Perilipins: A family of five fat-droplet storing proteins that play a significant role in fat homeostasis.

MASLD/MASH fatty liver hepatocellular carcinoma lipid droplets lipid homeostasis perilipins steatosis

Journal

Journal of cellular biochemistry
ISSN: 1097-4644
Titre abrégé: J Cell Biochem
Pays: United States
ID NLM: 8205768

Informations de publication

Date de publication:
15 May 2024
Historique:
revised: 18 04 2024
received: 27 02 2024
accepted: 30 04 2024
medline: 15 5 2024
pubmed: 15 5 2024
entrez: 15 5 2024
Statut: aheadofprint

Résumé

Lipid droplets are organelles with unique spherical structures. They consist of a hydrophobic neutral lipid core that varies depending on the cell type and tissue. These droplets are surrounded by phospholipid monolayers, along with heterogeneous proteins responsible for neutral lipid synthesis and metabolism. Additionally, there are specialized lipid droplet-associated surface proteins. Recent evidence suggests that proteins from the perilipin family (PLIN) are associated with the surface of lipid droplets and are involved in their formation. These proteins have specific roles in hepatic lipid droplet metabolism, such as protecting the lipid droplets from lipase action and maintaining a balance between lipid storage and utilization in specific cells. Metabolic dysfunction-associated steatotic liver disease (MASLD) is characterized by the accumulation of lipid droplets in more than 5% of the hepatocytes. This accumulation can progress into metabolic dysfunction-associated steatohepatitis, fibrosis, cirrhosis, and hepatocellular carcinoma. The accumulation of hepatic lipid droplets in the liver is associated with the progression of MASLD and other diseases such as sarcopenic obesity. Therefore, it is crucial to understand the role of perilipins in this accumulation, as these proteins are key targets for developing novel therapeutic strategies. This comprehensive review aims to summarize the structure and characteristics of PLIN proteins, as well as their pathogenic role in the development of hepatic steatosis and fatty liver diseases.

Identifiants

pubmed: 38747370
doi: 10.1002/jcb.30579
doi:

Types de publication

Journal Article Review

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : Interdisciplinary Center for Clinical Research within the faculty of Medicine at the RWTH Aachen University
ID : PTD 1-5
Organisme : Deutsche Krebshilfe
ID : 70115581
Organisme : Deutsche Forschungsgemeinschaft
ID : WE2554/13-1
Organisme : Deutsche Forschungsgemeinschaft
ID : WE2554/15-1
Organisme : Deutsche Forschungsgemeinschaft
ID : WE2554/17-1

Informations de copyright

© 2024 The Authors. Journal of Cellular Biochemistry published by Wiley Periodicals LLC.

