Lauren Peirol
Research Mentor: Ruma Banerjee
Mentor Department: Biological Chemistry, Medicine
Author(s): Joesph Brake, Lauren Peirol
Session: Session 5 (2:00 PM – 2:50 PM)
Presentation Type: Poster 50
Abstract
Hydrogen sulfide (H 2 S), which is endogenously produced by mammalian cells by the transsulfuration pathway, can both power and poison mitochondrial respiration. Cells lining the colon are additionally exposed to high H 2 S levels originating from gut microbial metabolism. High levels of H 2 S poison cellular respiration by inhibiting complex IV in the electron transport chain (ETC). To prevent respiratory poisoning, cells rely on the H 2 S detoxification pathway, in which sulfide quinone oxidoreductase (SQOR) initiates H 2 S oxidation and couples to the ETC. At low H 2 S levels, SQOR feeds electrons into the ETC to power cellular respiration. Both increased H 2 S exposure and defective H 2 S oxidation machinery result in H 2 S accumulation and toxicity. Heat shock proteins (HSPs) are stress-responsive markers that are upregulated in response to metabolic and mitochondrial stress. In an ongoing study, we are quantifying the upregulation of select HSPs, e.g. HSP70, HSP27, CLPB (selection guided by a proteomics dataset) in response to H2S exposure and/or SQOR knockdown in multiple colon cell lines. HSP protein expression is being assessed by Western blotting followed by quantitative analysis of protein expression normalized to loading controls. The extent to which key HSPs are upregulated under H 2 S stress is discussed and builds a foundation for exploring the poorly understood role of HSPs in maintaining cellular health in response to H 2 S exposure.
