• Startseite
  • Suchergebnisse
  • Phospholipase C-related catalytically inactive protein (PRIP) regulates lipolysis in adipose tissue by modulating the phosphorylation of hormone-sensitive lipase.

Phospholipase C-related catalytically inactive protein (PRIP) regulates lipolysis in adipose tissue by modulating the phosphorylation of hormone-sensitive lipase.

PloS one (2014-06-20)
Toshiya Okumura, Kae Harada, Kana Oue, Jun Zhang, Satoshi Asano, Masaki Hayashiuchi, Akiko Mizokami, Hiroto Tanaka, Masahiro Irifune, Nobuyuki Kamata, Masato Hirata, Takashi Kanematsu
ZUSAMMENFASSUNG

Phosphorylation of hormone-sensitive lipase (HSL) and perilipin by protein kinase A (PKA) promotes the hydrolysis of lipids in adipocytes. Although activation of lipolysis by PKA has been well studied, inactivation via protein phosphatases is poorly understood. Here, we investigated whether phospholipase C-related catalytically inactive protein (PRIP), a binding partner for protein phosphatase 1 and protein phosphatase 2A (PP2A), is involved in lipolysis by regulating phosphatase activity. PRIP knockout (PRIP-KO) mice displayed reduced body-fat mass as compared with wild-type mice fed with standard chow ad libitum. Most other organs appeared normal, suggesting that mutant mice had aberrant fat metabolism in adipocytes. HSL in PRIP-KO adipose tissue was highly phosphorylated compared to that in wild-type mice. Starvation of wild-type mice or stimulation of adipose tissue explants with the catabolic hormone, adrenaline, translocated both PRIP and PP2A from the cytosol to lipid droplets, but the translocation of PP2A was significantly reduced in PRIP-KO adipocytes. Consistently, the phosphatase activity associated with lipid droplet fraction in PRIP-KO adipocytes was significantly reduced and was independent of adrenaline stimulation. Lipolysis activity, as assessed by measurement of non-esterified fatty acids and glycerol, was higher in PRIP-KO adipocytes. When wild-type adipocytes were treated with a phosphatase inhibitor, they showed a high lipolysis activity at the similar level to PRIP-KO adipocytes. Collectively, these results suggest that PRIP promotes the translocation of phosphatases to lipid droplets to trigger the dephosphorylation of HSL and perilipin A, thus reducing PKA-mediated lipolysis.

MATERIALIEN
Produktnummer
Marke
Produktbeschreibung

Sigma-Aldrich
Glycerin, for molecular biology, ≥99.0%
Sigma-Aldrich
Glycerin, ≥99.5%
Sigma-Aldrich
Glycerin, ACS reagent, ≥99.5%
Sigma-Aldrich
Glycerin, ReagentPlus®, ≥99.0% (GC)
Sigma-Aldrich
Glycerin, BioReagent, suitable for cell culture, suitable for insect cell culture, suitable for electrophoresis, ≥99% (GC)
Sigma-Aldrich
Glycerin, meets USP testing specifications
Supelco
Glycerin, Pharmaceutical Secondary Standard; Certified Reference Material
Sigma-Aldrich
Glycerin, BioXtra, ≥99% (GC)
Sigma-Aldrich
Anti-GAPDH-Antikörper, Maus monoklonal in Maus hergestellte Antikörper, clone GAPDH-71.1, purified from hybridoma cell culture
Sigma-Aldrich
Anti-GAPDH in Kaninchen hergestellte Antikörper, ~1 mg/mL, affinity isolated antibody, buffered aqueous solution
Sigma-Aldrich
Glycerin, BioUltra, for molecular biology, anhydrous, ≥99.5% (GC)
Sigma-Aldrich
Glycerin -Lösung, 83.5-89.5% (T)
Sigma-Aldrich
Glycerin, FCC, FG
USP
Glycerin, United States Pharmacopeia (USP) Reference Standard
Supelco
Glycerin, analytical standard
Sigma-Aldrich
Glycerin, tested according to Ph. Eur., anhydrous
Adrenalin, European Pharmacopoeia (EP) Reference Standard
Sigma-Aldrich
Anti-GAPDH antibody produced in rabbit, affinity isolated antibody
Sigma-Aldrich
Anti-CLEC10A antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution, Ab1
Sigma-Aldrich
Anti-PLIN1 antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
Sigma-Aldrich
Anti-GAPDH antibody produced in chicken, affinity isolated antibody, buffered aqueous solution
Sigma-Aldrich
Anti-GAPDH antibody produced in mouse, purified immunoglobulin, buffered aqueous solution
Sigma-Aldrich
Anti-HSL antibody produced in rabbit, affinity isolated antibody
Sigma-Aldrich
Anti-MGLL antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
Sigma-Aldrich
Anti-phospho-HSL (pSer855/554) antibody produced in rabbit, affinity isolated antibody
Sigma-Aldrich
Anti-phospho-HSL (pSer552) antibody produced in rabbit, affinity isolated antibody
Sigma-Aldrich
Anti-GAPDH antibody produced in rabbit, Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
Sigma-Aldrich
Monoclonal Anti-CLEC10A antibody produced in mouse, clone 2D6, purified immunoglobulin, buffered aqueous solution
Sigma-Aldrich
Anti-CLEC10A antibody produced in mouse, purified immunoglobulin, buffered aqueous solution
Sigma-Aldrich
Anti-MGLL antibody produced in mouse, purified immunoglobulin, buffered aqueous solution

Soziale Medien

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon

Merck

Forschung. Entwicklung. Produktion.

Wir sind ein führender Anbieter für die globale Life-Science-Industrie mit Lösungen und Dienstleistungen für die Forschung, Entwicklung und Produktion in der Biotechnologie sowie für die Arzneimittelforschung und -produktion in der Pharmaindustrie.

© 2021 Merck KGaA, Darmstadt, Deutschland und/oder Tochterunternehmen. Alle Rechte vorbehalten.

Die Vervielfältigung von Inhalten dieser Internetseite ist ohne Genehmigung strengstens untersagt.