The Experts below are selected from a list of 4827 Experts worldwide ranked by ideXlab platform
Shuichi Kimura - One of the best experts on this subject based on the ideXlab platform.
-
Interaction of rat Lecithin-Cholesterol Acyltransferase with rat apolipoprotein A-I and with Lecithin-Cholesterol vesicles.
Journal of Biochemistry, 1992Co-Authors: Yuji Furukawa, Takashi Urano, Yoshifumi Hida, Harumi Itoh, Chizuko Takahashi, Shuichi KimuraAbstract:: The interaction of rat plasma Lecithin-Cholesterol Acyltransferase with Lecithin-Cholesterol vesicles and with rat apo-A-I was studied in comparison with that of human plasma Lecithin-Cholesterol Acyltransferase to clarify the reaction mechanism of rat plasma Lecithin-Cholesterol Acyltransferase. The interaction of both human and rat Lecithin-Cholesterol Acyltransferase with Lecithin-Cholesterol vesicles was investigated by gel permeation chromatography on Superose 12. Both enzymes had almost the same affinity to the vesicles. The affinity of rat enzyme to rat apo-A-I was stronger than that of human enzyme to human apo-A-I when estimated on the apo-A-I-Sepharose 4B column. When human apo-A-I was added to the human enzyme/vesicle mixture which contained the enzyme-vesicle complex, the enzyme was effectively dissociated from the complex. But when rat apo-A-I was added to the rat enzyme/vesicle mixture, apo-A-I-enzyme-vesicle complex was still recognized by its elution pattern on gel permeation chromatography. This suggests that the mixture of rat enzyme, rat apo-A-I, and vesicles, which are the major components in the rat Lecithin-Cholesterol Acyltransferase reaction, forms a stronger complex than do the components of the human reaction.
Francisco Blanco-vaca - One of the best experts on this subject based on the ideXlab platform.
-
A novel homozygous mutation causing lecithin–cholesterol Acyltransferase deficiency in a proband of Romanian origin with a record of extreme gestational hyperlipidemia
Journal of clinical lipidology, 2017Co-Authors: David Rial-crestelo, Josep Julve, Francisco Blanco-vaca, Ildefonso Santos-recuero, Miguel TorralbaAbstract:Abstract A patient from Romania with extraordinarily high total cholesterol levels and clinical and biochemical features consistent with familial lecithin–cholesterol Acyltransferase deficiency is reported. The genetic analysis performed on our proband showed a novel homozygous mutation on codon 119 of lecithin–cholesterol Acyltransferase gene that causes the substitution of glycine by aspartate. The same mutation, also in homozygosis, was observed in her older sister, whereas his brother presented it in heterozygosis.
-
Molecular diagnosis of lecithin: cholesterol Acyltransferase deficiency in a presymptomatic proband.
Clinical Chemistry and Laboratory Medicine, 1998Co-Authors: Susanna Cirera, Josep Julve, Immaculada Ferrer, Carles Mainou, Rosa Bonet, Jesús M. Martín-campos, Francesc González-sastre, Francisco Blanco-vacaAbstract:: We report the molecular diagnosis of a lecithin : cholesterol Acyltransferase deficiency in a 12-year old proband with a high-density lipoprotein deficiency. The increased percentage of free cholesterol in plasma and high-density lipoprotein indicated an inherited lecithin : cholesterol Acyltransferase deficiency as the underlying cause. This diagnosis was confirmed by a low plasma lecithin : cholesterol Acyltransferase activity and a combination of genetic analyses which demonstrated compound heterozygosity for two mutations in the lecithin : cholesterol Acyltransferase gene of the proband. One was a previously unreported 2 bp deletion leading to a stop signal in codon 77 and the other a point mutation causing Arg 135-->Gln transition. To our knowledge, this is the first diagnosis of lecithin : cholesterol Acyltransferase deficiency in a pre-symptomatic patient. Whether the proband will develop signs of complete lecithin : cholesterol Acyltransferase deficiency or the milder form (Fish Eye Disease) is uncertain, although the former possibility is more likely. The risk of premature atherosclerosis conferred by lecithin : cholesterol Acyltransferase deficiency is not well established. The proband will need to be carefully monitored in the future.
Yuji Furukawa - One of the best experts on this subject based on the ideXlab platform.
-
Interaction of rat Lecithin-Cholesterol Acyltransferase with rat apolipoprotein A-I and with Lecithin-Cholesterol vesicles.
