The Daily Bulletin Archive

Melissa Boler, a master's degree candidate in forensic science at Buffalo State, will present her master's defense seminar, "Hsp110 and Hsp7 in Wild Type and 11485 Drosophila When Exposed to Stressful Environments," at 12:30 p.m. Thursday, October 16, in Classroom Building B119. Light refreshments will be served before the seminar. This event is supported by the Faculty-Student Association.

Abstract
Heat shock proteins are a type of molecular chaperone protein that are significant in assisting in the refolding of denatured proteins and escorting terminally misfolded proteins to the proteasomes for degradation. Parkinson’s, Alzheimer’s, and Polyglutamine diseases (e.g., Huntington’s disease) are all diseases that can be caused by aggregation of misfolded proteins, so clearance of the misfolding proteins is essential. The over-expression of heat shock protein Hsp70 along with co chaperone Hsp110 plays a vital role in many of these neurological diseases.

The protein expression levels of wild type and 11485 Drosophila lysates were observed in this study. 11485 Drosophila differ from the wild type Drosophila in that they are heterozygous for the hsc70Cb⁰⁰⁰⁸² disruption allele. The protein expression levels from western blots probed with antibodies of Hsp70 and Hsp110 were compared under stress-induced environments by heat shocking the lysates. The western blot data was also compared to mRNA data from q RT-PCR to understand the gene expression regulation with these specific proteins.

Findings suggested that female 11485 Drosophila over-compensated not only when heat shocked but also under non heat shock conditions, an unexpected finding. They also suggested that these genes are most likely regulated at the transcription level. Understanding how the heat shock proteins, specifically the Hsp70 family, work is the key to future studies that might lead to therapeutic and drug discoveries of many neurological diseases.