scholarly journals DNA Polymorphisms and Haplotypes of Apolipoprotein A5's Attribution to the Plasma Triglyceride Levels in Koreans

2007 ◽  
Vol 48 (4) ◽  
pp. 609 ◽  
Author(s):  
Jung Ran Choi ◽  
Chung Mo Nam ◽  
Dae Ryong Kang ◽  
Sang Mi Eom ◽  
Hye Jin Lee ◽  
...  
Keyword(s):  
Plasma Triglyceride ◽  
Dna Polymorphisms ◽  
Apolipoprotein A5

scholarly journals Olanzapine inhibits hepatic apolipoprotein A5 secretion inducing hypertriglyceridemia in schizophrenia patients and mice

2021 ◽  
Author(s):  
Xiansheng Huang ◽  
Yiqi Zhang ◽  
Wenqiang Zhu ◽  
Piaopiao Huang ◽  
Jingmei Xiao ◽  
...  
Keyword(s):  
Mrna Expression ◽  
Plasma Triglyceride ◽  
High Dose ◽  
Mrna Levels ◽  
Apolipoprotein A5 ◽  
Protein Levels ◽  
Olanzapine Treatment ◽  
Primary Mouse

Olanzapine, an antipsychotic drug, was reported to induce hypertriglyceridemia, whereas the underlying mechanism remains incompletely understood. This study was to determine the role of apolipoprotein A5 (apoA5) in olanzapine-induced hypertriglyceridemia. In this study, 36 drug-naive and first-episode schizophrenic adult patients (aged 18-60 years) in a multi-center clinical trial (ClinicalTrials.gov NCT03451734) were enrolled. Before and after olanzapine treatment, plasma lipid and apoA5 levels were detected. Moreover, 21 female C57BL/6 J mice (8 weeks old) were divided into 3 groups (n = 7/each group): low-dose olanzapine (3 mg/kg/day), high-dose olanzapine (6 mg/kg/day) and control group. After 6 weeks, plasma glucose, lipids and apoA5 as well as hepatic apoA5 protein and mRNA expression in these animals were detected. In our study in vitro, primary mouse hepatocytes and HepG2 cells were treated with olanzapine of 25, 50, 100 μmol/L, respectively. After 24 hours, apoA5 protein and mRNA levels in hepatocytes were detected. Our study showed that olanzapine treatment significantly increased plasma triglyceride levels and decreased plasma apoA5 levels in these schizophrenic patients. A significant negative correlation was indicated between plasma triglyceride and apoA5 levels in these patients. Consistently, olanzapine dose-dependently increased plasma triglyceride levels and decreased plasma apoA5 levels in mice. Surprisingly, an elevation of hepatic apoA5 protein levels was detected in mice after olanzapine treatment, with no changes of APOA5 mRNA expression. Likewise, olanzapine increased apoA5 protein levels in hepatocytes in vitro, without changes of hepatocyte APOA5 mRNA. Therefore, our study provides the first evidence about the role of apoA5 in olanzapine-induced hypertriglyceridemia. Furthermore, plasma apoA5 reduction, resulting in hypertriglyceridemia, could be attributed to olanzapine-induced inhibition of hepatic apoA5 secretion.

scholarly journals Genetic Predisposition of Human Plasma Triglyceride Concentrations

2015 ◽  
pp. S341-S354 ◽  
Author(s):  
L. SCHWARZOVA ◽  
J. A. HUBACEK ◽  
M. VRABLIK
Keyword(s):  
Cardiovascular Disease ◽  
Genetic Predisposition ◽  
Dietary Habits ◽  
Disease Risk ◽  
Binding Protein ◽  
Cardiovascular Disease Risk ◽  
Regulatory Protein ◽  
Plasma Triglyceride ◽  
Apolipoprotein A5 ◽  
Element Binding Protein

The issue of plasma triglyceride levels relative to the risk of development of cardiovascular disease, as well as overall mortality, has been actively discussed for many years. Like other cardiovascular disease risk factors, final plasma TG values have environmental influences (primarily dietary habits, physical activity, and smoking), and a genetic predisposition. Rare mutations (mainly in the lipoprotein lipase and apolipoprotein C2) along with common polymorphisms (within apolipoprotein A5, glucokinase regulatory protein, apolipoprotein B, apolipo-protein E, cAMP responsive element binding protein 3-like 3, glycosylphosphatidylinositol-anchored HDL-binding protein 1) play an important role in determining plasma TG levels.

scholarly journals Magnolol-mediated regulation of plasma triglyceride through affecting lipoprotein lipase activity in apolipoprotein A5 knock-in mice

PLoS ONE ◽  
2018 ◽  
Vol 13 (2) ◽  
pp. e0192740 ◽  
Author(s):  
Chun-Kai Chang ◽  
Xiu-Ru Lin ◽  
Yen-Lin Lin ◽  
Woei-Horng Fang ◽  
Shu-Wha Lin ◽  
...  
Keyword(s):  
Lipoprotein Lipase ◽  
Lipase Activity ◽  
Plasma Triglyceride ◽  
Lipoprotein Lipase Activity ◽  
Apolipoprotein A5

scholarly journals Analysis of Apolipoprotein A5, C3, and Plasma Triglyceride Concentrations in Genetically Engineered Mice

2004 ◽  
Vol 24 (7) ◽  
pp. 1297-1302 ◽  
Author(s):  
Nadine Baroukh ◽  
Eric Bauge ◽  
Jennifer Akiyama ◽  
Jessie Chang ◽  
Veena Afzal ◽  
...  
Keyword(s):  
Genetically Engineered ◽  
Plasma Triglyceride ◽  
Apolipoprotein A5 ◽  
Genetically Engineered Mice

Application of Two Neutral Mspl DNA Polymorphisms in the Analysis of Hereditary Protein C Deficiency

1990 ◽  
Vol 64 (02) ◽  
pp. 239-244 ◽  
Author(s):  
P H Reitsma ◽  
W te Lintel Hekkert ◽  
E Koenhen ◽  
P A van der Velden ◽  
C F Allaart ◽  
...  
Keyword(s):  
Protein C ◽  
Stop Codon ◽  
Normal Population ◽  
Amino Acid Position ◽  
Rare Allele ◽  
Dna Polymorphisms ◽  
Type I ◽  
Protein C Deficiency ◽  
Gene Deletions ◽  
Allelic Frequencies

SummaryScreening of restriction erzyme digested DNA from normal and protein C deficient individuals with a variety of probes derived from the protein C locus has revealed the existence of two neutral MspI polymorphism. One polymorphism (MI), which is located ≈7 kb upstream of the protein C gene, has allelic frequencies of 69 and 31%, and was used to exclude extensive gene deletions as a likely cause of type I protein C deficiency in 50% of cases in a panel of 22 families. Furtherrnore, the same polymorphism has been used in 5 doubly affected individuals establishing compound heterozygosity in 3 of these.The second, intragenic, polymorphism (MII) has allelic frequencies of 99 and 1% in the normal population. The frequency of the rare allele of this RFLP was with 7% much higher in a panel of 22 Dutch families with protein C deficiency. Interestingly, in all three probands that were heterozygous for MII the rare allele of MII coincided with a point mutation that leads to a stop codon in amino acid position 306 of the protein C coding sequence. This mutation may account for 14% of the protein C deficient individuals in The Netherlands.

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