Perilipin 5 Proteins (PLIN5)

Pig (Porcine) Perilipin 5 (PLIN5) interaction partners

1. C/EBPalpha is an essential regulatory factor for perilipin5 transcription and suggest that fasting stimulates perilipin5 transcription through influencing C/EBPalpha expression.

Human Perilipin 5 (PLIN5) interaction partners

1. Even though total PLIN5 protein content was almost double in Trained versus type 2 diabetes patients, PLIN5 coating did not affect lipid droplet number or size significantly.

2. 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.

3. Using two super-resolution imaging approaches, the study shows that in sections of human skeletal muscle PLIN2 and PLIN5 localize to lipid droplets (LD) at distinct sites, with abundance of PLIN5 at LD-mitochondria tethering sites.

4. 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.

5. Notch1 expression is reduced and glucose-6-phosphatase and perilipin-5 (G6PC/PLIN5) are upregulated in liver biopsies from nonalcoholic steatohepatitis (NASH) and nonalcoholic fatty liver disease (NAFLD) patients.

6. High oxygen consumption in middle-aged men was reflected in higher perilipin 5 expression in skeletal muscle.

7. PLIN5 was significantly colocated with ATGL, mitochondria and CGI-58, indicating a close association between the key lipolytic effectors in resting skeletal muscle.

8. Perilipin 5 as a lipid droplet protein adapted to mitochondrial energy utilization

9. Sprint interval and traditional endurance training increase net intramuscular triglyceride breakdown and expression of perilipin 2 and 5

10. PLIN5 likely plays an important role in intramyocellular lipid accumulation and oxidation, both of which increase with endurance training in human skeletal muscle.

11. The lipid droplet coat protein perilipin 5 also localizes to muscle mitochondria.

12. 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]

13. interaction of ATGL with CGI-58 increased lipolysis, whereas interaction of ATGL with perilipin 5 decreased lipolysis.

14. Results indicate involvement of OXPAT and ADRP in muscular lipid accumulation and type 2 diabetes.

Mouse (Murine) Perilipin 5 (PLIN5) interaction partners

1. Study show that Plin5 is an important modulator of intrahepatic lipid metabolism and suggest that the increased Plin5 expression that occurs with overnutrition may play an important role in preventing hepatic insulin resistance.

2. Our data highlight a protective role of Plin5 against hepatic lipotoxic injuries induced by HCV NS5A, which is helpful for understanding the steatosis and injuries in liver during HCV infection.

3. perilipin 5 and liver fatty acid binding protein function to restore quiescence in mouse hepatic stellate cells

4. 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.

5. During catecholamine-stimulated lipolysis, Perilipin 5 is phosphorylated by protein kinase A and forms transcriptional complexes with PGC-1alpha and SIRT1 in the nucleus. Perilipin 5 promotes PGC-1alpha co-activator function by disinhibiting SIRT1 deacetylase activity.

6. Changes in lipid metabolism resulting from PLIN5 deletion reduce ER stress in muscle, decrease FGF21 production by muscle and liver, and impair glycemic control.

7. 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.

8. 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.

9. mitochondria isolated from hearts deficient in Plin5, have specific functional defects

10. Plin5 deficiency alters cardiac lipid metabolism and associates with reduced survival following myocardial ischemia.

11. Data show that glucose-6-phosphatase and perilipin-5 (G6PC/PLIN5) are upregulated in notch1 knockout (KO) mice.

12. 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.

13. High fat diet-induced liver fibrosis is accompanied by an approximate 75% reduction in Plin5 in hepatic stellate cells (HSC), and spontaneous activation of primary HSC produces temporally coincident loss of Plin5 expression and lipid droplet depletion.

14. Here, we identify synthetic ligands that release ABHD5 from PLIN1 or PLIN5 without PKA activation and rapidly activate adipocyte and muscle lipolysis.

15. the increase in liver PLIN5 during hepatosteatosis drives further lipid accumulation but does not adversely affect hepatic health or insulin sensitivity.

16. upregulating the PLIN5 level in skeletal muscle drives expression of the FGF21 gene in fast-twitch fibers and is metabolically protective.

17. the elevation of islet PLIN5 during fasting allows partitioning of fatty acids into lipid droplets that is released upon refeeding to support postprandial insulin secretion in cAMP- and GPR40-dependent manners.

18. protein kinase A and perilipin 5 interact to regulate cardiac lipolysis

19. found that Plin5 expression was increased in steatotic livers

20. Results suggest that Plin5 allows excess triacylglycerol accumulation in the hearts of mice with streptozotocin-induced type 1 diabetes.