| First Author | Bhat PV | Year | 1995 |
| Journal | Gene | Volume | 166 |
| Issue | 2 | Pages | 303-6 |
| PubMed ID | 8543180 | Mgi Jnum | J:31079 |
| Mgi Id | MGI:78549 | Doi | 10.1016/0378-1119(96)81752-5 |
| Citation | Bhat PV, et al. (1995) Cloning of a cDNA encoding rat aldehyde dehydrogenase with high activity for retinal oxidation. Gene 166(2):303-6 |
| abstractText | 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. |
