| First Author | Hansis C | Year | 1998 |
| Journal | Eur J Biochem | Volume | 258 |
| Issue | 1 | Pages | 53-60 |
| PubMed ID | 9851691 | Mgi Jnum | J:51470 |
| Mgi Id | MGI:1316799 | Doi | 10.1046/j.1432-1327.1998.2580053.x |
| Citation | Hansis C, et al. (1998) The gene for the Alzheimer-associated beta-amyloid-binding protein (ERAB) is differentially expressed in the testicular Leydig cells of the azoospermic by w/w(v) mouse. Eur J Biochem 258(1):53-60 |
| abstractText | In order to discover possible new testicular paracrine factors involved in the establishment of spermatogenesis, a modified differential display reverse transcription, polymerase chain reaction (DDRT-PCR) procedure was used to detect gene transcripts preferentially expressed in the testes of the azoospermic w/w(v) mutant mouse. One of the differentially expressed gene products showed partial similarity to members of the short-chain alcohol dehydrogenase family of enzymes. This cDNA fragment was used to obtain the full-length mouse cDNA sequence, which initially showed moderate similarity to a 20beta- steroid dehydrogenase from lower organisms, and later shown to have >85% similarity to a novel endoplasmic-reticulum-associated-binding protein (ERAB) from the human brain, implicated in Alzheimer's disease. A recently cloned bovine sequence also of high similarity suggests that this molecule might also represent an isozyme of 3-hydroxyacyl-CoA dehydrogenase. Using the mouse cDNA as probe, northern hybridization showed enrichment of the transcript to the testicular Leydig cells, and showed a specific approximately 20-fold enrichment in the azoospermic mouse testis. The level of the testicular ERAB transcript does not seem to change through puberty, suggesting that a lack of germ cells alone is not responsible for the up-regulation in the w/w(v) testis. Using the three-dimensional coordinates of the published 20beta- hydroxysteroid dehydrogenase structure as template, it was additionally possible to construct a molecular model of the novel protein which showed it to have a very similar structure to this enzyme, including the substrate-binding domain. |