Références

Chandrasekaran P, Weiskirchen R. The pivotal role of the membrane‐bound O‐acyltransferase domain containing 7 in non‐alcoholic fatty liver disease. Livers. 2024;4(1):1‐14. doi:10.3390/livers4010001
Olzmann JA, Carvalho P. Dynamics and functions of lipid droplets. Nat Rev Mol Cell Biol. 2019;20(3):137‐155. doi:10.1038/s41580-018-0085-z
Kimmel AR, Sztalryd C. The perilipins: major cytosolic lipid droplet–associated proteins and their roles in cellular lipid storage, mobilization, and systemic homeostasis. Annu Rev Nutr. 2016;36(1):471‐509. doi:10.1146/annurev-nutr-071813-105410
Itabe H, Yamaguchi T, Nimura S, Sasabe N. Perilipins: a diversity of intracellular lipid droplet proteins. Lipids Health Dis. 2017;16(1):83. doi:10.1186/s12944-017-0473-y
Chandrasekaran P, Weiskirchen R. The role of SCAP/SREBP as central regulators of lipid metabolism in hepatic steatosis. Int J Mol Sci. 2024b;25(2):1109. doi:10.3390/ijms25021109
Rinella ME, Lazarus JV, Ratziu V, et al. A multisociety delphi consensus statement on new fatty liver disease nomenclature. Hepatology. 2023;78(6):1966‐1986. doi:10.1097/HEP.0000000000000520
Xia M, Chandrasekaran P, Rong S, Fu X, Mitsche MA. Hepatic deletion of Mboat7 (LPIAT1) causes activation of SREBP‐1c and fatty liver. J Lipid Res. 2021;62:100031. doi:10.1194/jlr.RA120000856
Leow WQ, Chan AWH, Mendoza PGL, Lo R, Yap K, Kim H. Non‐alcoholic fatty liver disease: the pathologist's perspective. Clin Mol Hepatol. 2023;29(suppl):S302‐S318. doi:10.3350/cmh.2022.0329
Fernando DH, Forbes JM, Angus PW, Herath CB. Development and progression of non‐alcoholic fatty liver disease: the role of advanced glycation end products. Int J Mol Sci. 2019;20(20):5037. doi:10.3390/ijms20205037
Younossi ZM, Koenig AB, Abdelatif D, Fazel Y, Henry L, Wymer M. Global epidemiology of nonalcoholic fatty liver disease—meta‐analytic assessment of prevalence, incidence, and outcomes. Hepatology. 2016;64(1):73‐84. doi:10.1002/hep.28431
Chandrasekaran P, Weiskirchen R. The role of obesity in type 2 diabetes mellitus—an overview. Int J Mol Sci. 2024c;25(3):1882. doi:10.3390/ijms25031882
Benhamed F, Denechaud PD, Lemoine M, et al. The lipogenic transcription factor ChREBP dissociates hepatic steatosis from insulin resistance in mice and humans. J Clin Invest. 2012;122(6):2176‐2194. doi:10.1172/jci41636
Lambert JE, Ramos–Roman MA, Browning JD, Parks EJ. Increased de novo lipogenesis is a distinct characteristic of individuals with nonalcoholic fatty liver disease. Gastroenterology. 2014;146(3):726‐735. doi:10.1053/j.gastro.2013.11.049
Kaori M, Philippe G. Role of lipid droplet proteins in the development of NAFLD and hepatic insulin resistance. In: Rodrigo V, ed. Non‐Alcoholic Fatty Liver Disease. IntechOpen; 2017:Ch. 3. doi:10.5772/intechopen.71572
Ploegh HL. A lipid‐based model for the creation of an escape hatch from the endoplasmic reticulum. Nature. 2007;448(7152):435‐438. doi:10.1038/nature06004
Walther TC, Farese Jr. RV. The life of lipid droplets. Biochimica et Biophysica Acta (BBA) ‐ Molecular and Cell Biology of Lipids. 2009;1791(6):459‐466. doi:10.1016/j.bbalip.2008.10.009
Gong J, Sun Z, Li P. CIDE proteins and metabolic disorders. Curr Opin Lipidol. 2009;20(2):121‐126. doi:10.1097/MOL.0b013e328328d0bb
Jambunathan S, Yin J, Khan W, Tamori Y, Puri V. FSP27 promotes lipid droplet clustering and then fusion to regulate triglyceride accumulation. PLoS One. 2011;6(12):e28614. doi:10.1371/journal.pone.0028614
Chorlay A, Thiam AR. Neutral lipids regulate amphipathic helix affinity for model lipid droplets. J Cell Biol. 2020;219(4):e201907099. doi:10.1083/jcb.201907099
