| First Author | Steele EC | Year | 1998 |
| Journal | Gap Junctions | Pages | 289-293 |
| Mgi Jnum | J:49492 | Mgi Id | MGI:1277597 |
| Citation | Steele EC, et al. (1998) Identification of a mutation in the connexin 50 (Cx50) gene of the No2 cataractous mouse mutant. Gap Junctions :289-293 |
| abstractText | The purpose of this study was to screen the entire Cx50 (MP70) protein coding region of the No2 (nuclear opacity #2) mouse mutant for a mutation that was linked to and consistent with the observed cataractous phenotype. Genomic DNA's were prepared from both mutant and normal, parental spleens. DNA oligonucleotides were designed and used to amplify the entire Cx50 coding region, including the upstream splice acceptor site from these DNA's via PCR. PCR products were gel purified and then directly sequenced. A single A-->C transversion was observed in the coding strand of the mutant DNA. This DNA substitution results in the nonconservative amino acid substitution of Ala for the normally encoded Asp in a conserved domain of the encoded polypeptide. The DNA alteration also creates a restriction site not present in the wild type DNA sequence. This was used to corroborate the sequence data. A mutation has been identified in the Cx50 gene of the No2 mouse mutant. This mutation is both linked to and consistent with the observed cataractous phenotype, as it is only present in mutant DNA and is predicted to alter a conserved domain of the ocular-specific membrane protein encoded by the gene. These results indicate that Cx50 plays an important role in normal lens development and maintenance and heralds its gene as a likely candidate in human congenital, hereditary cataract. |
