Apolipoprotein C-III, An Important Player in Lipoprotein Metabolism

1996 ◽  
pp. 631-638
Author(s):  
J. C. Fruchart ◽  
V. Clavey ◽  
G. Luc ◽  
J. Dallongeville ◽  
B. Staels ◽  
...  
Keyword(s):  
Lipoprotein Metabolism ◽  
Apolipoprotein C ◽  
Important Player

Apolipoprotein C-III in triglyceride-rich lipoprotein metabolism

2018 ◽  
Vol 29 (3) ◽  
pp. 171-179 ◽  
Author(s):  
Bastian Ramms ◽  
Philip L.S.M. Gordts
Keyword(s):  
Lipoprotein Metabolism ◽  
Apolipoprotein C ◽  
Triglyceride Rich Lipoprotein

scholarly journals Age-dependent Participation of Apolipoprotein C-II in Lipoprotein Metabolism, an Observation in Healthy Adults

1984 ◽  
Vol 12 (4) ◽  
pp. 927-933
Author(s):  
Shigeru TAKAMATSU ◽  
Yoko KAWAMURA ◽  
Kei SATOH ◽  
Ikuko OSANAI ◽  
Seitoku MIZUNO ◽  
...  
Keyword(s):  
Lipoprotein Metabolism ◽  
Healthy Adults ◽  
Apolipoprotein C ◽  
Age Dependent

scholarly journals Metabolic Roles of Apolipoprotein C, Sialylation of Apolipoprotein CIII and Its Effects on Lipoprotein Metabolism in Diabetics

1983 ◽  
Vol 11 (5) ◽  
pp. 1061-1070
Author(s):  
Norio TADA ◽  
Kazuo KONDO ◽  
Toshitsugu ISHIKAWA ◽  
Haruo NAKAMURA ◽  
Emiko MIYAZIMA
Keyword(s):  
Lipoprotein Metabolism ◽  
Apolipoprotein Ciii ◽  
Apolipoprotein C

scholarly journals Detection of apolipoprotein C in human and rat enterocytes.

1980 ◽  
Vol 86 (2) ◽  
pp. 562-567 ◽  
Author(s):  
G Schonfeld ◽  
N Grimme ◽  
D Alpers
Keyword(s):  
Lamina Propria ◽  
Corn Oil ◽  
Lipoprotein Metabolism ◽  
Lipid Transport ◽  
Rat Jejunum ◽  
Adult Rats ◽  
Apolipoprotein C ◽  
Fat Feeding ◽  
Rat Enterocytes ◽  
Fasted Rats

Apoproteins have important physiologic functions in lipoprotein metabolism. Several apoproteins are produced in the intestine including ApoA-I, ApoA-IV, and ApoB. Each appears to participate in intestinal lipid transport. The liver also produces several apoproteins, including ApoC-II and ApoC-III, but the data demonstrating the ability of the intestine to produce ApoC is incomplete. Our aim was to ascertain whether ApoC-II and ApoC-III were present in human and rat jejunum, and if so, whether their presence was altered by fat feeding. The technique of immunolocalization and a newly developed double antibody radioimmunoassay for rat ApoC-III3 were used. ApoC-III3 was found in the supranuclear regions of enterocytes along the entire lengths of villi in the jejuna of 12-h-fasted rats. 1 hour after the gastric ingestion of corn oil. ApoC-III3 was found primarily in between cells and in the lamina propria. Similar results were obtained in human jejunal biopsies with ApoC-II and ApoC-III. ApoC-III3 was also detected by radioimmunoassay in enterocytes isolated from jejuna of neonatal and adult rats. Thus, ApoC-II and ApoC-III are clearly present in the intestine as well as in the liver. In addition, because their localization is altered after fat feeding, they are also likely to be produced in the enterocyte.

scholarly journals Distinct patterns of apolipoprotein C-I, C-II and C-III isoforms are associated with markers of Alzheimer’s disease

2020 ◽  
pp. jlr.RA120000919
Author(s):  
Yueming Hu ◽  
Cristiana Meuret ◽  
Ashley Martinez ◽  
Hussein Yassine ◽  
Dobrin Nedelkov
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Lipoprotein Metabolism ◽  
Lower Percentage ◽  
Older Individuals ◽  
Apolipoprotein C ◽  
Amyloid Accumulation ◽  
E4 Allele ◽  
And Function ◽  
Truncated Isoforms

