The Daily Bulletin Archive

Please join the Great Lakes Center, the Biology Department, and the Great Lakes ecosystem science program for the seminar "Expression and Localization of Heat Shock Protein 110 during Drosophila Development: Clues to Its Roles in Embryonic Development," presented by Douglas Easton, research professor in the Biology Department at Buffalo State, today, April 17, from 4:00 to 5:15 p.m. in Bulger Communication Center East 2. All students, staff, and faculty are welcome.

Abstract
Heat shock proteins (HSPs) are a class of proteins that protect cells against environmental conditions that damage proteins. When cells undergo extreme environmental stresses, for example, heat shock, proteins can fold incorrectly or denature. Unfolded or misfolded proteins can form aggregates that interfere with cellular functions and lead to cell death. Cells respond to such stressful conditions by the synthesis of a set of heat shock proteins. Some HSPs have cognates (HSC) continually expressed in the cell. HSC and HSP molecules are identified by their molecular weights, for example, the 70 kilo Dalton heat shock protein is hsp70, and its cognate is hsc70.

Because HSPs and HSCs bind to their substrates to prevent interactions between unfolded proteins—or in order to fold, refold, or transport them—they are referred to as “molecular chaperones.” There is a complex set of molecular chaperones in all cells. These chaperones form a functionally interacting network that regulates the folding, unfolding, transport, and assembly into cellular structures and degradation of the full assemblage of cellular proteins.

Hsp110 is constitutive molecular chaperone that is not as well understood as some other hsp's. It cooperates with a number of other molecular chaperones, particularly hsp70, in the folding, transport, and degradation of cellular proteins. Since the chaperone network is so important to protein integrity and function, key chaperones may have special functions in developing embryos. We have begun to investigate the expression and localization of hsp110 in developing embryos to find clues to its developmental function.

We have investigated the regulation of hsp110 expression and the localization of hsp110 in Drosophila embryos by measuring location and quantize the expression of green florescent protein (GFP) tagged hsp110 during development. We have measured the timing and the expression of the hsp110 by quantizing the fluorescent hsp110 throughout development. Hsp110 was also shown to be inducible by heat shock. The changed cellular location of hsp110 was followed with confocal fluorescence microscopy. We have also observed differential concentration of hsp110 in embryonic structures. The above and other findings are related to the findings of other researchers. We have discovered novel correlations between our findings and those from other researchers. Further, our results lead to the conclusion that hsp110 may have multiple developmental functions in Drosophila and also protects embryos from environmental stresses that they encounter in the field.