Search results for LCAT

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Species

Types

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Reaction types

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Protein (1 results from a total of 1)

Identifier: R-HSA-194239
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: LCAT: P04180

Reaction (6 results from a total of 6)

Identifier: R-HSA-264689
Species: Homo sapiens
Compartment: extracellular region
The LCAT:discoidal HDL complex dissociates reversibly to yield LCAT and a discoidal HDL particle.
Identifier: R-HSA-266310
Species: Homo sapiens
Compartment: extracellular region
The LCAT:spherical HDL complex dissociates reversibly to yield LCAT and a spherical HDL particle.
Identifier: R-HSA-264678
Species: Homo sapiens
Compartment: extracellular region
LCAT (lecithin-cholesterol acyltransferase) associates strongly but reversibly with discoidal HDL particles (Jonas 2000).
Identifier: R-HSA-266315
Species: Homo sapiens
Compartment: extracellular region
LCAT (lecithin-cholesterol acyltransferase) associates strongly but reversibly with spherical HDL particles (Jonas 2000).
Identifier: R-HSA-8952251
Species: Homo sapiens
Compartment: extracellular region
Lecithin cholesterol acyltransferase (LCAT) is a key enzyme in the esterification of plasma cholesterol. Group XV phospholipase A2 (PLA2G15 aka LCAT-like lysophospholipase, LLPL or lysosomal phospholipase A2, LPLA2) bears 49% sequence similarity to LCAT (Taniyama et al. 1999) and is present in plasma. PLA2G15 possesses both calcium-independent phospholipase A(2) and transacylase activities (Abe & Shayman 1998) and could hydrolyse lysophosphatidylcholine (lysoPC), a proatherogenic lipid, to glycerophosphorylcholine (GPCho) and a free fatty acid anion (LCFA(-)) (Taniyama et al. 1999, Hiraoka et al. 2002).
Identifier: R-HSA-264695
Species: Homo sapiens
Compartment: extracellular region
LCAT activated by apoA-I catalyzes the reaction of cholesterol and phosphatidylcholine to yield cholesterol esterified with a long-chain fatty acid and 2-lysophosphatidylcholine. While this reaction was first studied in vitro using purified proteins in solution, it occurs in vivo on the surfaces of HDL particles where transiently-bound LCAT is activated by HDL-associated apoA-I protein and consumes HDL-associated cholesterol and phosphatidylcholine. The cholesterol ester reaction product is strongly associated with the HDL particle because of its increased hydrophobicity, while the 2-lysophosphatidylcholine product is released from the particle (Fielding et al. 1972 [2 references]; Adimoolam et al. 1998).

Complex (2 results from a total of 2)

Identifier: R-HSA-264684
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-266308
Species: Homo sapiens
Compartment: extracellular region

Pathway (1 results from a total of 1)

Identifier: R-HSA-8964058
Species: Homo sapiens
HDL (high-density lipoprotein) particles play a central role in the reverse transport of cholesterol, the process by which cholesterol in tissues other than the liver is returned to the liver for conversion to bile salts and excretion from the body and provided to tissues such as the adrenals and gonads for steroid hormone synthesis (Tall et al. 2008).
ABCG1 mediates the movement of intracellular cholesterol to the extracellular face of the plasma membrane where it is accessible to circulating HDL (Vaughan & Oram 2005). Spherical (mature) HDL particles can acquire additional molecules of free cholesterol (CHOL) and phospholipid (PL) from cell membranes.
At the HDL surface, LCAT (lecithin-cholesterol acyltransferase) associates strongly with HDL particles and, activated by apoA-I, catalyzes the reaction of cholesterol and phosphatidylcholine to yield cholesterol esterified with a long-chain fatty acid and 2-lysophosphatidylcholine. The hydrophobic cholesterol ester reaction product is strongly associated with the HDL particle while the 2-lysophosphatidylcholine product is released. Torcetrapib associates with a molecule of CETP and a spherical HDL particle to form a stable complex, thus trapping CETP and inhibiting CETP-mediated lipid transfer between HDL and LDL (Clark et al. 2006).
Spherical HDL particles can bind apoC-II, apoC-III and and apoE proteins.
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