Apolipoproteins C-I, C-II and C-III interact with ApoE to regulate lipoprotein metabolism and contribute to Alzheimer’s disease pathophysiology. In plasma, apoC-I and C-II exist as truncated isoforms, while apoC-III exhibits multiple glycoforms. This study aimed to 1. delineate apoC-I, C-II and C-III isoform profiles in CSF and plasma in a cohort of non-demented older individuals (n = 61), and 2. examine the effect of APOE4 on these isoforms and their correlation with CSF Aβ42, a surrogate of brain amyloid accumulation. The isoforms of the apoCs were immunoaffinity enriched and measured with MALDI-TOF mass spectrometry, revealing a significantly higher percentage of truncated apoC-I and apoC-II in CSF compared to matched plasma, with positive correlation between CSF and plasma. A greater percentage of monosialylated and disialylated apoC-III isoforms was detected in CSF, accompanied by a lower percentage of the two non-sialylated apoC-III isoforms, with significant linear correlations between CSF and plasma. Furthermore, a greater percentage of truncated apoC-I in CSF, and apoC-II in plasma and CSF, was observed in individuals carrying at least one apoE Ɛ4 allele. Increased apoC-I and apoC-II truncations were  associated with lower CSF Aβ42. Finally, monosialylated apoC-III was lower, and disialylated apoC-III greater in the CSF of Ɛ4 carriers. Together, these results reveal distinct patterns of the apoCs isoforms in CSF, implying CSF-specific apoCs processing. These patterns were accentuated in APOE Ɛ4 allele carriers, suggesting an association between APOE4 genotype and Alzheimer’s disease pathology with apoCs processing and function in the brain.

Abstract 58: Adipose-Specific Deletion of ARV1 Results in Decreased HDL Cholesterol, Reduced White Adipose Tissue Mass and Improved Glucose Tolerance in Mice

2012 ◽  
Vol 32 (suppl_1) ◽  
Author(s):  
William R Lagor ◽  
Fumin Tong ◽  
David W Fields ◽  
Wen Lin ◽  
Jeffrey T Billheimer ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Glucose Tolerance ◽  
Lipoprotein Metabolism ◽  
Hdl Cholesterol ◽  
Sphingolipid Metabolism ◽  
Chow Diet ◽  
Tissue Mass ◽  
Adipose Tissue Mass ◽  
Important Player ◽  
Specific Deletion

ACAT related enzyme 2 required for viability 1 (ARV1) was identified as a gene required for viability in yeast in the absence of cholesterol esterification. ARV1 encodes a putative lipid transporter believed to be important in trafficking of lipids from the ER to the Golgi. ARV1 deficient yeast exhibit profound alterations in cholesterol, phospholipid, and sphingolipid metabolism, accompanied by a constitutively activated unfolded protein response and impaired GPI anchor synthesis. To study the role of ARV1 in mammalian lipid metabolism, we have generated mice with an adipose specific deletion of ARV1 using Cre/loxP technology with Cre expression driven by the Ap2 promoter. ARV1 adipose specific knockout (ASKO) mice exhibited significant reductions in plasma total cholesterol (↓21%, p < 0.05), HDL cholesterol (↓25%, p < 0.01), and phospholipid (↓17.6%, p < 0.05) levels, while fasting triglyceride levels were unaffected. ARV1 ASKO mice also had substantial reductions in epididymal adipose (WT: 0.41 +/- 0.07 g vs. KO: 0.10 +/- 0.07 g, p = 0.0002) and subcutaneous adipose tissue mass (WT: 0.32 +/- 0.03 g vs. KO: 0.11 +/- 0.08 g; p= 0.0002) on a chow diet. In contrast to nearly every other lipodystrophic mouse model, the reduced fat mass in these animals was paradoxically accompanied by improved glucose tolerance (WT AUC: 32,055 vs. KO AUC: 21,470 mg/dl*minutes, p<0.05). These data identify mammalian ARV1 as an important player in adipose tissue biology, and support an important role for adipose tissue in circulating lipoprotein metabolism.

A review of the role of apolipoprotein C-II in lipoprotein metabolism and cardiovascular disease

Metabolism ◽  
2012 ◽  
Vol 61 (7) ◽  
pp. 906-921 ◽  
Author(s):  
Anastazia A. Kei ◽  
Theodosios D. Filippatos ◽  
Vasilios Tsimihodimos ◽  
Moses S. Elisaf
Keyword(s):  
Cardiovascular Disease ◽  
Lipoprotein Metabolism ◽  
Apolipoprotein C
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