Cloning and expression of a novel lysophospholipase which structurally resembles lecithin cholesterol acyltransferase

Citation
Y. Taniyama et al., Cloning and expression of a novel lysophospholipase which structurally resembles lecithin cholesterol acyltransferase, BIOC BIOP R, 257(1), 1999, pp. 50-56
Citations number
22
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
ISSN journal
0006291X → ACNP
Volume
257
Issue
1
Year of publication
1999
Pages
50 - 56
Database
ISI
SICI code
0006-291X(19990402)257:1<50:CAEOAN>2.0.ZU;2-N
Abstract
Lecithin cholesterol acyltransferase (LCAT) is the key enzyme in the esteri fication of plasma cholesterol and in the reverse cholesterol transport on high-density lipoprotein (HDL). We have found a novel LCAT-related gene amo ng differentially expressed cDNA fragments between two types of foam cells derived from THP-I cells, which are different in cholesterol efflux ability , using a subtractive PCR technique. The deduced 412-amino-acid sequence ha s 49% amino acid sequence similarity with human LCAT. in contrast to the Li ver-specific expression of LCAT, mRNA expression of the gene was observed m ainly in peripheral tissues including kidney, placenta, pancreas, testis, s pleen, heart, and skeletal muscle. The protein exists in human plasma and i s probably associated with HDL. Moreover, we discovered that the recombinan t protein hydrolyzed lysophosphatidylcholine (lysoPC), a proatherogenic lip id, to glycerophosphorylcholine and a free fatty acid. We have therefore na med this novel enzyme LCAT-like lysophospholipase (LLPL), through which a n ew catabolic pathway for lysoPC on lipoproteins could be elucidated. (C) 19 99 Academic Press.