Rat prominin, like its mouse and human orthologues, is a pentaspan membrane glycoprotein.
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
Abstract
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.
Details
Original language | English |
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Pages (from-to) | 939-944 |
Number of pages | 6 |
Journal | Biochemical and biophysical research communications |
Volume | 285 |
Issue number | 4 |
Publication status | Published - Jul 2001 |
Peer-reviewed | Yes |
External IDs
PubMed | 11467842 |
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Scopus | 0034811912 |