A novel flexible baseband processor architecture framework

Srivastava, Harshit; Sk, Noor Mahammad

doi:10.1109/spin.2014.6777007

Cited by 1 publication

(1 citation statement)

References 14 publications

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“…8 The primary role of GSTs in PAH metabolism is thought to be the glutathione conjugation of PAH metabolites, such as epoxides and diol epoxides. [9][10][11][12][13][14][15] Induction of GST expression is thought to be caused by changes in redox conditions; for instance, one study showed that the Aryl hydrocarbon receptor (Ahr) mediated little induction of GSTs, and that induction via NFE2-related factor 2 (Nrf2) is much more potent. 16 Previously, GST induction by polycyclic aromatic hydrocarbons (PAHs) has been measured by determining mRNA levels, by western blotting for protein abundance, via GSH-agarose column enriched samples, and/or by GST activity via simple colorimetric assays.…”

Section: Introductionmentioning

confidence: 99%

Benzo[a]pyrene Induction of Glutathione S-Transferases: An Activity-Based Protein Profiling Investigation

Stoddard

Killinger

Nag

et al. 2019

Chem. Res. Toxicol.

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Polycyclic aromatic hydrocarbons (PAHs) are ubiquitous environmental contaminants generated from combustion of carbon-based matter. Upon ingestion these molecules can be bioactivated by cytochrome P450 monooxygenases to oxidized toxic metabolites. Some of these metabolites are potent carcinogens that can form irreversible adducts with DNA and other biological macromolecules. Conjugative enzymes, such as glutathione S-transferases or UDPglucuronosyltransferases, are responsible for the detoxification and/or facilitate the elimination of these carcinogens. While responses to PAH exposures have been extensively studied for the bioactivating cytochrome P450 enzymes, much less is known regarding the response of glutathione S-transferases in mammalian systems. In this study, we investigated the expression and activity responses of murine hepatic glutathione S-transferases to benzo[a]pyrene exposure using global proteomics and activity-based protein profiling for chemoproteomics, respectively. Using this approach, we identified several enzymes exhibiting increased activity including GSTA2, M1, M2, M4, M6, and P1. The activity of one GST enzyme, GSTA4, was found to be downregulated with increasing B[a]P dose. Activity responses of several of these enzymes were identified as *

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