Regular Article
Molecular Cloning and Characterization of a Novel Putative Carboxylesterase, Present in Human Intestine and Liver

https://doi.org/10.1006/bbrc.1997.6413Get rights and content

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.

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    W. B. Jakoby, Ed.

    1

    To whom correspondence should be addressed at Institute for Clinical Chemistry and Laboratory Medicine, University of Regensburg, Franz-Josef-Strauß-Allee 11, D-93042 Regensburg, Germany. Fax: (+49)-941-944-6202; E-mail: [email protected] burg.de.

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