W., The
effect of overexpression of the small heat shock protein, HSP27,
on the heat and drug sensitivities of human testis tumor cells.
Cancer Research 56:2446-2451 (1996) .
Oesterreich, S., Fuqua, S., Weber, L.A., and Hickey, E., Basal
regulatory promoter elements of the HSP27 gene in human breast
cancer cells. Biochem. Biophys. Res. Comm. 222:155-163 (1996)
Street address
University of Nevada, Reno Biology Department m/s 314 Reno, NV
89557
Electronic mail address
weber@unr.edu
Web address
http://www.scsr.nevada.edu/~bioweb/weber.html
Office phone
775-784-4484
FAX number
775-784-1302