By Trevor M. Penning, J. Mark Petrash
content material: part 1: basic assessment ; 1. creation and assessment 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 problems ; three. Aldose Reductase Detoxifies Lipid Aldehydes and Their Glutathione Conjugates ; four. position of Aldose Reductase within the detoxing of Oxidized Phospholipids ; part three: AKRS AND EXOGENOUS TOXICANTS: TOBACCO comparable cancer causing agents ; five. Competing Roles of Reductases within the cleansing 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 relief vs Adduction with Lysine ; thirteen. using mammalian phone strains to enquire the position of aldo-keto reductases within the detoxication of aldehydes and ketones ; part five: AKRS, the tension reaction AND cellphone SIGNALING ; 14. Aldose Reductase and the tension reaction ; 15. Aldose Reductase Regulates Reactive Oxygen Species Mediated-Inflammatory indications ; sixteen. Aldo-Keto Reductases within the rigidity reaction of the Budding Yeast Saccharomyces cerevisiae
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Content material: part 1: common assessment ; 1. creation and review 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.
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Conklin, D. ; Liu, S. ; Prakash, N . ; Boor, P. ; Srivastava, S. ; Bhatnagar A. Atherosclerosis 2001, 158, 339-350. 38. ; Dixit, B. ; Hurst, H. ; Srivastava, S. K. Free Radic. Biol. Med. 2000, 29, 642-651. 39. Ramana, K. ; Aggarwal, B. ; Srivastava, S. K. J. Biol. Chem. 2002, 277, 32063-32070. 40. ; Liu, S. ; Runge, M. ; Bhatnagar, A. Arterioscler Thromb. 2000, 20, 1745-1752. ; ACS Symposium Series; American Chemical Society: Washington, DC, 2003. Chapter 4 Role of Aldose Reductase in the Detoxification of Oxidized Phospholipids 1 2 2 Sanjay Srivastava , Kota V.
That AR remains partially inhibited in euglycemic tissues by an NO-dependent mechanism is supported by our observation that inhibiting NO synthesis in normal rodents results in increased sorbitol accumulation (24). However, most of the enzyme is free and displays kinetic properties similar to the enzyme completely reduced in vitro, and it remains highly sensitive to inhibition by sorbinil or tolrestat. ; ACS Symposium Series; American Chemical Society: Washington, DC, 2003. ch003 43 mechanism of keeping the polyol pathway in check when glucose availability is limited.
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). Thus, with MeG as substrate AKR1B1 is both an aldehyde and a ketone reductase. Both lactaldehyde and acetol can be reduced further to propananediol, catalyzed by AKR1B1, again demonstrating the ability of AKR1B1 to function as a ketone reductase.