Schwer, Heinz and Langmann, Thomas and Daig, Rosemarie and Becker, Alfred and Aslanidis, Charalampos and Schmitz, Gerd (1997) Molecular cloning and characterization of a novel putative carboxylesterase, present in human intestine and liver. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 233 (1). pp. 117-120. ISSN 0006-291X, 1090-2104
Full text not available from this repository.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. (C) 1997 Academic Press.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ACYL-COENZYME-A; CHOLESTEROL ESTERASE; RAT-LIVER; MICROSOMAL CARBOXYLESTERASES; ENDOPLASMIC-RETICULUM; PROTEINS; SEQUENCE; ACYLTRANSFERASE; MEMBRANE; CDNA |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Innere Medizin I Medicine > Lehrstuhl für Klinische Chemie und Laboratoriumsmedizin |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 11 May 2023 08:40 |
| Last Modified: | 11 May 2023 08:40 |
| URI: | https://pred.uni-regensburg.de/id/eprint/50886 |
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