Cloning and expression of human lecithin-cholesterol acyltransferase cDNA.

1986/04/01 by J W McLean, Ceri A. Fielding, Dennis Drayna +5 · 8 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · #Glycosylation and Glycoproteins Research #Caveolin-1 and cellular processes #Lipid metabolism and biosynthesis #Complementary DNA #Biochemistry #Amino acid #Peptide sequence #Lipase #Molecular biology #Cloning (programming) #Untranslated region #Acyltransferase #Biology #Molecular cloning #Chemistry #Messenger RNA #Enzyme #Gene

paper · doi:10.1073/pnas.83.8.2335

openalex publication_date 1986/04/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01

Abstract

cDNA and genomic cloning has been used to determine the mRNA and amino acid sequence of human plasma lecithin-cholesterol acyltransferase (LCATase; EC 2.3.1.43). The mature protein was found to contain 416 amino acid residues with a hydrophobic leader sequence of 24 amino acids. An unusual feature of the message is that the poly(A) signal AATAAA overlaps the COOH-terminal glutamic acid and stop codons, and the 3' untranslated region is only 23 bases. The protein itself is distinguished by a number of extended sequences of hydrophobic amino acids, one of which contains a hexapeptide identical with the interfacial binding segment of the active site of pancreatic lipase and is similar to the same site of lingual lipase. The cloned cDNA allows the expression of active LCATase by transfected tissue culture cells.

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• Human lecithin-cholesterol acyltransferase gene: complete gene sequence and sites of expression
• The structural gene for lecithin:cholesterol acyl transferase (LCAT) maps to 16q22
• Advances in understanding of the role of lecithin cholesterol acyltransferase (LCAT) in cholesterol transport
• Site-directed mutagenesis and structure-function analysis of the human apolipoprotein A-I. Relation between lecithin-cholesterol acyltransferase activation and lipid binding.
• Lecithin:cholesterol acyltransferase. Functional regions and a structural model of the enzyme.
• Site‐specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion
• Cloning and expression of human apolipoprotein D cDNA.
• Cellular localization of apolipoprotein D and lecithin:cholesterol acyltransferase mRNA in rhesus monkey tissues by in situ hybridization.
• Lecithin–cholesterol acyltransferase [wikipedia]