{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,22]],"date-time":"2026-03-22T18:06:48Z","timestamp":1774202808238,"version":"3.50.1"},"reference-count":47,"publisher":"Elsevier BV","issue":"11","license":[{"start":{"date-parts":[[2012,11,1]],"date-time":"2012-11-01T00:00:00Z","timestamp":1351728000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"crossref","award":["21590342"],"award-info":[{"award-number":["21590342"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100007591","name":"Akiyama Life Science Foundation","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100007591","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biochimica et Biophysica Acta (BBA) - General Subjects"],"published-print":{"date-parts":[[2012,11]]},"DOI":"10.1016\/j.bbagen.2012.07.003","type":"journal-article","created":{"date-parts":[[2012,7,20]],"date-time":"2012-07-20T16:47:09Z","timestamp":1342802829000},"page":"1787-1796","source":"Crossref","is-referenced-by-count":39,"title":["In vivo role of aldehyde reductase"],"prefix":"10.1016","volume":"1820","author":[{"given":"Motoko","family":"Takahashi","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Satoshi","family":"Miyata","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Junichi","family":"Fujii","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yoko","family":"Inai","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shigemitsu","family":"Ueyama","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Motoko","family":"Araki","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tomoyoshi","family":"Soga","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Reiko","family":"Fujinawa","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chiaki","family":"Nishitani","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shigeru","family":"Ariki","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Takeyuki","family":"Shimizu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tomomi","family":"Abe","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yoshito","family":"Ihara","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Morimitsu","family":"Nishikimi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yasunori","family":"Kozutsumi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Naoyuki","family":"Taniguchi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yoshio","family":"Kuroki","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.bbagen.2012.07.003_bb0005","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/0167-4838(82)90402-2","article-title":"Purification and properties of human liver aldehyde reductases","volume":"707","author":"Petrash","year":"1982","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbagen.2012.07.003_bb0010","doi-asserted-by":"crossref","first-page":"9547","DOI":"10.1016\/S0021-9258(18)60566-6","article-title":"The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases","volume":"264","author":"Bohren","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0015","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1107\/S0907444993004044","article-title":"Crystallization and preliminary structure determination of porcine aldehyde reductase from two crystal forms","volume":"49","author":"El-Kabbani","year":"1993","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0020","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1016\/S0009-2797(02)00193-X","article-title":"The aldo-keto reductase superfamily homepage","volume":"143\u2013144","author":"Hyndman","year":"2003","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0025","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/0304-4165(90)90175-V","article-title":"Metabolism of 3-deoxyglucosone, an intermediate compound in the Maillard reaction, administered orally or intravenously to rats","volume":"1035","author":"Kato","year":"1990","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbagen.2012.07.003_bb0030","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1111\/j.1432-1033.1991.tb15921.x","article-title":"Purification and characterization of NADPH-dependent 2-oxoaldehyde reductase from porcine liver. A self-defence enzyme preventing the advanced stage of the Maillard reaction","volume":"197","author":"Liang","year":"1991","journal-title":"Eur. J. Biochem."},{"issue":"Pt 3","key":"10.1016\/j.bbagen.2012.07.003_bb0035","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1042\/bj2790903","article-title":"Aldehyde reductase is a major protein associated with 3-deoxyglucosone reductase activity in rat, pig and human livers","volume":"279","author":"Kanazu","year":"1991","journal-title":"Biochem. J."