Cloning and sequencing of a novel murine liver carboxylesterase cDNA.
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.
Ellinghaus
P
P
Institut für Arterioskleroseforschung, Westfälische Wilhelms-Universität Münster, 48149 Münster, Germany.
Seedorf
U
U
Assmann
G
G
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002265:Carboxylic Ester Hydrolases / Q000235:genetics*; D003001:Cloning, Molecular; D016384:Consensus Sequence; D018076:DNA, Complementary; D007668:Kidney / Q000201:enzymology; D008099:Liver / Q000201:enzymology*; D008168:Lung / Q000201:enzymology; D051379:Mice; D018345:Mice, Knockout; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D021382:Protein Sorting Signals; D014018:Tissue Distribution
D018076:DNA, Complementary; D021382:Protein Sorting Signals; D002265:Carboxylic Ester Hydrolases; C112205:ES-x carboxylesterase