Widespread expression of perilipin 5 in normal human tissues and in diseases is restricted to distinct lipid droplet subpopulations

• Verfasst von: Hashani, Merita [VerfasserIn]
• Verfasst von: Witzel, Hagen Roland [VerfasserIn]
• Verfasst von: Pawella, Lena Maria [VerfasserIn]
• Verfasst von: Lehmann-Koch, Judith [VerfasserIn]
• Verfasst von: Schumacher, Jens [VerfasserIn]
• Verfasst von: Mechtersheimer, Gunhild [VerfasserIn]
• Verfasst von: Schnölzer, Martina [VerfasserIn]
• Verfasst von: Schirmacher, Peter [VerfasserIn]
• Verfasst von: Roth, Wilfried [VerfasserIn]
• Verfasst von: Straub, Beate Katharina [VerfasserIn]
• Titel: Widespread expression of perilipin 5 in normal human tissues and in diseases is restricted to distinct lipid droplet subpopulations
• Verf.angabe: Merita Hashani, Hagen Roland Witzel, Lena Maria Pawella, Judith Lehmann-Koch, Jens Schumacher, Gunhild Mechtersheimer, Martina Schnölzer, Peter Schirmacher, Wilfried Roth, Beate Katharina Straub
• E-Jahr: 2018
• Jahr: 11 May 2018
• Umfang: 16 S.
• Fussnoten: Gesehen am 16.10.2019
• Titel Quelle: Enthalten in: Cell & tissue research
• Ort Quelle: Berlin : Springer, 1974
• Jahr Quelle: 2018
• Band/Heft Quelle: 374(2018), 1, Seite 121-136
• ISSN Quelle: 0302-766X
• DOI: doi:10.1007/s00441-018-2845-7
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: Cardiomyopathy
• Sach-SW: Hepatic steatogenesis
• Sach-SW: Lipid droplets
• Sach-SW: Perilipin 5
• Sach-SW: Tumorigenesis
• K10plus-PPN: 1678951250

Abstract

Diseases associated with the accumulation of lipid droplets are increasing in western countries. Lipid droplet biogenesis, structure and degradation are regulated by proteins of the perilipin family. Perilipin 5 has been shown to regulate basal lipolysis in oxidative tissues. We examine perilipin 5 in normal human tissues and in diseases using protein biochemical and microscopic techniques. Perilipin 5 was constitutively located at small lipid droplets in skeletal myocytes, cardiomyocytes and brown adipocytes. In addition, perilipin 5 was detected in the epithelia of the gastrointestinal and urogenital tract, especially in hepatocytes, the mitochondria-rich parietal cells of the stomach, tubular kidney cells and ductal cells of the salivary gland and pancreas. Granular cytoplasmic expression, without a lipid droplet-bound localization was detected elsewhere. In cardiomyopathies, in skeletal muscle diseases and during hepatocyte steatogenesis, perilipin 5 was upregulated and localized to larger and more numerous lipid droplets. In steatotic human hepatocytes, perilipin 5 was moderately increased and colocalized with perilipins 1 and 2 but not with perilipin 3 at lipid droplets. In liver diseases implicated in alterations of mitochondria, such as mitochondriopathies, alcoholic liver disease, Wilson’s disease and acute liver injury, perilipin 5 was frequently localized to small lipid droplets and less in the cytoplasm. In tumorigenesis, perilipin 5 was especially upregulated in lipo-, leio- and rhabdomyosarcoma and hepatocellular and renal cell carcinoma. In summary, our study provides evidence that perilipin 5 is not restricted to certain cell types but localizes to distinct lipid droplet subpopulations reflecting a possible function in oxidative energy supply in normal tissues and in diseases.