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0040","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/0378-1119(93)90728-L","article-title":"Identity of a major 3-deoxyglucosone-reducing enzyme with aldehyde reductase in rat liver established by amino acid sequencing and cDNA expression","volume":"127","author":"Takahashi","year":"1993","journal-title":"Gene"},{"key":"10.1016\/j.bbagen.2012.07.003_bb0045","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1093\/jb\/mvj017","article-title":"The internalization and metabolism of 3-deoxyglucosone in human umbilical vein endothelial cells","volume":"139","author":"Sakiyama","year":"2006","journal-title":"J. Biochem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0050","doi-asserted-by":"crossref","first-page":"4364","DOI":"10.1016\/S0021-9258(18)42844-X","article-title":"Reduction of trioses by NADPH-dependent aldo-keto reductases. Aldose reductase, methylglyoxal, and diabetic complications","volume":"267","author":"Vander Jagt","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0055","doi-asserted-by":"crossref","first-page":"3758","DOI":"10.1016\/S0021-9258(19)84914-1","article-title":"Aging of proteins: immunological detection of a glucose-derived pyrrole formed during Maillard reaction in vivo","volume":"264","author":"Hayase","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0060","doi-asserted-by":"crossref","first-page":"1102","DOI":"10.1172\/JCI115690","article-title":"Immunohistochemical detection of advanced glycosylation end products in diabetic tissues using monoclonal antibody to pyrraline","volume":"89","author":"Miyata","year":"1992","journal-title":"J. Clin. Invest."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0065","doi-asserted-by":"crossref","first-page":"20275","DOI":"10.1016\/S0021-9258(17)31987-7","article-title":"Increase in 3-deoxyglucosone levels in diabetic rat plasma. Specific in vivo determination of intermediate in advanced Maillard reaction","volume":"269","author":"Yamada","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0070","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1006\/bbrc.1996.1157","article-title":"Induction of apoptotic cell death by methylglyoxal and 3-deoxyglucosone in macrophage-derived cell lines","volume":"225","author":"Okado","year":"1996","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0075","doi-asserted-by":"crossref","first-page":"18453","DOI":"10.1074\/jbc.272.29.18453","volume":"272","author":"Che","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0080","doi-asserted-by":"crossref","first-page":"32299","DOI":"10.1016\/S0021-9258(18)31635-1","article-title":"Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with N alpha-acetylarginine, N alpha-acetylcysteine, and N alpha-acetyllysine, and bovine serum albumin","volume":"269","author":"Lo","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0085","doi-asserted-by":"crossref","first-page":"28228","DOI":"10.1074\/jbc.270.47.28228","article-title":"Free radicals generated during the glycation reaction of amino acids by methylglyoxal. A model study of protein-cross-linked free radicals","volume":"270","author":"Yim","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0090","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1080\/1071576021000041005","article-title":"Identification of the binding site of methylglyoxal on glutathione peroxidase: methylglyoxal inhibits glutathione peroxidase activity via binding to glutathione binding sites Arg 184 and 185","volume":"37","author":"Park","year":"2003","journal-title":"Free Radic. Res."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0095","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/j.cell.2005.11.024","article-title":"Methylglyoxal modification of mSin3A links glycolysis to angiopoietin-2 transcription","volume":"124","author":"Yao","year":"2006","journal-title":"Cell"},{"key":"10.1016\/j.bbagen.2012.07.003_bb0100","doi-asserted-by":"crossref","first-page":"24031","DOI":"10.1016\/S0021-9258(18)54387-8","article-title":"Expression of human aldose and aldehyde reductases. Site-directed mutagenesis of a critical lysine 262","volume":"266","author":"Bohren","year":"1991","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0105","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1111\/j.1742-4658.2006.05607.x","article-title":"Vitamin C. Biosynthesis, recycling and degradation in mammals","volume":"274","author":"Linster","year":"2007","journal-title":"FEBS J."