Cloning of a cDNA encoding rat aldehyde dehydrogenase with high activity for retinal oxidation

Gene. 1995 Dec 12;166(2):303-6. doi: 10.1016/0378-1119(96)81752-5.


Retinoic acid (RA), an important regulator of cell differentiation, is biosynthesized from retinol via retinal by a two-step oxidation process. We previously reported the purification and partial amino acid (aa) sequence of a rat kidney aldehyde dehydrogenase (ALDH) isozyme that catalyzed the oxidation of 9-cis and all-trans retinal to corresponding RA with high efficiency [Labrecque et al. Biochem. J. 305 (1995) 681-684]. A rat kidney cDNA library was screened using a 291-bp PCR product generated from total kidney RNA using a pair of oligodeoxyribonucleotide primers matched with the aa sequence. The full-length rat kidney ALDH cDNA contains a 2315-bp (501 aa) open reading frame (ORF). The aa sequence of rat kidney ALDH is 89, 96 and 87% identical to that of the rat cytosolic ALDH, the mouse cytosolic ALDH and human cytosolic ALDH, respectively. Northern blot and RT-PCR-mediated analysis demonstrated that rat kidney ALDH is strongly expressed in kidney, lung, testis, intestine, stomach and trachea, but weakly in the liver.

MeSH terms

  • Aldehyde Dehydrogenase / genetics*
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • DNA Primers / chemistry
  • DNA, Complementary / genetics
  • Gene Expression
  • Kidney / enzymology
  • Molecular Sequence Data
  • Oxidation-Reduction
  • RNA, Messenger / genetics
  • Rats
  • Retinaldehyde / metabolism*
  • Substrate Specificity
  • Tissue Distribution


  • DNA Primers
  • DNA, Complementary
  • RNA, Messenger
  • Aldehyde Dehydrogenase
  • Retinaldehyde

Associated data

  • GENBANK/L42009