P. Ellinghaus et al., CLONING AND SEQUENCING OF A NOVEL MURINE LIVER CARBOXYLESTERASE CDNA, Biochimica et biophysica acta, N. Gene structure and expression, 1397(2), 1998, pp. 175-179
Carboxylesterases (EC 3.1.1.1) comprise a group of serine hydrolases w
ith at least 20 genetically distinct loci in mice. Here, we describe d
ifferential display PCR-based cloning of a cDNA, encoding a novel muri
ne 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, includin
g an N-terminal hydrophobic signal peptide which directs the synthesis
into microsomal lumen and a C-terminal HVEL consensus sequence for re
taining the protein in the lumen of the endoplasmic reticulum. The pre
dicted amino acid sequence of ES-x exhibited 75% identity with rat liv
er pi 6.1 esterase. We further demonstrate that feeding mice with diet
s containing cholestyramine or sodium cholate increases mRNA-expressio
n of ES-x in liver 2.5- to 3-fold. (C) 1998 Elsevier Science B.V.