Bacle A, Gautier R, Jackson CL, Fuchs PFJ, Vanni S. Interdigitation between triglycerides and lipids modulates surface properties of lipid droplets. Biophys J. 2017;112(7):1417‐1430. doi:10.1016/j.bpj.2017.02.032
(a) Rowe ER, Mimmack ML, Barbosa AD, et al. Conserved amphipathic helices mediate lipid droplet targeting of perilipins 1‐3. J Biol Chem. 2016;291(13):6664‐6678. doi:10.1074/jbc.M115.691048
Correction in: J Biol Chem, 2022;298(1):101490. doi:10.1016/j.jbc.2021.101490
Mason RR, Mokhtar R, Matzaris M, et al. PLIN5 deletion remodels intracellular lipid composition and causes insulin resistance in muscle. Mol Metab. 2014;3(6):652‐663. doi:10.1016/j.molmet.2014.06.002
Mass‐Sanchez PB, Krizanac M, Stancl P, et al. Perlipin 5 depletion protects against nonalcoholic fatty liver disease and hepatocellular carcinoma by modulating lipid metabolism and inflammatory responses. Cell Death Disc. 2024;10(1):94. doi:10.1038/s41420-024-01860-4
Najt CP, Devarajan M, Mashek DG. Perilipins at a glance. J Cell Sci. 2022;135(5):jcs259501. doi:10.1242/jcs.259501
Kory N, Farese Jr. RV, Walther TC. Targeting fat: mechanisms of protein localization to lipid droplets. Trends Cell Biol. 2016;26(7):535‐546. doi:10.1016/j.tcb.2016.02.007
Hickenbottom SJ, Kimmel AR, Londos C, Hurley JH. Structure of a lipid droplet protein. Structure. 2004;12(7):1199‐1207. doi:10.1016/j.str.2004.04.021
Zhang S, Liu G, Xu C, et al. Perilipin 1 mediates lipid metabolism homeostasis and inhibits inflammatory cytokine synthesis in bovine adipocytes. Front Immunol. 2018;9:467. doi:10.3389/fimmu.2018.00467
Hansen JS, de Maré S, Jones HA, Göransson O, Lindkvist‐Petersson K. Visualization of lipid directed dynamics of perilipin 1 in human primary adipocytes. Sci Rep. 2017;7(1):15011. doi:10.1038/s41598-017-15059-4
Tomohiro Y, Naoto O, Emi M, et al. CGI‐58 facilitates lipolysis on lipid droplets but is not involved in the vesiculation of lipid droplets caused by hormonal stimulation. J Lipid Res. 2007;48(5):1078‐1089. doi:10.1194/jlr.M600493-JLR200
Zechner R, Kienesberger PC, Haemmerle G, Zimmermann R, Lass A. Adipose triglyceride lipase and the lipolytic catabolism of cellular fat stores. J Lipid Res. 2009;50(1):3‐21. doi:10.1194/jlr.R800031-JLR200
Fujii H, Ikura Y, Arimoto J, et al. Expression of perilipin and adipophilin in nonalcoholic fatty liver disease; relevance to oxidative injury and hepatocyte ballooning. J Atheroscler Thromb. 2009;16(6):893‐901. doi:10.5551/jat.2055
Simard JR, Meshulam T, Pillai BK, et al. Caveolins sequester FA on the cytoplasmic leaflet of the plasma membrane, augment triglyceride formation, and protect cells from lipotoxicity. J Lipid Res. 2010;51(5):914‐922. doi:10.1194/jlr.M900251
Sohn JH, Lee YK, Han JS, et al. Perilipin 1 (Plin1) deficiency promotes inflammatory responses in lean adipose tissue through lipid dysregulation. J Biol Chem. 2018;293(36):13974‐13988. doi:10.1074/jbc.ra118.003541
Miyoshi H, Souza SC, Endo M, et al. Perilipin overexpression in mice protects against diet‐induced obesity. J Lipid Res. 2010;51(5):975‐982. doi:10.1194/jlr.M002352
Tsai TH, Chen E, Li L, et al. The constitutive lipid droplet protein PLIN2 regulates autophagy in liver. Autophagy. 2017;13(7):1130‐1144. doi:10.1080/15548627.2017.1319544
McManaman JL, Bales ES, Orlicky DJ, et al. Perilipin‐2‐null mice are protected against diet‐induced obesity, adipose inflammation, and fatty liver disease. J Lipid Res. 2013;54(5):1346‐1359. doi:10.1194/jlr.M035063
Dalen KT, Ulven SM, Arntsen BM, Solaas K, Nebb HI. PPARα activators and fasting induce the expression of adipose differentiation‐related protein in liver. J Lipid Res. 2006;47(5):931‐943. doi:10.1194/jlr.M500459-JLR200
