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. doi: 10.1006/bbrc.1997.6413.


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.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Carboxylesterase
  • Carboxylic Ester Hydrolases / genetics*
  • Cloning, Molecular
  • DNA, Complementary
  • Humans
  • Intestine, Small / enzymology*
  • Liver / enzymology*
  • Molecular Sequence Data
  • RNA, Messenger / genetics
  • Sequence Homology, Amino Acid


  • DNA, Complementary
  • RNA, Messenger
  • Carboxylic Ester Hydrolases
  • Carboxylesterase

Associated data

  • GENBANK/Y09616