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Single Nucleotide Polymorphism in LCAT gene is associated with dyslipidemia.
data suggests a model wherein the active site of LCAT is shielded from soluble substrates by a dynamic lid until it interacts with HDL (zeige HSD11B1 Proteine) to allow transesterification to proceed
Increased LCAT activity may be associated with increased formation of triglyceride rich lipoproteins, leading to a reduction in LDL particle size and atherosclerosis.
Mapping the naturally occurring mutations onto the structure provides insight into how they may affect LCAT enzymatic activity.
Report slightly reduction in LCAT that would probably reflect a delay in reverse cholesterol transport occurring in MetS (zeige ETV3 Proteine).
rs5923 polymorphism is not associated with low high-density lipoprotein cholesterol(HDL (zeige HSD11B1 Proteine)-C)levels in Iranian population
increased cholesterol esterification by LCAT is atheroprotective
The data indicate that this novel apoA-I (zeige APOA1 Proteine) missense is associated with markedly decreased levels of HDL (zeige HSD11B1 Proteine) cholesterol and very large alpha-1 HDL (zeige HSD11B1 Proteine), as well as decreased serum cellular cholesterol efflux and LCAT activity
A robust all-atom model for LCAT generated by homology modeling
This study investigated how the natural LCAT[T147I] and LCAT[P274S] mutations affect the pathway of biogenesis of high-density lipoproteins.
Taken together, these results suggest that apoE (zeige APOE Proteine)-containing discoidal HDLs (zeige CSF1R Proteine) do not require LCAT-dependent maturation to mediate efficient Abeta (zeige APP Proteine) clearance
Gene transfer of WT LCAT in LCAT(-/-) mice increased 11.8-fold the plasma cholesterol, whereas the LCAT[T147I] and LCAT[P274S] mutants caused a 5.2- and 2.9-fold increase, respectively.
DYRK1A (zeige DYRK1A Proteine) overexpression decreases plasma lecithin:cholesterol acyltransferase activity and apolipoprotein A-I (zeige APOA1 Proteine) levels.
adrenal glucocorticoid function in LCAT knockout (KO) mice
a novel function of apoA-IV (zeige APOA4 Proteine) in the biogenesis of discrete HDL (zeige HSD11B1 Proteine)-A-IV particles with the participation of ABCA1 (zeige ABCA1 Proteine) and LCAT
Studies suggest that absence of lecithin cholesterol acyltransferase (LCAT) may protect against insulin (zeige INS Proteine) resistance, diabetes and obesity.
Data show that LCAT activity was significantly higher in long chain base biosynthesis protein 2 (Sptlc2 (zeige SPTLC2 Proteine))+/- and sphingomyelin synthase 2 (Sms2 (zeige SGMS2 Proteine))-/- mice, but markedly lower in ApoE (zeige APOE Proteine)-/- and Ldlr (zeige LDLR Proteine)-/- mice.
LCAT deficiency confers gender-specific protection against diet-induced obesity and insulin (zeige INS Proteine) resistance at least in part through regulation in UPR, white adipose tissue adipogenesis, and brown adipocyte partitioning
Oxidative stress is markedly elevated in lecithin:cholesterol acyltransferase-deficient mice and is paradoxically reversed in the apolipoprotein E (zeige APOE Proteine) knockout background in association with a reduction in atherosclerosis
LCAT cholesterol esterification is associated with the increase of ApoE (zeige APOE Proteine)/ApoA-I (zeige APOA1 Proteine) ratio during atherosclerosis progression in rabbit.
The 1,434 bp mRNA sequence of porcine LCAT including the full coding region and encoding a protein of 472 amino acids, was obtained.
This gene encodes the extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. Mutations in this gene have been found to cause fish-eye disease as well as LCAT deficiency.
, phospholipid-cholesterol acyltransferase
, lecithin-cholesterol acyltransferase Lcat
, lecithin-cholesterol acyltransferase
, lecithin cholesterol acyltransferase
, Lecithin-cholesterol acyltransferase