Masuda Y, Itabe H, Odaki M, et al. ADRP/adipophilin is degraded through the proteasome‐dependent pathway during regression of lipid‐storing cells. J Lipid Res. 2006;47(1):87‐98. doi:10.1194/jlr.M500170-JLR200
Takahashi Y, Shinoda A, Kamada H, Shimizu M, Inoue J, Sato R. Perilipin2 plays a positive role in adipocytes during lipolysis by escaping proteasomal degradation. Sci Rep. 2016;6(1):20975. doi:10.1038/srep20975
Kaushik S, Cuervo AM. Degradation of lipid droplet‐associated proteins by chaperone‐mediated autophagy facilitates lipolysis. Nature Cell Biol. 2015;17(6):759‐770. doi:10.1038/ncb3166
Straub BK, Stoeffel P, Heid H, Zimbelmann R, Schirmacher P. Differential pattern of lipid droplet‐associated proteins and de novo perilipin expression in hepatocyte steatogenesis. Hepatology. 2008;47(6):1936‐1946. doi:10.1002/hep.22268
Imai Y, Boyle S, Varela GM, et al. Effects of perilipin 2 antisense oligonucleotide treatment on hepatic lipid metabolism and gene expression. Physiol Genomics. 2012;44(22):1125‐1131. doi:10.1152/physiolgenomics.00045.2012
Libby AE, Bales E, Orlicky DJ, McManaman JL. Perilipin‐2 deletion impairs hepatic lipid accumulation by interfering with sterol regulatory element‐binding protein (SREBP) activation and altering the hepatic lipidome. J Biol Chem. 2016;291(46):24231‐24246. doi:10.1074/jbc.M116.759795
Conte M, Santoro A, Collura S, et al. Circulating perilipin 2 levels are associated with fat mass, inflammatory and metabolic markers and are higher in women than men. Aging. 2021;13(6):7931‐7942. doi:10.18632/aging.202840
Kurt B, Buendgens L, Wirtz TH, et al. Serum perilipin 2 (PLIN2) predicts multiple organ dysfunction in critically ill patients. Biomedicines. 2021;9(9):1210. doi:10.3390/biomedicines9091210
Magné J, Aminoff A, Sundelin JP, et al. The minor allele of the missense polymorphism Ser251Pro in perilipin 2 (PLIN2) disrupts an α‐helix, affects lipolysis, and is associated with reduced plasma triglyceride concentration in humans. FASEB J. 2013;27(8):3090‐3099. doi:10.1096/fj.13-228759
Motomura W, Inoue M, Ohtake T, et al. Up‐regulation of ADRP in fatty liver in human and liver steatosis in mice fed with high fat diet. Biochem Biophys Res Commun. 2006;340(4):1111‐1118. doi:10.1016/j.bbrc.2005.12.121
Li X, Ye J, Zhou L, Gu W, Fisher EA, Li P. Opposing roles of cell death‐inducing DFF45‐like effector B and perilipin 2 in controlling hepatic VLDL lipidation. J Lipid Res. 2012;53(9):1877‐1889. doi:10.1194/jlr.M026591
Najt CP, Senthivinayagam S, Aljazi MB, et al. Liver‐specific loss of perilipin 2 alleviates diet‐induced hepatic steatosis, inflammation, and fibrosis. American J Physiol Gastroint Liver Physiol. 2016;310(9):G726‐G738. doi:10.1152/ajpgi.00436.2015
Orlicky DJ, Libby AE, Bales ES, et al. Perilipin‐2 promotes obesity and progressive fatty liver disease in mice through mechanistically distinct hepatocyte and extra‐hepatocyte actions. J Physiol. 2019;597(6):1565‐1584. doi:10.1113/jp277140
Kaushik S, Cuervo AM. AMPK‐dependent phosphorylation of lipid droplet protein PLIN2 triggers its degradation by CMA. Autophagy. 2016;12(2):432‐438. doi:10.1080/15548627.2015.1124226
Libby AE, Bales ES, Monks J, Orlicky DJ, McManaman JL. Perilipin‐2 deletion promotes carbohydrate‐mediated browning of white adipose tissue at ambient temperature. J Lipid Res. 2018;59(8):1482‐1500. doi:10.1194/jlr.M086249
Xiong X, Bales ES, Ir D, et al. Perilipin‐2 modulates dietary fat‐induced microbial global gene expression profiles in the mouse intestine. Microbiome. 2017;5(1):117. doi:10.1186/s40168-017-0327-x
