Insight into the role of LCAT from mouse models

DS Ng - Reviews in Endocrine and Metabolic Disorders, 2004 - Springer
DS Ng
Reviews in Endocrine and Metabolic Disorders, 2004Springer
Lecithin cholesterol acyltransferase (LCAT) was first described as a plasma enzyme which
mediates the transfer of fatty acids at the sn-2 position from phosphatidylcholine (PC) to free
cholesterol (FC), forming the neutral lipid cholesterol ester (CE) and
lysophosphatidylcholine (LPC)[1]. LCAT is synthesized mainly in the liver and circulates in
plasma bound primarily to high density lipoproteins (HDL) but it is also found in
apolipoprotein (apo) B-containing particles, especially the low density lipoproteins (LDL) …
Lecithin cholesterol acyltransferase (LCAT) was first described as a plasma enzyme which mediates the transfer of fatty acids at the sn-2 position from phosphatidylcholine (PC) to free cholesterol (FC), forming the neutral lipid cholesterol ester (CE) and lysophosphatidylcholine (LPC)[1]. LCAT is synthesized mainly in the liver and circulates in plasma bound primarily to high density lipoproteins (HDL) but it is also found in apolipoprotein (apo) B-containing particles, especially the low density lipoproteins (LDL). Kinetic studies in humans have provided an estimate that approximately 70% of plasma CE are formed in the HDL and 30% in the apoB-containing particles [2]. Esterification of FC on apoB-containing particles and HDL by LCAT are coined the terms β-activity and α-activity respectively and each plays different role in lipoprotein metabolism.
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