Journal of Biochemistry, 1992Co-Authors: Yuji Furukawa, Takashi Urano, Yoshifumi Hida, Harumi Itoh, Chizuko Takahashi, Shuichi KimuraAbstract:: The interaction of rat plasma Lecithin-Cholesterol Acyltransferase with Lecithin-Cholesterol vesicles and with rat apo-A-I was studied in comparison with that of human plasma Lecithin-Cholesterol Acyltransferase to clarify the reaction mechanism of rat plasma Lecithin-Cholesterol Acyltransferase. The interaction of both human and rat Lecithin-Cholesterol Acyltransferase with Lecithin-Cholesterol vesicles was investigated by gel permeation chromatography on Superose 12. Both enzymes had almost the same affinity to the vesicles. The affinity of rat enzyme to rat apo-A-I was stronger than that of human enzyme to human apo-A-I when estimated on the apo-A-I-Sepharose 4B column. When human apo-A-I was added to the human enzyme/vesicle mixture which contained the enzyme-vesicle complex, the enzyme was effectively dissociated from the complex. But when rat apo-A-I was added to the rat enzyme/vesicle mixture, apo-A-I-enzyme-vesicle complex was still recognized by its elution pattern on gel permeation chromatography. This suggests that the mixture of rat enzyme, rat apo-A-I, and vesicles, which are the major components in the rat Lecithin-Cholesterol Acyltransferase reaction, forms a stronger complex than do the components of the human reaction.
H B Brewer - One of the best experts on this subject based on the ideXlab platform.
-
Lecithin-Cholesterol Acyltransferase: role in lipoprotein metabolism, reverse cholesterol transport and atherosclerosis.
Current opinion in lipidology, 2000Co-Authors: Silvia Santamarina-fojo, Gilles Lambert, Jeffrey M. Hoeg, H B BrewerAbstract:In the past several years significant advances have been made in our understanding of Lecithin-Cholesterol Acyltransferase (LCAT) function. LCAT beneficially alters the plasma concentrations of apolipoprotein B-containing lipoproteins, as well as HDL. In addition, its proposed role in facilitating reverse cholesterol transport and modulating atherosclerosis has been demonstrated in vivo. Analysis of LCAT transgenic animals has established the importance of evaluating HDL function, as well as HDL plasma levels, to predict atherogenic risk.
Josep Julve - One of the best experts on this subject based on the ideXlab platform.
-
a novel homozygous mutation causing lecithin cholesterol Acyltransferase deficiency in a proband of romanian origin with a record of extreme gestational hyperlipidemia
Journal of Clinical Lipidology, 2017Co-Authors: David Rialcrestelo, Josep Julve, Ildefonso Santosrecuero, Francisco Blancovaca, Miguel TorralbaAbstract:Abstract A patient from Romania with extraordinarily high total cholesterol levels and clinical and biochemical features consistent with familial lecithin–cholesterol Acyltransferase deficiency is reported. The genetic analysis performed on our proband showed a novel homozygous mutation on codon 119 of lecithin–cholesterol Acyltransferase gene that causes the substitution of glycine by aspartate. The same mutation, also in homozygosis, was observed in her older sister, whereas his brother presented it in heterozygosis.
-
A novel homozygous mutation causing lecithin–cholesterol Acyltransferase deficiency in a proband of Romanian origin with a record of extreme gestational hyperlipidemia
Journal of clinical lipidology, 2017Co-Authors: David Rial-crestelo, Josep Julve, Francisco Blanco-vaca, Ildefonso Santos-recuero, Miguel TorralbaAbstract:Abstract A patient from Romania with extraordinarily high total cholesterol levels and clinical and biochemical features consistent with familial lecithin–cholesterol Acyltransferase deficiency is reported. The genetic analysis performed on our proband showed a novel homozygous mutation on codon 119 of lecithin–cholesterol Acyltransferase gene that causes the substitution of glycine by aspartate. The same mutation, also in homozygosis, was observed in her older sister, whereas his brother presented it in heterozygosis.
-
Molecular diagnosis of lecithin: cholesterol Acyltransferase deficiency in a presymptomatic proband.
Clinical Chemistry and Laboratory Medicine, 1998Co-Authors: Susanna Cirera, Josep Julve, Immaculada Ferrer, Carles Mainou, Rosa Bonet, Jesús M. Martín-campos, Francesc González-sastre, Francisco Blanco-vacaAbstract:: We report the molecular diagnosis of a lecithin : cholesterol Acyltransferase deficiency in a 12-year old proband with a high-density lipoprotein deficiency. The increased percentage of free cholesterol in plasma and high-density lipoprotein indicated an inherited lecithin : cholesterol Acyltransferase deficiency as the underlying cause. This diagnosis was confirmed by a low plasma lecithin : cholesterol Acyltransferase activity and a combination of genetic analyses which demonstrated compound heterozygosity for two mutations in the lecithin : cholesterol Acyltransferase gene of the proband. One was a previously unreported 2 bp deletion leading to a stop signal in codon 77 and the other a point mutation causing Arg 135-->Gln transition. To our knowledge, this is the first diagnosis of lecithin : cholesterol Acyltransferase deficiency in a pre-symptomatic patient. Whether the proband will develop signs of complete lecithin : cholesterol Acyltransferase deficiency or the milder form (Fish Eye Disease) is uncertain, although the former possibility is more likely. The risk of premature atherosclerosis conferred by lecithin : cholesterol Acyltransferase deficiency is not well established. The proband will need to be carefully monitored in the future.