Department Chair

M. Scott Goodman, Ph.D., Chair and Associate Professor of Chemistry

Date of Award

5-2015

Access Control

Campus-Only Access

Degree Name

Forensic Science, M.S.

Department

Chemistry Department

Advisor

Douglas P. Easton, Ph.D., Reseach Professor of Biology

Department Home page

http://chemistry.buffalostate.edu/forensic-science-ms-6

First Reader

Douglas P. Easton, Ph.D., Research Professor of Biology

Second Reader

M. Scott Goodman, Ph.D., Chair and Associate Professor of Chemistry

Third Reader

Derek L. Beahm, Ph.D., Research Assistant Professor of Biology

Abstract

Heat shock proteins are a class of molecular chaperone protein that assist in the refolding of misfolded proteins and escorting terminally misfolded (or aggregated) proteins to the proteasomes for degradation. Parkinson’s, Alzheimer’s, and Polyglutamine diseases such as Huntington’s disease are all diseases that can be caused by aggregation of misfolded proteins. Therefore clearance of misfolded proteins is essential.

In this study, western blotting was performed to investigate the Hsp70 and Hsp70Cb/Hsp110 protein expression levels of wild type and 11485 Drosophila that are heterozygous for the hsc70Cb00082 P element disruption allele, under normal and heat shock conditions. The western blots were scanned and quantitated. These data were compared to the corresponding Hsp70 and Hsc70Cb mRNA quantitation by q RT-PCR. This allowed examination of the contributions of transcriptional and translational control of Hsp70 and Hsp70Cb/Hsp110 gene regulation.

The results of these experiments suggested that female 11485 Drosophila over-compensated for the disruption of one Hsc70Cb allele by overexpression of both Hsc70Cb and Hsp70. These results while unexpected are supported by similar results obtained from measurements of hsc70Cb and Hsp70 mRNA levels by qRT-PCR. The comparison of protein and mRNA levels for the two heat shock proteins also suggested that their levels are most likely regulated at the transcriptional level. Understanding how the levels of heat shock proteins are regulated both with respect to response to the loss of one allele and to the proteotoxic effects of heat shock is important in understanding the possible role of reduced chaperoning capacity in aging and in diseases characterized by protein misfolding and aggregation.

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