The stress protein response (SPR) is a conserved and ubiquitous mechanism that enables cells to tolerate a wide variety of environmental insults. This response involves the preferential synthesis of an array of proteins with different molecular weights. These proteins perform a variety of functions, such as protein folding, multimeric protein assembly, steroid receptor binding, and heme catabolism.
To evaluate the potential use of the SPR as a biomonitoring tool, a stepwise plan was utilized that proceeded through various physical and chemical laboratory exposures and culminated with a field validation study. The goals of the laboratory exposures were threefold: (1) determine the time required for induction of the SPR; (2) determine the dose-responsiveness of the SPR; and (3) compare the increased syntheses and accumulations of stress proteins to classical toxicological endpoints (i.e. percent mortality, LC50, LC1, etc).
| Identifer | oai:union.ndltd.org:unt.edu/info:ark/67531/metadc798352 |
| Date | 05 1900 |
| Creators | Dyer, Scott Douglas |
| Publisher | University of North Texas |
| Source Sets | University of North Texas |
| Language | English |
| Detected Language | English |
| Type | Thesis or Dissertation |
| Format | Text |
| Rights | Public, Copyright, Copyright is held by the author, unless otherwise noted. All rights |
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