Nitric oxide and cutaneous vasomotor response in coronary artery disease patients

Tretjakovs, Pēteris; Kalnins, Uldis; Dabina, I.; Dinne, I.; Ērglis, Andrejs; Jurka, Antra

doi:10.1016/s0021-9150(00)80049-0

Cited by 2 publications

(3 citation statements)

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“…Mouse plasma (15 l) was incubated with the labeled substrate for 1 h at 37°C. Plasma LCAT activity against endogenous substrate (endogenous esterification rate) was measured by using the lipoproteins of the whole plasma as substrate as described (16 3,6,10,15,30, and 60 min and 3, 6, 10, and 24 h after injection. The plasma decay curve was used to fit an exponential curve by computer analysis.…”

Section: Nmr Lipoprotein Analysismentioning

confidence: 99%

“…It may protect low-density lipoprotein (LDL) from oxidation, a process that greatly increases its atherogenicity (3). In addition, HDL may inhibit the inflammatory response and down-regulate the production of adhesion molecules by endothelial cells (4); it also has anticoagulant properties on the vessel wall (5) and facilitates the production of nitric oxide, a vasculoprotective molecule (6).…”

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confidence: 99%

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Endothelial lipase is a major genetic determinant for high-density lipoprotein concentration, structure, and metabolism

Çilingiroğlu

Otvos

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

216

220

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High-density lipoprotein (HDL) protects against atherosclerosis. Endothelial lipase (EL) has been postulated to be involved in lipoprotein, and possibly HDL, metabolism, yet the evidence has been scarce and conflicting. We have inactivated EL in mice by gene targeting. EL ؊/؊ mice have elevated plasma and HDL cholesterol, and increased apolipoproteins A-I and E. NMR analysis reveals an abundance of large HDL particles. There is down-regulation of the transcripts for phospholipid transfer protein, but up-regulation of those for hepatic lipase and lipoprotein lipase. Plasma lecithin:cholesterol acyltransferase is unchanged despite an increase in hepatic mRNA; lecithin:cholesterol acyltransferase activity toward endogenous EL ؊/؊ substrate is, however, reduced by 50%. HDL clearance is decreased in EL ؊/؊ mice; both the structure of HDL and the presence of EL are factors that determine the rate of clearance. To determine EL's role in humans, we find a significant association between a single-nucleotide polymorphism 584C͞T in the EL (LIPG) gene and HDL cholesterol in a well characterized population of 372 individuals. We conclude that EL is a major determinant of HDL concentration, structure, and metabolism in mice, and a major determinant of HDL concentration in humans.lipoprotein metabolism ͉ atherosclerosis ͉ gene targeting

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Section: Nmr Lipoprotein Analysismentioning

confidence: 99%

mentioning

confidence: 99%

Endothelial lipase is a major genetic determinant for high-density lipoprotein concentration, structure, and metabolism

Çilingiroğlu

Otvos

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

216

220

View full text Add to dashboard Cite

show abstract

“…Thus, HDL are considered as anti-atherothrombotic lipoproteins with cardioprotective properties. Proposed protective roles attributed to HDL include reverse cholesterol transport from extrahepatic tissues to the liver (1), antioxidant effects against oxidation of low density lipoproteins (2), inhibition of inflammation through actions of the associated protein paraoxonase (3), and enhancement of the production of nitric oxide (4). Formation, remodeling, and catabolism of HDL are achieved through multiple pathways and are regulated by a variety of proteins.…”

mentioning

confidence: 99%

Severe Hypoalphalipoproteinemia in Mice Expressing Human Hepatic Lipase Deficient in Binding to Heparan Sulfate Proteoglycan

Brown

Gauthier

Parks

et al. 2004

Journal of Biological Chemistry

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Unlike human hepatic lipase (hHL) that is mainly cell surface-anchored via binding to heparan sulfate proteoglycans (HSPG), mouse HL (mHL) has a low affinity to HSPG and thus is largely blood-borne. The reduced HSPG binding of mHL is attributable to the C-terminal amino acids. To determine the functions of HSPG binding of hHL in vivo, we created adenovirus vectors encoding hHL or a chimeric protein (designated hHLmt) in which the C-terminal HSPG-binding sequences were replaced with the corresponding mouse sequences. Injecting hHLmt-expressing virus into C57BL/6J mice (1.8 ؋ 10 10 virus particles/mouse) resulted in a 3-fold increase in pre-heparin HL activity, whereas infection with an identical dose of hHL virus did not change pre-heparin HL activity. In hHLmt-expressing mice, the concentration of total cholesterol and phospholipids was inversely related to the hHL activity in pre-heparin plasma in a dose-and time-dependent manner, and the decrease was mainly attributable to high density lipoproteins (HDL) cholesterol and HDL phospholipids. The expression of hHL exhibited no change in plasma total cholesterol or phospholipid levels as compared with control mice infected with luciferase or injected with saline. The reduced HDL lipids in the hHLmt-expressing mice were accompanied by markedly decreased plasma and hepatic apolipoprotein (apo) A-I. In primary hepatocytes isolated from hHLmt-expressing mice, the concentration of cell-associated and secreted apoA-I was decreased by 2-3-fold as compared with hepatocytes isolated from control mice, whereas the levels of apoB and apoE were unaltered. Infection of primary hepatocytes with hHLmt virus ex vivo also resulted in reduced apoA-I secretion but had no effect on cell-associated apoA-I. These results suggest that expression of HSPG binding-deficient hHL has a profound HDL-lowering effect.

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Nitric oxide and cutaneous vasomotor response in coronary artery disease patients

Cited by 2 publications

References 0 publications

Endothelial lipase is a major genetic determinant for high-density lipoprotein concentration, structure, and metabolism

Endothelial lipase is a major genetic determinant for high-density lipoprotein concentration, structure, and metabolism

Severe Hypoalphalipoproteinemia in Mice Expressing Human Hepatic Lipase Deficient in Binding to Heparan Sulfate Proteoglycan

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