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0110","doi-asserted-by":"crossref","first-page":"618","DOI":"10.1093\/oxfordjournals.jbchem.a127352","article-title":"Enzymic studies on TPN l-hexonate dehydrogenase from rat liver","volume":"49","author":"Mano","year":"1961","journal-title":"J. Biochem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0115","doi-asserted-by":"crossref","first-page":"2933","DOI":"10.1016\/S0021-9258(19)41576-7","article-title":"Properties of the nicotinamide adenine dinucleotide phosphate-dependent aldehyde reductase from pig kidney. Amino acid composition, reactivity of cysteinyl residues, and stereochemistry of d-glyceraldehyde reduction","volume":"250","author":"Flynn","year":"1975","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0120","doi-asserted-by":"crossref","first-page":"3821","DOI":"10.1016\/S0021-9258(17)40325-5","article-title":"Purification and properties of NADPH-dependent aldehyde reductase from human liver","volume":"252","author":"Wermuth","year":"1977","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0125","doi-asserted-by":"crossref","first-page":"19510","DOI":"10.1074\/jbc.M110.110247","article-title":"Ascorbate synthesis pathway: dual role of ascorbate in bone homeostasis","volume":"285","author":"Gabbay","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0130","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1002\/ijc.2910620617","article-title":"Elevation of aldose reductase gene expression in rat primary hepatoma and hepatoma cell lines: implication in detoxification of cytotoxic aldehydes","volume":"62","author":"Takahashi","year":"1995","journal-title":"Int. J. Cancer"},{"key":"10.1016\/j.bbagen.2012.07.003_bb0135","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1111\/j.1349-7006.1996.tb00227.x","article-title":"Induction of aldose reductase gene expression in LEC rats during the development of the hereditary hepatitis and hepatoma","volume":"87","author":"Takahashi","year":"1996","journal-title":"Jpn. J. Cancer Res."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0140","doi-asserted-by":"crossref","first-page":"5723","DOI":"10.1073\/pnas.0511225103","article-title":"Senescence marker protein 30 functions as gluconolactonase in l-ascorbic acid biosynthesis, and its knockout mice are prone to scurvy","volume":"103","author":"Kondo","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0145","doi-asserted-by":"crossref","first-page":"16768","DOI":"10.1074\/jbc.M601876200","article-title":"Differential metabolomics reveals ophthalmic acid as an oxidative stress biomarker indicating hepatic glutathione consumption","volume":"281","author":"Soga","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0150","doi-asserted-by":"crossref","first-page":"10731","DOI":"10.1074\/jbc.M610717200","article-title":"Roles of hemoglobin Allostery in hypoxia-induced metabolic alterations in erythrocytes: simulation and its verification by metabolome analysis","volume":"282","author":"Kinoshita","year":"2007","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0155","first-page":"189","article-title":"Kinetic studies on NADPH-linked aldehyde reductase from human liver","volume":"132","author":"Wermuth","year":"1980","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0160","doi-asserted-by":"crossref","first-page":"443","DOI":"10.1007\/978-1-4615-5871-2_50","article-title":"Aldehyde reductase. Catalytic mechanism and substrate recognition","volume":"414","author":"Barski","year":"1997","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0165","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1006\/abbi.1998.0721","article-title":"Aldehyde reductase: the role of C-terminal residues in defining substrate and cofactor specificities","volume":"355","author":"Rees-Milton","year":"1998","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0170","doi-asserted-by":"crossref","first-page":"13685","DOI":"10.1016\/S0021-9258(17)36884-9","article-title":"Cloning and chromosomal mapping of the human nonfunctional gene for l-gulono-gamma-lactone oxidase, the enzyme for l-ascorbic acid biosynthesis missing in man","volume":"269","author":"Nishikimi","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0175","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1097\/00062752-200001000-00012","article-title":"Expression and function of serum amyloid A, a major acute-phase protein, in normal and disease states","volume":"7","author":"Urieli-Shoval","year":"2000","journal-title":"Curr. Opin. Hematol."