Cloning and sequencing of a novel murine liver carboxylesterase cDNA

Biochim Biophys Acta. 1998 Apr 29;1397(2):175-9. doi: 10.1016/s0167-4781(98)00023-2.

Abstract

Carboxylesterases (EC 3.1.1.1) comprise a group of serine hydrolases with at least 20 genetically distinct loci in mice. Here, we describe differential display PCR-based cloning of a cDNA, encoding a novel murine carboxylesterase termed ES-x, which was expressed predominantly in liver but also in kidney and lung. The cDNA of ES-x spanned a 2249-bp sequence with an open reading frame encoding 565 amino acids, including an N-terminal hydrophobic signal peptide which directs the synthesis into microsomal lumen and a C-terminal HVEL consensus sequence for retaining the protein in the lumen of the endoplasmic reticulum. The predicted amino acid sequence of ES-x exhibited 75% identity with rat liver pI 6.1 esterase. We further demonstrate that feeding mice with diets containing cholestyramine or sodium cholate increases mRNA-expression of ES-x in liver 2.5- to 3-fold.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Carboxylic Ester Hydrolases / genetics*
  • Cloning, Molecular
  • Consensus Sequence
  • DNA, Complementary
  • Kidney / enzymology
  • Liver / enzymology*
  • Lung / enzymology
  • Mice
  • Mice, Knockout
  • Molecular Sequence Data
  • Open Reading Frames
  • Protein Sorting Signals
  • Tissue Distribution

Substances

  • DNA, Complementary
  • Protein Sorting Signals
  • Carboxylic Ester Hydrolases
  • ES-x carboxylesterase

Associated data

  • GENBANK/Y12887