| First Author | Corbeil D | Year | 2001 |
| Journal | Biochem Biophys Res Commun | Volume | 285 |
| Issue | 4 | Pages | 939-44 |
| PubMed ID | 11467842 | Mgi Jnum | J:70732 |
| Mgi Id | MGI:2138052 | Doi | 10.1006/bbrc.2001.5271 |
| Citation | Corbeil D, et al. (2001) Rat prominin, like its mouse and human orthologues, is a pentaspan membrane glycoprotein. Biochem Biophys Res Commun 285(4):939-44 |
| abstractText | Mouse prominin is the first characterized member of a novel family of membrane glycoproteins. It displays a characteristic membrane topology with five transmembrane segments and two large glycosylated extracellular loops. Prominin orthologues and paralogues have been identified in human, fish, fly, and worm. Recently, a cDNA sequence encoding the rat homologue of mouse prominin has been reported [Zhu et al. (2001) Biochem. Biophys. Res. Commun. 281, 951-956]. Surprisingly, due to a single nucleotide deletion that shifts the reading frame and introduces a premature stop codon, the protein predicted from this cDNA would correspond to a C-terminally truncated form of prominin with only four transmembrane segments. Here we report evidence that is in contrast to the report of Zhu et al. (2001). We isolated a rat prominin cDNA devoid of any frameshift mutation, demonstrate that rat prominin, like the other mammalian prominins, is a full-length 120-kDa pentaspan membrane glycoprotein, and have not been able to detect any C-terminally truncated form of rat prominin. Copyright 2001 Academic Press. |