Khaddaj R, Stribny J, Cottier S, Schneiter R. Perilipin 3 promotes the formation of membrane domains enriched in diacylglycerol and lipid droplet biogenesis proteins. Front Cell Dev Biol. 2023;11:1116491. doi:10.3389/fcell.2023.1116491
Ohsaki Y, Maeda T, Maeda M, Tauchi‐Sato K, Fujimoto T. Recruitment of TIP47 to lipid droplets is controlled by the putative hydrophobic cleft. Biochem Biophys Res Commun. 2006;347(1):279‐287. doi:10.1016/j.bbrc.2006.06.074
Buers I, Robenek H, Lorkowski S, Nitschke Y, Severs NJ, Hofnagel O. TIP47, a lipid cargo protein involved in macrophage triglyceride metabolism. Arterioscler Thromb Vasc Biol. 2009;29(5):767‐773. doi:10.1161/atvbaha.108.182675
Tsuiki E, Fujita A, Ohsaki Y, et al. All‐trans‐retinol generated by rhodopsin photobleaching induces rapid recruitment of TIP47 to lipid droplets in the retinal pigment epithelium. Invest Opthalmol Visu Sci. 2007;48(6):2858‐2867. doi:10.1167/iovs.06-0768
Patel S, Yang W, Kozusko K, Saudek V, Savage DB. Perilipins 2 and 3 lack a carboxy‐terminal domain present in perilipin 1 involved in sequestering ABHD5 and suppressing basal lipolysis. Proc Nat Acad Sci. 2014;111(25):9163‐9168. doi:10.1073/pnas.1318791111
Dichlberger A, Schlager S, Lappalainen J, et al. Lipid body formation during maturation of human mast cells. J Lipid Res. 2011;52(12):2198‐2208. doi:10.1194/jlr.M019737
Nose F, Yamaguchi T, Kato R, et al. Crucial role of perilipin‐3 (TIP47) in formation of lipid droplets and PGE2 production in HL‐60‐derived neutrophils. PLoS One. 2013;8(8):e71542. doi:10.1371/journal.pone.0071542
Carr RM, Patel RT, Rao V, et al. Reduction of TIP47 improves hepatic steatosis and glucose homeostasis in mice. American J Physiol Regul Integrat Compa Physiol. 2012;302(8):R996‐R1003. doi:10.1152/ajpregu.00177.2011
Camera E, Dahlhoff M, Ludovici M, Zouboulis CC, Schneider MR. Perilipin 3 modulates specific lipogenic pathways in SZ95 sebocytes. Exp Dermatol. 2014;23(10):759‐761. doi:10.1111/exd.12507
Kleinert M, Parker BL, Chaudhuri R, et al. mTORC2 and AMPK differentially regulate muscle triglyceride content via Perilipin 3. Mol Metab. 2016;5(8):646‐655. doi:10.1016/j.molmet.2016.06.007
Sołtysik K, Ohsaki Y, Tatematsu T, Cheng J, Fujimoto T. Nuclear lipid droplets derive from a lipoprotein precursor and regulate phosphatidylcholine synthesis. Nat Commun. 2019;10(1):473. doi:10.1038/s41467-019-08411-x
Nimura S, Yamaguchi T, Ueda K, et al. Olanzapine promotes the accumulation of lipid droplets and the expression of multiple perilipins in human adipocytes. Biochem Biophys Res Commun. 2015;467(4):906‐912. doi:10.1016/j.bbrc.2015.10.045
Wolins NE, Quaynor BK, Skinner JR, et al. OP9 mouse stromal cells rapidly differentiate into adipocytes: characterization of a useful new model of adipogenesis. J Lipid Res. 2006;47(2):450‐460. doi:10.1194/jlr.D500037-JLR200
Kimmel AR, Brasaemle DL, McAndrews‐Hill M, Sztalryd C, Londos C. Adoption of PERILIPIN as a unifying nomenclature for the mammalian PAT‐family of intracellular lipid storage droplet proteins. J Lipid Res. 2010;51(3):468‐471. doi:10.1194/jlr.R000034
Kuramoto K, Okamura T, Yamaguchi T, et al. Perilipin 5, a lipid droplet‐binding protein, protects heart from oxidative burden by sequestering fatty acid from excessive oxidation. J Biol Chem. 2012;287(28):23852‐23863. doi:10.1074/jbc.M111.328708
Lin J, Chen A. Perilipin 5 restores the formation of lipid droplets in activated hepatic stellate cells and inhibits their activation. Lab Invest. 2016;96(7):791‐806. doi:10.1038/labinvest.2016.53
