PNPLA3 has retinyl-palmitate lipase activity in human hepatic stellate cells

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PNPLA3 has retinyl-palmitate lipase activity in human hepatic stellate cells

Retinoids are micronutrients that are stored as retinyl esters in the retina and hepatic stellate cells (HSCs). HSCs are key players in fibrogenesis in chronic liver diseases. The enzyme responsible for hydrolysis and release of retinyl esters from HSCs is unknown and the relationship between retinoid metabolism and liver disease remains unclear. We hypothesize that the patatin-like phospholipa...

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PNPLA3 I148M Variant Influences Circulating Retinol in Adults with Nonalcoholic Fatty Liver Disease or Obesity.

BACKGROUND Retinol is a lipid-soluble essential nutrient that is stored as retinyl esters in lipid droplets of hepatic stellate cells. Patatin-like phospholipase domain-containing 3 (PNPLA3), through its retinyl-palmitate lipase activity, releases retinol from lipid droplets in hepatic stellate cells in vitro and ex vivo. We have shown that the genetic variant I148M (rs738409) reduces the PNPLA...

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Unusual properties of retinyl palmitate hydrolase activity in rat liver.

These studies report the hydrolysis of retinyl palmitate with liver homogenates and homogenate fractions from retinol-depleted rats. The studies utilized an effective in vitro assay for retinyl palmitate hydrolase (RPH) activity, in which microgram amounts of retinyl palmitate were employed as substrate, followed by the chromatographic separation and fluorescence assay of free and esterified re...

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Unusual properties of retinyl palmitate hydrolase activity in rat liver1

These studies report the hydrolysis of retinyl palmitate with liver homogenates and homogenate fractions from retinol-depleted rats. The studies utilized an effective in vitro assay for retinyl palmitate hydrolase (RPH) activity, in which p g amounts of retinyl palmitate were employed as substrate, followed by the chromatographic separation and fluorescence assay of free and esterified retinol....

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Retinyl palmitate hydrolase activity in normal rat liver.

Retinyl esters are hydrolyzed in liver both during uptake and mobilization of vitamin A. Studies were conducted to explore the enzymatic hydrolysis of retinyl palmitate in normal rat liver. Retinyl palmitate hydrolase activity was assayed with a sensitive and accurate microassay, employing retinyl [~-‘~C]palmitate as substrate. The products of the reaction were identified as retinol and free fa...

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ژورنال

عنوان ژورنال: Human Molecular Genetics

سال: 2014

ISSN: 0964-6906,1460-2083

DOI: 10.1093/hmg/ddu121