High impact information on Akr7a3

• We have cloned and sequenced a cDNA encoding an aldehyde reductase (AFB1-AR), which is expressed in rat liver in response to dietary ethoxyquin [1].
• Alignment of the amino acid sequence of AFB1-AR with other known and putative aldehyde reductases shows that it defines a subfamily within the aldo-keto reductase superfamily [1].
• The relative importance of AFB1-AR and the glutathione-S-transferase Yc2 subunit in conferring resistance to aflatoxin B1 is discussed [2].
• Kidney contains high constitutive levels of AFB1-AR and the administration of EQ increases its concentration in renal cytosol about 3-fold [2].
• By contrast with rAFAR1, which comprises 327 amino acids, rAFAR2 contains 367 amino acids [3].

Associations of Akr7a3 with chemical compounds

• Western blot analysis showed that DADS is a potent inducer of glutathione S-transferase A5 (rGSTA5) and AFB(1) aldehyde reductase 1 (rAFAR1), while DAS is a weak inducer of these enzymes [4].

Regulatory relationships of Akr7a3

• Besides its distinct electrophoretic and immunochemical properties, rAFAR2 appears to be regulated differently from rAFAR1 as it is expressed in most rat tissues and does not appear to be induced by ethoxyquin [5].

Analytical, diagnostic and therapeutic context of Akr7a3

• The distinct subcellular localization of the rAFAR1 and rAFAR2 subunits was confirmed by immunocytochemistry in H4IIE cells [3].
• Herein, we report the molecular cloning of rAFAR2, showing that it shares 76% sequence identity with rAFAR1 [3].

References