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anti-Human LCAT Antikörper:
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Human Polyclonal LCAT Primary Antibody für ELISA, WB - ABIN152886
Furbee, Francone, Parks: In vivo contribution of LCAT to apolipoprotein B lipoprotein cholesteryl esters in LDL receptor and apolipoprotein E knockout mice. in Journal of lipid research 2002
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Polyclonal LCAT Primary Antibody für WB - ABIN540393
Lee, Badeau, Mulya, Boudyguina, Gebre, Smith, Parks: Functional LCAT deficiency in human apolipoprotein A-I transgenic, SR-BI knockout mice. in Journal of lipid research 2007
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Human Polyclonal LCAT Primary Antibody für ICC, IF - ABIN438375
Mulya, Lee, Gebre, Boudyguina, Chung, Smith, Colvin, Jiang, Parks: Initial interaction of apoA-I with ABCA1 impacts in vivo metabolic fate of nascent HDL. in Journal of lipid research 2008
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Cow (Bovine) Polyclonal LCAT Primary Antibody für WB - ABIN2776941
Calabresi, Pisciotta, Costantin, Frigerio, Eberini, Alessandrini, Arca, Bon, Boscutti, Busnach, Frascà, Gesualdo, Gigante, Lupattelli, Montali, Pizzolitto, Rabbone, Rolleri, Ruotolo, Sampietro, Sessa, Vaudo, Cantafora, Veglia, Calandra, Bertolini, Frances: The molecular basis of lecithin:cholesterol acyltransferase deficiency syndromes: a comprehensive study of molecular and biochemical findings in 13 unrelated Italian families. in Arteriosclerosis, thrombosis, and vascular biology 2005
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APOA1 may use a reciprocating thumbwheel-like mechanism to activate HDL-remodeling proteins
Increased LCAT activity may be associated with increased formation of TRLs, leading to a reduction in the LDL-particle size in patients at a high risk for atherosclerotic cardiovascular disease.
The CETP rs708272 polymorphism is associated with a heightened risk of developing ACS. In addition, we report the association of the rs708272 and rs2292318 polymorphisms with HDL-C levels and HDL subclasses.
data suggest that Arg123 of apoA-I on discoidal HDL participates in lecithin:cholesterol acyltransferase (LCAT)-mediated cholesterol esterification
the crystal structure of human LCAT in complex with a potent piperidinylpyrazolopyridine activator and an acyl intermediate-like inhibitor, revealing LCAT in an active conformation, is reported.
Plasma LCAT activity was higher in patients with NAFLD.
results demonstrated increased CETP and decreased LCAT and PON-1 activities in colorectal cancer (CRC)patients. In preliminary analysis CETP mass was identified as potential significant predictor of CRC development, suggesting that alterations in HDL-C levels, alongside with changes in HDL structure might have a role in carcinogenesis.
It has been found a significant association between LCAT serum activity and risk of diabetes mellitus in men but not in women.
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 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.
rs5923 polymorphism is not associated with low high-density lipoprotein cholesterol(HDL-C)levels in Iranian population
increased cholesterol esterification by LCAT is atheroprotective
The data indicate that this novel apoA-I missense is associated with markedly decreased levels of HDL cholesterol and very large alpha-1 HDL, as well as decreased serum cellular cholesterol efflux and LCAT activity
A robust all-atom model for LCAT generated by homology modeling
genetic polymorphism is associated with coronary artery disease in Egyptians
This study investigated how the natural LCAT[T147I] and LCAT[P274S] mutations affect the pathway of biogenesis of high-density lipoproteins.
A synonymous H287H mutation in the coding region of exon 6 of the lecithin cholesterol acyltransferase gene was observed in an individual with HDLC levels of 75 mg/dl.
metabolic phenotypes in lecithin cholesterol acyltyransferase-deficient mice
Taken together, these results suggest that apoE-containing discoidal HDLs do not require LCAT-dependent maturation to mediate efficient Abeta 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 overexpression decreases plasma lecithin:cholesterol acyltransferase activity and apolipoprotein A-I levels.
adrenal glucocorticoid function in LCAT knockout (KO) mice
a novel function of apoA-IV in the biogenesis of discrete HDL-A-IV particles with the participation of ABCA1 and LCAT
Studies suggest that absence of lecithin cholesterol acyltransferase (LCAT) may protect against insulin resistance, diabetes and obesity.
Data show that LCAT activity was significantly higher in long chain base biosynthesis protein 2 (Sptlc2)+/- and sphingomyelin synthase 2 (Sms2)-/- mice, but markedly lower in ApoE-/- and Ldlr-/- mice.
Lecithin:cholesterol acyltransferase deficiency protects against cholesterol-induced hepatic endoplasmic reticulum stress in mice.
LCAT deficiency confers gender-specific protection against diet-induced obesity and insulin 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 knockout background in association with a reduction in atherosclerosis
LCAT contributes significantly to the cholesteryl ester (CE) fatty acid pool of apoB lipoprotein and is the only source of plasma long chain polyunsaturated CE in LDL receptor and apoE knockout mice.
hypertriglyceridemia and the improved fasting glucose phenotype seen in the lecithin-cholesterol acyltransferase and ldl receptor double knockout mice are in part attributable to up-regulation of hepatic sterol regulatory element binding factor-1c gene
LCAT has a role in regulating plasma HDL cholesterol levels and biliary cholesterol excretion
apoE is a more significant activator of LCAT than apoA-I on mouse apoB lipoproteins
ACAT2 provides core CE of newly secreted VLDL, whereas LCAT adds CE during LDL particle formation
In LCAT deficient mice, alterations in hepatic expression of the gene for fads2, soat2, and dgat2, results in changes in total hepatic and cholesterol ester-associated polyunsaturated fatty acids.
LCAT deficiency induces complex alterations in hepatic signal transduction cascades.
These data show that brain LCAT esterifies cholesterol on glial-derived apoE-lipoproteins, and influences CSF apoE and apoA-I levels.
LCAT cholesterol esterification is associated with the increase of ApoE/ApoA-I 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