Comparing Heat Shock Protein Levels Between Similar Species of Different Longevity
Heat shock proteins are involved in the hormetic response to mild levels of molecular damage, such as that induced by heat, in which cells increase their housekeeping and maintenance activities. If the damage is mild then the end result is a net gain: cells remain on alert and tissues are kept more free of damage and functional than would otherwise be the case. This ultimately translates into greater healthy longevity, and this effect can be observed by measuring levels of heat shock proteins in similar species with different life spans:
The longevity of an organism is directly related to its ability to effectively cope with cellular stress. Heat shock response (HSR) protects the cells against accumulation of damaged proteins after exposure to elevated temperatures and also in aging cells. To understand the role of Hsp70 in regulating life span of Daphnia, we examined the expression of Hsp70 in two ecotypes that exhibit strikingly different life spans.Daphnia pulicaria, the long lived ecotype, showed a robust Hsp70 induction as compared to the shorter lived Daphnia pulex. Interestingly, the short-lived D. pulex isolates showed no induction of Hsp70 at the mid point in their life span. In contrast to this, the long-lived D. pulicaria continued to induce Hsp70 expression at an equivalent age.
We further show that the Hsp70 expression was induced at transcriptional level in response to heat shock. The transcription factor responsible for Hsp70 induction, heat shock factor-1 (HSF-1), although present in aged organisms did not exhibit DNA-binding capability. Thus, the decline of Hsp70 induction in old organisms could be attributed to a decline in HSF-1's DNA-binding activity. These results for the first time, present a molecular analysis of the relationship between HSR and life span in Daphnia.