| First Author | Schwer H | Year | 1997 |
| Journal | Biochem Biophys Res Commun | Volume | 233 |
| Issue | 1 | Pages | 117-20 |
| PubMed ID | 9144407 | Mgi Jnum | J:39668 |
| Mgi Id | MGI:87022 | Doi | 10.1006/bbrc.1997.6413 |
| Citation | Schwer H, et al. (1997) Molecular cloning and characterization of a novel putative carboxylesterase, present in human intestine and liver. Biochem Biophys Res Commun 233(1):117-20 |
| abstractText | A full-length cDNA coding for a putative intestinal carboxylesterase (iCE) was isolated from a human small intestine cDNA library. The cDNA has an open reading frame of 559 amino acids with up to 65% homology to other carboxylesterases of different mammalian species. The deduced amino-acid sequence contains many structural features, that are highly conserved among all carboxylesterase isoenzymes, like the serine esterase active site, an ER-retention signal and one Asn-Xxx-Thr site for N-linked carbohydrate addition. Northern blot analysis revealed that the corresponding mRNA is 3.4-3.6 kb in size and is preferentially expressed in human intestine with a weak signal also in liver. Analysis of cells from the gastrointestinal tract unveiled site-specific, transcriptional regulation of iCE, with higher expression in small intestine and lower expression in colon and rectum. The high expression in small intestine is attributable to a higher expression in jejunum compared to duodenum and ileum. |
