Measurement of lecithin-cholesterol acyltransferase activity with the use of a Peptide-proteoliposome substrate.

Abstract

Lecithin-cholesterol acyltransferase (LCAT) is the major enzyme responsible for the esterification of free cholesterol on plasma lipoproteins, which is a key step in the reverse cholesterol transport pathway. The measurement of plasma LCAT activity not only is important in the diagnosis of patients with genetic or acquired LCAT deficiency but is also valuable in calculating cardiovascular risk, as well as in research studies of lipoprotein metabolism. In this chapter, we describe a convenient LCAT assay based on the use of an apoA-I mimetic peptide. The proteoliposome substrate used in this assay for LCAT is easily made with the peptide and can be stored by deep freezing without significant loss of activity.

• Authors: Boris L Vaisman, Alan T Remaley
• Journal: Methods in molecular biology (Clifton, N.J.) (Methods Mol Biol) Vol. 1027 Pg. 343-52 ( 2013) ISSN: 1940-6029 [Electronic] United States
• PMID: 23912995 (Publication Type: Journal Article)

Chemical References

• Apolipoprotein A-I
• Cholesterol Esters
• Lecithins
• Proteolipids
• proteoliposomes
• Cholesterol
• Phosphatidylcholine-Sterol O-Acyltransferase

Topics

• Apolipoprotein A-I (chemistry, metabolism)
• Cardiovascular Diseases (blood, enzymology)
• Cholesterol (blood)
• Cholesterol Esters (blood)
• Humans
• Lecithins (blood)
• Phosphatidylcholine-Sterol O-Acyltransferase (blood)
• Proteolipids (chemistry, genetics)
• Substrate Specificity