Trevino MB, Machida Y, Hallinger DR, et al. Perilipin 5 regulates islet lipid metabolism and insulin secretion in a cAMP‐dependent manner: implication of its role in the postprandial insulin secretion. Diabetes. 2015;64(4):1299‐1310. doi:10.2337/db14-0559
Ma SY, Sun KS, Zhang M, et al. Disruption of Plin5 degradation by CMA causes lipid homeostasis imbalance in NAFLD. Liver Int. 2020;40(10):2427‐2438. doi:10.1111/liv.14492
Dalen KT, Dahl T, Holter E, et al. LSDP5 is a PAT protein specifically expressed in fatty acid oxidizing tissues. Biochimica et Biophysica Acta (BBA). 2007;1771(2):210‐227. doi:10.1016/j.bbalip.2006.11.011
Kimmel AR, Sztalryd C. Perilipin 5, a lipid droplet protein adapted to mitochondrial energy utilization. Curr Opin Lipidol. 2014;25(2):110‐117. doi:10.1097/mol.0000000000000057
Wang H, Bell M, Sreenevasan U, et al. Unique regulation of adipose triglyceride lipase (ATGL) by perilipin 5, a lipid droplet‐associated protein. J Biol Chem. 2011;286(18):15707‐15715. doi:10.1074/jbc.M110.207779
Wang C, Zhao Y, Gao X, et al. Perilipin 5 improves hepatic lipotoxicity by inhibiting lipolysis. Hepatology. 2015;61(3):870‐882. doi:10.1002/hep.27409
Keenan SN, Meex RC, Lo JCY, et al. Perilipin 5 deletion in hepatocytes remodels lipid metabolism and causes hepatic insulin resistance in mice. Diabetes. 2019;68(3):543‐555. doi:10.2337/db18-0670
Bernsmeier C, Dill MT, Provenzano A, et al. Hepatic Notch1 deletion predisposes to diabetes and steatosis via glucose‐6‐phosphatase and perilipin‐5 upregulation. Lab Invest. 2016;96(9):972‐980. doi:10.1038/labinvest.2016.75
Langhi C, Marquart TJ, Allen RM, Baldán Á. Perilipin‐5 is regulated by statins and controls triglyceride contents in the hepatocyte. J Hepatol. 2014;61(2):358‐365. doi:10.1016/j.jhep.2014.04.009
Zhong W, Fan B, Cong H, Wang T, Gu J. Oleic acid‐induced perilipin 5 expression and lipid droplets formation are regulated by the PI3K/PPARα pathway in HepG2 cells. App Physiol Nutr Metabol. 2019;44(8):840‐848. doi:10.1139/apnm-2018-0729
Harris LALS, Skinner JR, Shew TM, Pietka TA, Abumrad NA, Wolins NE. Perilipin 5‐driven lipid droplet accumulation in skeletal muscle stimulates the expression of fibroblast growth factor 21. Diabetes. 2015;64(8):2757‐2768. doi:10.2337/db14-1035
Wang H, Sreenivasan U, Gong DW, et al. Cardiomyocyte‐specific perilipin 5 overexpression leads to myocardial steatosis and modest cardiac dysfunction. J Lipid Res. 2013;54(4):953‐965. doi:10.1194/jlr.M032466
Tan Y, Jin Y, Wang Q, Huang J, Wu X, Ren Z. Perilipin 5 protects against cellular oxidative stress by enhancing mitochondrial function in HepG2 cells. Cells. 2019;8(10):1241. doi:10.3390/cells8101241
Asimakopoulou A, Engel KM, Gassler N, et al. Deletion of Perilipin 5 protects against hepatic injury in nonalcoholic fatty liver disease via missing inflammasome activation. Cells. 2020;9(6):1346. doi:10.3390/cells9061346
Asimakopoulou A, Borkham‐Kamphorst E, Henning M, et al. Lipocalin‐2 (LCN2) regulates PLIN5 expression and intracellular lipid droplet formation in the liver. Biochimica et Biophysica Acta (BBA). 2014;1841(10):1513‐1524. doi:10.1016/j.bbalip.2014.07.017
Mastoridou EM, Goussia AC, Kanavaros P, Charchanti AV. Involvement of lipophagy and chaperone‐mediated autophagy in the pathogenesis of non‐alcoholic fatty liver disease by regulation of lipid droplets. Int J Mol Sci. 2023;24(21):15891. doi:10.3390/ijms242115891
Chandrasekaran P, Weiskirchen R. Cellular and molecular mechanisms of insulin resistance. Curr Tissue Microenviro Rep. 2024. doi:10.1007/s43152-024-00056-3
Tarantino G, Sinatti G, Citro V, Santini S, Balsano C. Sarcopenia, a condition shared by various diseases: can we alleviate or delay the progression. Intern Emerg Med. 2023;18(7):1887‐1895. doi:10.1007/s11739-023-03339-z
