Molecular cloning and characterization of a novel putative carboxylesterase, present in human intestine and liver.
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Schwer H, Langmann T, Daig R, Becker A, Aslanidis C, Schmitz G
Molecular cloning and characterization of a novel putative carboxylesterase, present in human intestine and liver.
Biochem Biophys Res Commun. 1997 Apr 7;233(1):117-20.
- PubMed ID
- 9144407 [ View in PubMed]
- Abstract
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.