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0180","doi-asserted-by":"crossref","first-page":"832","DOI":"10.1093\/jn\/128.5.832","article-title":"Ascorbic acid deficiency changes hepatic gene expression of acute phase proteins in scurvy-prone ODS rats","volume":"128","author":"Ikeda","year":"1998","journal-title":"J. Nutr."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0185","doi-asserted-by":"crossref","first-page":"28","DOI":"10.3177\/jnsv.52.28","article-title":"Ascorbic acid deficiency stimulates hepatic expression of inflammatory chemokine cytokine-induced neutrophil chemoattractant-1, in scurvy-prone ODS rats","volume":"52","author":"Horio","year":"2006","journal-title":"J. Nutr. Sci. Vitaminol. (Tokyo)"},{"key":"10.1016\/j.bbagen.2012.07.003_bb0190","doi-asserted-by":"crossref","first-page":"1433","DOI":"10.1021\/bi00004a038","article-title":"In vivo glycation of aldehyde reductase, a major 3-deoxyglucosone reducing enzyme: identification of glycation sites","volume":"34","author":"Takahashi","year":"1995","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbagen.2012.07.003_bb0195","doi-asserted-by":"crossref","first-page":"1","DOI":"10.2337\/diabetes.48.1.1","article-title":"Role of oxidative stress in diabetic complications: a new perspective on an old paradigm","volume":"48","author":"Baynes","year":"1999","journal-title":"Diabetes"},{"key":"10.1016\/j.bbagen.2012.07.003_bb0200","doi-asserted-by":"crossref","first-page":"14775","DOI":"10.1016\/S0021-9258(18)63766-4","article-title":"Cloning and sequence determination of human placental aldose reductase gene","volume":"264","author":"Chung","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0205","doi-asserted-by":"crossref","first-page":"9788","DOI":"10.1016\/S0021-9258(19)38740-X","article-title":"Cloning and expression of human aldose reductase","volume":"265","author":"Nishimura","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0210","doi-asserted-by":"crossref","first-page":"24841","DOI":"10.1016\/S0021-9258(18)35840-X","article-title":"The crystal structure of the aldose reductase. NADPH binary complex","volume":"267","author":"Borhani","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0215","doi-asserted-by":"crossref","first-page":"469","DOI":"10.1038\/355469a0","article-title":"Novel NADPH-binding domain revealed by the crystal structure of aldose reductase","volume":"355","author":"Rondeau","year":"1992","journal-title":"Nature"},{"key":"10.1016\/j.bbagen.2012.07.003_bb0220","first-page":"593","article-title":"Erythrocyte aldose reductase activity and sorbitol levels in diabetic retinopathy","volume":"14","author":"Reddy","year":"2008","journal-title":"Mol. Vis."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0225","doi-asserted-by":"crossref","first-page":"793","DOI":"10.1161\/CIRCRESAHA.109.200568","article-title":"Aldose reductase protects against early atherosclerotic lesion formation in apolipoprotein E-null mice","volume":"105","author":"Srivastava","year":"2009","journal-title":"Circ. Res."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0230","doi-asserted-by":"crossref","first-page":"36328","DOI":"10.1074\/jbc.M306593200","article-title":"Rapid stimulation of free glucuronate formation by non-glucuronidable xenobiotics in isolated rat hepatocytes","volume":"278","author":"Linster","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbagen.2012.07.003_bb0235","doi-asserted-by":"crossref","first-page":"F200","DOI":"10.1152\/ajprenal.00411.2004","article-title":"Developmental expression and function of aldehyde reductase in proximal tubules of the kidney","volume":"289","author":"Barski","year":"2005","journal-title":"Am. J. Physiol. Renal Physiol."}],"container-title":["Biochimica et Biophysica Acta (BBA) - General Subjects"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0304416512002000?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0304416512002000?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,1,22]],"date-time":"2022-01-22T12:06:32Z","timestamp":1642853192000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0304416512002000"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,11]]},"references-count":47,"journal-issue":{"issue":"11","published-print":{"date-parts":[[2012,11]]}},"alternative-id":["S0304416512002000"],"URL":"https:\/\/doi.org\/10.1016\/j.bbagen.2012.07.003","relation":{},"ISSN":["0304-4165"],"issn-type":[{"value":"0304-4165","type":"print"}],"subject":[],"published":{"date-parts":[[2012,11]]}}}