نتایج جستجو برای: lcat

تعداد نتایج: 582  

Journal: :Journal of biomolecular structure & dynamics 2006
Yana Reshetnyak Kissaou T Tchedre Maya P Nair P Haydn Pritchard Andras G Lacko

Fluorescence spectroscopy has been used to investigate the conformational changes that occur upon binding of wild type (WT) and mutant (Thr123Ile) lecithin:cholesterol acyltransferase (LCAT) to the potential substrates (dioleoyl-phosphatidyl choline [DOPC] and high density lipoprotein [HDL]). For a detailed analysis of structural differences between WT and mutant LCAT, we performed decompositio...

2011
Masayuki Kuroda Yasuyuki Aoyagi Sakiyo Asada Hideaki Bujo Shigeaki Tanaka Shunichi Konno Masami Tanio Itsuko Ishii Kazuhiko Machida Fumiaki Matsumoto Kaneshige Satoh Masayuki Aso Yasushi Saito

Human proliferative adipocytes propagated via ceiling culture technique from subcutaneous fat tissue (designated as ccdPA) were herein evaluated for their potential as a recipient for retroviral vector-mediated gene transduction of a therapeutic protein delivery. Exposure to the ZsGreen-expressing vector supernatant using a cell preparation generated by a 7-day ceiling culture induced a 40-50% ...

Journal: :Arteriosclerosis, thrombosis, and vascular biology 2013
Shin-ichiro Tanaka Tomoyuki Yasuda Tatsuro Ishida Yoshio Fujioka Takeshi Tsujino Tetsuo Miki Ken-ichi Hirata

OBJECTIVE Lecithin:cholesterol acyltransferase (LCAT) is thought to be important in reverse cholesterol transport. However, its association with coronary heart disease (CHD) and sudden death is controversial. APPROACH AND RESULTS We prospectively studied 1927 individuals from the general population. Serum concentrations of apolipoprotein A-I, A-II, B, C-II, C-III, E, and LCAT activity measure...

Journal: :Journal of lipid research 2005
Richard G Lee Ramesh Shah Janet K Sawyer Robert L Hamilton John S Parks Lawrence L Rudel

The relative contributions of ACAT2 and LCAT to the cholesteryl ester (CE) content of VLDL and LDL were measured. ACAT2 deficiency led to a significant decrease in the percentage of CE (37.2 +/- 2.1% vs. 3.9 +/- 0.8%) in plasma VLDL, with a concomitant increase in the percentage of triglyceride (33.0 +/- 3.2% vs. 66.7 +/- 2.5%). Interestingly, the absence of ACAT2 had no apparent effect on the ...

2005
G. M. Anantharamaiah Y. V. Venkatachalapathi Christie G. Brouillette Jere P. Segrest

The major protein of high density llpoproteln (HDL), apolipoprotein (apo) A-l, is the major activator of the plasma enzyme lecithin:cholesterol acyltransferase (LCAT). A consensus amlno acid sequence has been defined for the eight, 22-resldue long, tandem amphlpathic helical repeats located in the carboxy-terminal region of apo A-l. A series of 22 and 44mer synthetic peptide analogues of the co...

Journal: :iranian biomedical journal 0
mohsen naseri mehdi hedayati maryam sadat daneshpour fatemeh bandarian fereidoun azizi

background: the serum concentration of high-density lipoprotein cholesterol (hdl-c) is one of the important heritable risk factors for cardiovascular disease and is a target for therapeutic intervention. in this study, we aimed to evaluate the effects of lecithin cholesterol acyltransferase (lcat) gene polymorphism rs5923 on lcat enzyme activity and serum hdl-c concentration. methods: the study...

Journal: :Transplantation 1989
M Shimada K Yanaga L Makowka S Kakizoe D H Van Thiel T E Starzl

Rapid and accurate assessment of allograft function in the early postoperative period is critical for successful liver transplantation. This study evaluated the efficacy of lecithin:cholesterol acyltransferase (LCAT) activity as an indicator of early allograft function in human orthotopic liver transplantation (OLTx). During a three-month period between September and November 1987, 9 of 11 adul...

Journal: :Protein engineering 1999
F Peelman B Vanloo O Perez-Mendez A Decout J L Verschelde C Labeur N Vinaimont A Verhee N Duverger R Brasseur J Vandekerckhove J Tavernier M Rosseneu

Lecithin cholesterol acyltransferase (LCAT) is an interfacial enzyme active on both high-density (HDL) and low-density lipoproteins (LDL). Threading alignments of LCAT with lipases suggest that residues 50-74 form an interfacial recognition site and this hypothesis was tested by site-directed mutagenesis. The (delta56-68) deletion mutant had no activity on any substrate. Substitution of W61 wit...

Journal: :Journal of lipid research 1998
A G Lacko A J Reason C Nuckolls B J Kudchodkar M P Nair G Sundarrajan P H Pritchard H R Morris A Dell

The major N-linked carbohydrate structures were determined for recombinant human plasma lecithin:cholesterol acyltransferase (LCAT). The analysis of the structure of oligosaccharides by fast atom bombardment mass spectrometry (FAB-MS) and linkage analysis was preceded by reduction and carboxymethylation of the intact glycoproteins and digestion with trypsin and proline specific endopeptidase. T...

Journal: :The Journal of biological chemistry 1989
M Jauhiainen W Yuan M H Gelb P J Dolphin

Lecithin-cholesterol acyltransferase (LCAT) is a plasma enzyme which catalyzes the transacylation of the sn-2-fatty acid of lecithin to cholesterol, forming lysolecithin and cholesteryl ester. We have recently proposed a covalent catalytic mechanism for LCAT in which lecithin cleavage proceeds via the formation of a transition state tetrahedral adduct between the oxygen atom of the catalytic se...

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