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Members of the perilipin family, such as PLIN5, coat intracellular lipid storage droplets and protect them from lipolytic degradation (Dalen et al., 2007 [PubMed 17234449]).[supplied by OMIM, Feb 2010].. Additionally we are shipping Perilipin 5 Antibodies (41) and Perilipin 5 Kits (5) and many more products for this protein.
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C/EBPalpha (show CEBPA Proteins) is an essential regulatory factor for perilipin5 transcription and suggest that fasting stimulates perilipin5 transcription through influencing C/EBPalpha (show CEBPA Proteins) expression.
The data highlight a key role of PLIN5 in lipid droplets function, first by finely adjusting lipid droplets fatty acids supply to mitochondrial oxidation, and second acting as a protective factor against lipotoxicity in skeletal muscle.
Notch1 expression is reduced and glu (show G6PC Proteins)cose-6-phosphatase and (show G6PC Proteins) perilipin-5 (G6PC/PLIN5) are upr (show NOTCH1 Proteins)egulated in liver biopsies from nonalcoholic steatohepatitis (NASH) and nonalcoholic fatty liver disease (NAFLD) patients.
High oxygen consumption in middle-aged men was reflected in higher perilipin 5 expression in skeletal muscle.
PLIN5 was significantly colocated with ATGL (show PNPLA2 Proteins), mitochondria and CGI-58 (show ABHD5 Proteins), indicating a close association between the key lipolytic effectors in resting skeletal muscle.
Perilipin 5 as a lipid droplet protein adapted to mitochondrial energy utilization
Sprint interval and traditional endurance training increase net intramuscular triglyceride breakdown and expression of perilipin 2 (show PLIN2 Proteins) and 5
PLIN5 likely plays an important role in intramyocellular lipid accumulation and oxidation, both of which increase with endurance training in human skeletal muscle.
The lipid droplet coat protein (show GOLPH3 Proteins) perilipin 5 also localizes to muscle mitochondria.
Perilipin 5 is the most recently established family member, highly expressed in oxidative tissues and could play an important role in regulating LD TAG hydrolysis in oxidative mammalian tissues. [Review]
interaction of ATGL (show PNPLA2 Proteins) with CGI-58 (show ABHD5 Proteins) increased lipolysis, whereas interaction of ATGL (show PNPLA2 Proteins) with perilipin 5 decreased lipolysis.
Plin5, a new regulator of myocardial lipid metabolism, decreases free fatty acid peroxidation by inhibiting the lipolysis of intracellular lipid droplets, thus providing cardioprotection against I/R injury and shedding new light on therapeutic solutions for I/R diseases.
During catecholamine-stimulated lipolysis, Perilipin 5 is phosphorylated by protein kinase A and forms transcriptional complexes with PGC-1alpha and SIRT1 (show SIRT1 Proteins) in the nucleus. Perilipin 5 promotes PGC-1alpha co-activator function by disinhibiting SIRT1 (show SIRT1 Proteins) deacetylase activity.
Changes in lipid metabolism resulting from PLIN5 deletion reduce ER stress in muscle, decrease FGF21 (show FGF21 Proteins) production by muscle and liver, and impair glycemic control.
The results indicated that atorvastatin promoted lipolysis and reduced TG accumulation in the liver by increasing PKA-mediated phosphorylation of Plin5. This new mechanism of lipid-lowering effects of atorvastatin might provide a new strategy for NAFLD treatment.
mitochondria isolated from hearts deficient in Plin5, have specific functional defects
Plin5 deficiency alters cardiac lipid metabolism and associates with reduced survival following myocardial ischemia.
Data show that glucose-6-phosphatase (show G6PC Proteins) and perilipin-5 (G6PC (show G6PC Proteins)/PLIN5) are upregulated in notch1 (show NOTCH1 Proteins) knockout (KO) mice.
PLIN5 is dispensable for normal substrate metabolism during exercise and is not required to promote mitochondrial biogenesis or enhance the cellular adaptations to endurance exercise training.
High fat diet-induced liver fibrosis is accompanied by an approximate 75% reduction in Plin5 in hepatic stellate cells (HSC (show FUT1 Proteins)), and spontaneous activation of primary HSC (show FUT1 Proteins) produces temporally coincident loss of Plin5 expression and lipid droplet depletion.
Members of the perilipin family, such as PLIN5, coat intracellular lipid storage droplets and protect them from lipolytic degradation (Dalen et al., 2007
lipid storage droplet protein 5
, perilipin 5
, lipid droplet associated protein
, lipid droplet-associated protein PAT-1
, myocardial LD protein