Son SW, Song DS, Chang UI, Yang JM. Definition of sarcopenia in chronic liver disease. Life (Basel, Switzerland). 2021;11(4):349. doi:10.3390/life11040349
Wiedmer P, Jung T, Castro JP, et al. Sarcopenia – molecular mechanisms and open questions. Ageing Res Rev. 2021;65:101200. doi:10.1016/j.arr.2020.101200
Conte M, Vasuri F, Trisolino G, et al. Increased Plin2 expression in human skeletal muscle is associated with sarcopenia and muscle weakness. PLoS One. 2013;8(8):e73709. doi:10.1371/journal.pone.0073709
Conte M, Vasuri F, Bertaggia E, et al. Differential expression of perilipin 2 and 5 in human skeletal muscle during aging and their association with atrophy‐related genes. Biogerontology. 2015;16(3):329‐340. doi:10.1007/s10522-014-9549-5
Erratum in: Biogerontology 2015;16(3):341.
Bosma M, Hesselink MKC, Sparks LM, et al. Perilipin 2 improves insulin sensitivity in skeletal muscle despite elevated intramuscular lipid levels. Diabetes. 2012;61(11):2679‐2690. doi:10.2337/db11-1402
Kalinkovich A, Livshits G. Sarcopenic obesity or obese sarcopenia: A cross talk between age‐associated adipose tissue and skeletal muscle inflammation as a main mechanism of the pathogenesis. Ageing Res Rev. 2017;35:200‐221. doi:10.1016/j.arr.2016.09.008
Affourtit C. Mitochondrial involvement in skeletal muscle insulin resistance: A case of imbalanced bioenergetics. Biochimica et Biophysica Acta. 2016;1857(10):1678‐1693. doi:10.1016/j.bbabio.2016.07.008
Bosma M, Sparks LM, Hooiveld GJ, et al. Overexpression of PLIN5 in skeletal muscle promotes oxidative gene expression and intramyocellular lipid content without compromising insulin sensitivity. Biochimica et Biophysica Acta (BBA). 2013;1831(4):844‐852. doi:10.1016/j.bbalip.2013.01.007
Cho KA, Kang PB. PLIN2 inhibits insulin‐induced glucose uptake in myoblasts through the activation of the NLRP3 inflammasome. Int J Mol Med. 2015;36(3):839‐844. doi:10.3892/ijmm.2015.2276
Conte M, Franceschi C, Sandri M, Salvioli S. Perilipin 2 and age‐related metabolic diseases: a new perspective. Trend Endocrinol Metabol. 2016;27(12):893‐903. doi:10.1016/j.tem.2016.09.001
Sharma A. Lipid droplets associated perilipins protein insights into finding a therapeutic target approach to cure non‐alcoholic fatty liver disease (NAFLD. Fut J Pharmaceut Sci. 2022;8(1):1. doi:10.1186/s43094-021-00395-0
Xu X, Park JG, So JS, Lee AH. Transcriptional activation of Fsp27 by the liver‐enriched transcription factor CREBH promotes lipid droplet growth and hepatic steatosis. Hepatology. 2015;61(3):857‐869. doi:10.1002/hep.27371
Rajamoorthi A, Lee RG, Baldán Á. Therapeutic silencing of FSP27 reduces the progression of atherosclerosis in ldlr‐/‐ mice. Atherosclerosis. 2018;275:43‐49. doi:10.1016/j.atherosclerosis.2018.05.045
Gupta A, Balakrishnan B, Karki S, et al. Human CIDEC transgene improves lipid metabolism and protects against high‐fat diet‐induced glucose intolerance in mice. J Biol Chem. 2022;298(9):102347. doi:10.1016/j.jbc.2022.102347

Auteurs

Preethi Chandrasekaran (P)

UT Southwestern Medical Center Dallas, Dallas, Texas, USA.

Sabine Weiskirchen (S)

Institute of Molecular Pathobiochemistry, Experimental Gene Therapy and Clinical Chemistry (IFMPEGKC), Rheinisch-Westfälische Technische Hochschule (RWTH), University Hospital Aachen, Aachen, Germany.

Ralf Weiskirchen (R)

Institute of Molecular Pathobiochemistry, Experimental Gene Therapy and Clinical Chemistry (IFMPEGKC), Rheinisch-Westfälische Technische Hochschule (RWTH), University Hospital Aachen, Aachen, Germany.

Classifications MeSH