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Seems to be the major enzyme contributing to lysophosphatidylcholine acyltransferase activity in the liver.
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Regulation of LPCAT3 expression might be associated with atherosclerotic progression in humans.
findings identify LPCAT3 as a direct PPARdelta (show PPARD ELISA Kits) target gene and suggest a novel function of PPARdelta (show PPARD ELISA Kits) in regulation of phospholipid metabolism through LPCAT3.
Our findings suggest that LPCAT3 plays an important role in M1/M2-macrophage polarization, providing novel potential therapeutic targets for the regulation of immune and inflammatory disorders
LPCAT3 a key contributor to the human macrophages inflammatory response.
Results establish for the first time that LPCAT3 is specifically regulated by LXRalpha (show NR1H3 ELISA Kits).
LPCAT3 is primarily responsible for hepatic LPCAT activity
MBOAT5 and MBOAT7 in arachidonate recycling, thus regulating free arachidonic acid levels and leukotriene synthesis in neutrophils
LPCAT3 is involved in phospholipids remodeling to achieve appropriate membrane lipid fatty acid composition.
These results indicate that human MBOAT5 is a lysophospholipid acyltransferase (show AGPAT1 ELISA Kits) acting preferentially on lysophosphatidylcholine, lysophosphatidylserine and lysophosphatidylethanolamine.
characterization of LPCAT3; LPCAT3 expression in tissue culture increased phospholipids with relatively more saturated acyl chains; limiting LPCAT3 expression increased abundance of phospholipids with more unsaturated acyl chains
small intestine Lpcat3 deficiency has a much bigger effect on plasma lipid levels than that of liver deficiency
LPCAT3 KO mice have longer and larger small intestines than control mice, with shorter wide villi, reduced lipid absorption, and lower levels NPC1L1 (show NPC1L1 ELISA Kits), CD36 (show CD36 ELISA Kits), and FATP4 (show SLC27A4 ELISA Kits) proteins.
Data show that the lack of LPCAT3 leads to drastic reductions in membrane arachidonate levels, and that LPCAT3-deficient mice are neonatally lethal due to an extensive triacylglycerol (TG) accumulation and dysfunction in enterocytes.
It is possible that enhanced phospholipid remodeling by LPCAT3 may be associated with adipocyte differentiation.
hepatic LPCAT3 modulates VLDL production by regulating LysoPC levels and MTP expression.
Seems to be the major enzyme contributing to lysophosphatidylcholine acyltransferase activity in the liver. Favors unsaturated fatty acyl-CoAs as acyl donors compared to saturated fatty acyl-CoAs. Displays lysophosphatidylserine acyltransferase (LPSAT) activity (By similarity).
, O-acyltransferase (membrane bound) domain containing 5
, membrane bound O-acyltransferase domain containing 5
, lysophospholipid acyltransferase 5
, lysophosphatidylcholine acyltransferase 3
, lysophospholipid acyltransferase 5-like
, 1-acylglycerophosphocholine O-acyltransferase
, LPLAT 5
, O-acyltransferase domain-containing protein 5
, gene rich cluster, C3f
, lyso-PC acyltransferase 3
, membrane-bound O-acyltransferase domain-containing protein 5
, 1-acylglycerophosphoserine O-acyltransferase
, lyso-PS acyltransferase
, lysophosphatidylserine acyltransferase
, putative protein similar to nessy
, LPC acyltransferase 3
, lyso-PE acyltransferase
, lysophosphatidylethanolamine acyltransferase