Wyniki wyszukiwania

1

Gender-related effect of cold water swimming on the seasonal changes in lipid profile, ApoB/ApoA-I ratio, and homocysteine concentration in cold water swimmers

100%

Checinska-Maciejewska Z., Miller-Kasprzak E., Checinska A., Korek E., Gibas-Dorna M., Adamczak-Ratajczak A., Bogdanski P., Krauss H.

Journal of Physiology and Pharmacology

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2017

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tom 68

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nr 6

2

The implication of adipocyte ATP-binding cassette A1 and G1 transporters in metabolic complications of obesity

100%

Choromanska B., Mysliwiec P., Hady H. R., Dadan J., Mysliwiec H., Bonda T., Chabowski A., Miklosz A.

Journal of Physiology and Pharmacology

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2019

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tom 70

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nr 1

3

Effect of quercetin on paraoxonase 1 activity - studies in cultured cells, mice and humans

80%

Boesch-Saadatmandi C., Egert S., Schrader C., Coumoul X., Barouki R., Muller M. J., Wolffram S., Rimbach G.

Journal of Physiology and Pharmacology

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2010

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tom 61

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nr 1

99-105

There is increasing evidence that the HDL-associated enzyme paraoxonase 1 (PON1) may have a protective function in the atherosclerotic process. An enhancement of PON1 activity by dietary factors including flavonoids is therefore of interest. Quercetin, a flavonol frequently present in fruits and vegetables has been shown to induce PON1 in cultured liver cells, but the in vivo efficacy of a dietary quercetin supplementation has yet not been evaluated. To this end, we fed laboratory mice quercetin-enriched diets with quercetin concentrations ranging from 0.05 to 2 mg/g diet for 6 weeks and determined the expression of the hepatic PON1 gene and its protein levels. Since we could establish a moderate but significant induction of PON1 mRNA levels by dietary quercetin in mice, we aimed to proof whether healthy human volunteers, given graded supplementary quercetin (50, 100 or 150 mg/day) for two weeks, would respond with likewise enhanced plasma paraoxonase activities. However, PON1 activity towards phenylacetate and paraoxon was not changed following quercetin supplementation in humans. Differences between mice and humans regarding the PON1 inducing activity of quercetin may be related to differences in quercetin metabolism. In mice, unlike in humans, a large proportion of quercetin is methylated to isorhamnetin which exhibits, according to our reporter gene data in cultured liver cells, a potent PON1 inducing activity.

4

Immune regulation by sphingosine 1-phosphate and its receptors

80%

Bode C., Graler M. H.

Archivum Immunologiae et Therapiae Experimentalis

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2012

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tom 60

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nr 1

5

Differences between group X and group V secretory phospholipase A2 in lipolytic modification of lipoproteins

80%

Kamitani S., Yamada K., Yamamoto S., Ishimoto Y., Ono T., Saiga A., Hanasaki K.

Cellular and Molecular Biology Letters

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2012

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tom 17

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nr 3

Secretory phospholipases A2 (sPLA2s) are a diverse family of low molecular mass enzymes (13–18 kDa) that hydrolyze the sn-2 fatty acid ester bond of glycerophospholipids to produce free fatty acids and lysophospholipids. We have previously shown that group X sPLA2 (sPLA2-X) had a strong hydrolyzing activity toward phosphatidylcholine in low-density lipoprotein (LDL) linked to the formation of lipid droplets in the cytoplasm of macrophages. Here, we show that group V sPLA2 (sPLA2-V) can also cause the lipolysis of LDL, but its action differs remarkably from that of sPLA2-X in several respects. Although sPLA2-V released almost the same amount of fatty acids from LDL, it released more linoleic acid and less arachidonic acid than sPLA2-X. In addition, the requirement of Ca2+ for the lipolysis of LDL was about 10-fold higher for sPLA2-V than sPLA2-X. In fact, the release of fatty acids from human serum was hardly detectable upon incubation with sPLA2-V in the presence of sodium citrate, which contrasted with the potent response to sPLA2-X. Moreover, sPLA2-X, but not sPLA2-V, was found to specifically interact with LDL among the serum proteins, as assessed by gel-filtration chromatography as well as sandwich enzyme-immunosorbent assay using anti-sPLA2-X and anti-apoB antibodies. Surface plasmon resonance studies have revealed that sPLA2-X can bind to LDL with high-affinity (Kd = 3.1 nM) in the presence of Ca2+. Selective interaction of sPLA2-X with LDL might be involved in the efficient hydrolysis of cell surface or intracellular phospholipids during foam cell formation.

6

Resistin is not a useful insulin resistance marker for non-obese patients

80%

Pastusiak K., Kregielska-Narozna M., Bogdanski P.

Journal of Physiology and Pharmacology

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2020

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tom 71

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nr 3

7

Species- and substrate-specific stimulation of human plasma paraoxonase 1 [PON1] activity by high chloride concentration

80%

Beltowski J., Wojcicka G., Marciniak A.

Acta Biochimica Polonica

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2002

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tom 49

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nr 4

Paraoxonase 1 (PON1), contained in plasma high-density lipoproteins, plays an important role in the protection of plasma lipoproteins and cell membranes from oxidative damage. Previous studies indicate that human PON1 is stimulated by high NaCl concentrations. The aim of this study was to characterize in more detail the effect of salts on serum PON1. Paraoxon-hydrolyzing activity of human serum was stimulated by 81.6% following the addition of 1 M NaCl. The effect of NaCl was dose-dependent between 0.5 and 2 M. PON1 activity toward phenyl acetate was reduced by 1 M NaCl by 55.2%. Both the paraoxon- and phenyl acetate-hydrolysing activity was slightly lower in heparinized plasma than in serum, but NaCl had similar stimulatory and inhibitory effects on these activities, respectively. In rat, rabbit, and mouse, NaCl reduced PON1 activity. KCl had a similar effect on human PON1 as NaCl. Sodium nitrite also stimulated human PON1 but much less effectively than chloride salts. In contrast, sucrose, sodium acetate and sodium lactate had no significant effect. NaBr was a less effective PON1 activator than NaCl, whereas the effect of NaJ was non-significant. The activity of human PON1 toward homogentisic acid lactone and y-decanolactone was unaltered by NaCl. These data indicate that: 1) high concentrations of chlorides stimulate human PON1 activity toward paraoxon but not other substrates, 2) PON1 is inhibited by Cl- in other mammalian species, 3) the potency of human PON1 activation by halogene salts increases with decreasing atomic mass of the halide anion.

Ograniczanie wyników

Gender-related effect of cold water swimming on the seasonal changes in lipid profile, ApoB/ApoA-I ratio, and homocysteine concentration in cold water swimmers

The implication of adipocyte ATP-binding cassette A1 and G1 transporters in metabolic complications of obesity

Effect of quercetin on paraoxonase 1 activity - studies in cultured cells, mice and humans

Immune regulation by sphingosine 1-phosphate and its receptors

Differences between group X and group V secretory phospholipase A2 in lipolytic modification of lipoproteins

Resistin is not a useful insulin resistance marker for non-obese patients

Species- and substrate-specific stimulation of human plasma paraoxonase 1 [PON1] activity by high chloride concentration