cDNA cloning, characterization and stable expression of novel human brain carboxylesterase.
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Mori M, Hosokawa M, Ogasawara Y, Tsukada E, Chiba K
cDNA cloning, characterization and stable expression of novel human brain carboxylesterase.
FEBS Lett. 1999 Sep 10;458(1):17-22.
- PubMed ID
- 10518925 [ View in PubMed]
- Abstract
The DNA sequence encoding a novel human brain carboxylesterase (CES) has been determined. The protein is predicted to have 567 amino acids, including conserved motifs, such as GESAGG, GXXXXEFG, and GDHGD which comprise a catalytic triad, and the endoplasmic reticulum retention motif (HXEL-COOH) observed in CES families. Their gene products exhibited hydrolase activity towards temocapril, p-nitrophenyl-acetate and long-chain acyl-CoA. Since the molecular masses of these gene products are similar to those that exist in capillary endothelial cells of the human brain [Yamamda et al. (1994) Brain Res. 658, 163-167], these CES isozymes may function as a blood-brain barrier to protect the central nervous system from ester or amide compounds.