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By Trevor M. Penning, J. Mark Petrash

content material: part 1: basic review ; 1. creation and evaluate of the Aldo-Keto Reductase (AKR) Superfamily ; part 2: AKRS AND ENDOGENOUS TOXICANTS ; 2. Aldo-Keto Reductase-Catalyzed Detoxication of Endogenous Aldehydes linked to Diabetic issues ; three. Aldose Reductase Detoxifies Lipid Aldehydes and Their Glutathione Conjugates ; four. function of Aldose Reductase within the cleansing of Oxidized Phospholipids ; part three: AKRS AND EXOGENOUS TOXICANTS: TOBACCO comparable cancer agents ; five. Competing Roles of Reductases within the detoxing of the Tobacco-Specific Nitrosamine Ketone NNK ; 6. Aldo-Keto Reductases and the Metabolic Activation of Polycyclic fragrant Hydrocarbons ; 7. Molecular Cloning and Characterization of Dihydrodiol Dehydrogenase from Mouse ; eight effective Synthesis of the energetic Metabolites of Carcinogenic Polycyclic fragrant Hydrocarbons ; nine. Chemistry of PAH o-Quinones Generated via the AKR Pathway of PAH Activation ; 10. research of Etheno-2'-Deoxyguanosine Adducts as Dosimeters of AKR Mediated Oxidative rigidity ; part four: AKRS AND EXOGENOUS TOXICANTS: MYCOTOXINS, ALDEHYDES AND KETONES ; eleven. Aflatoxin Aldehyde Reductases ; 12. Competing Reactions of Aflatoxin B1-Dialdehyde: Enzymatic aid vs Adduction with Lysine ; thirteen. using mammalian telephone strains to enquire the position of aldo-keto reductases within the detoxication of aldehydes and ketones ; part five: AKRS, the tension reaction AND mobilephone SIGNALING ; 14. Aldose Reductase and the strain reaction ; 15. Aldose Reductase Regulates Reactive Oxygen Species Mediated-Inflammatory signs ; sixteen. Aldo-Keto Reductases within the tension reaction of the Budding Yeast Saccharomyces cerevisiae

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Royer, R. E. Adv. Exp. 1996, 414, 491-497. ; ACS Symposium Series; American Chemical Society: Washington, DC, 2003. ch002 35 29. Kolb, N. ; Hunsaker, L. ; Vander Jagt, D. L. Mol. Pharmacol. 1994, 45, 797-801. 30. Vander Jagt, D. ; Kolb, N . ; Vander Jagt, T. ; Martinez, F. E. Biochim. Biophys. Acta 1995, 1249, 117126. 31. Vander Jagt, D. ; Hunsaker, L. ; Vander Jagt, T. ; Gomez, M . ; Gonzales, D. M . ; Deck, L. M . ; Royer, R. E. Biochem. Pharmacology 1997, 53, 1133-1140. 33. Wilson, D. ; Bohren, K.

Vander Jagt, D. L. Mol. Pharmacol. 1994, 45, 797-801. 30. Vander Jagt, D. ; Kolb, N . ; Vander Jagt, T. ; Martinez, F. E. Biochim. Biophys. Acta 1995, 1249, 117126. 31. Vander Jagt, D. ; Hunsaker, L. ; Vander Jagt, T. ; Gomez, M . ; Gonzales, D. M . ; Deck, L. M . ; Royer, R. E. Biochem. Pharmacology 1997, 53, 1133-1140. 33. Wilson, D. ; Bohren, K. ; Gabbay, K. ; Quiocho, F. A. Science 1992, 257, 81-84. 34. ; Ginell, S. ; Myles, D. ; DeLucas, L. G. Nat. Struct. Biol. 1995, 2, 687-692. 35. ; O'Donoghue, S.

Adapted in partfromdata in Reference 27. Role of Glutathione in AKR1A1 and AKR1B1-Catalyzed Reactions Glutathione reacts non-enzymatically with MeG to form the hemithioacetal. Thus intracellular MeG is an equilibrium mixture of free and hydrated MeG along with the glutathione-MeG hemithioacetal (Figure 2). ; ACS Symposium Series; American Chemical Society: Washington, DC, 2003. 30 catalyze the reduction of the aldehyde functional group of MeG to produce acetol as well as the ketone of the hemithioacetal to produce the hemithioacetal of lactaldehyde, which can then form lactaldehyde (39).

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