Perilipin, a major hormonally regulated adipocyte-specific phosphoprotein associated with the periphery of lipid storage droplets

Greenberg, Andrew S.; Egan, John J.; Wek, Sheree A.; Garty, Nira B.; Blanchette‐Mackie, E. Joan; Londos, Constantine

doi:10.1016/s0021-9258(18)99168-4

Cited by 719 publications

(141 citation statements)

References 34 publications

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“…Adipophilin is a ubiquitously expressed protein in all mammalian cell types and is found only in lipid droplets and in no other subcellular compartment (Brasaemle et al 1997b; Heid et al 1998). Perilipin, a structurally related protein, associates with lipid droplets in adipocytes and steriodogenic cells (Greenberg et al 1991; Blanchette-Mackie et al 1995; Servetnick et al 1995). In these cells it restricts the access of hormone-sensitive lipase and other cytosolic lipases to the lipid droplet under basal conditions (Souza et al 1998,2002; Brasaemle et al 2000b; Martinez-Botas et al 2000; Tansey et al 2001), and facilitates lipase access to the droplet under lipolytically stimulating conditions (Tansey et al 2001; Souza et al 2002).…”

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confidence: 99%

Fixation Methods for the Study of Lipid Droplets by Immunofluorescence Microscopy

DiDonato

Brasaemle

2003

J Histochem Cytochem.

132

124

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S U M M A R YThe study of proteins associated with lipid droplets in adipocytes and many other cells is a rapidly developing area of inquiry. Although lipid droplets are easily visible by light microscopy, few standardized microscopy methods have been developed. Several methods of chemical fixation have recently been used to preserve cell structure before visualization of lipid droplets by light microscopy. We tested the most commonly used methods to compare the effects of the fixatives on cellular lipid content and lipid droplet structure. Cold methanol fixation has traditionally been used before visualization of cytoskeletal elements. We found this method unacceptable for study of lipid droplets because it extracted the majority of cellular phospholipids and promoted fusion of lipid droplets. Cold acetone fixation is similarly unacceptable because the total cellular lipids are extracted, causing collapse of the shell of lipid droplet-associated proteins. Fixation of cells with paraformaldehyde is the method of choice, because the cells retain their lipid content and lipid droplet structure is unaffected. As more lipid droplet-associated proteins are discovered and studied, it is critical to use appropriate methods to avoid studying artifacts. L ipid droplets are found in many different organisms and across many different tissues and cell types. Although the lipid droplets within adipocytes in the adipose tissue of animals are the largest and most easily observed, these specialized structures have been found across the biological kingdom and are now characterized as ubiquitous components of most types of cells (Murphy 2001). Lipid droplets play an important role in lipid storage and trafficking in mammalian cells. These structures provide energy and substrates for synthesis and repair of cell membranes in most types of cells, for synthesis of mediators of the inflammatory response, for steroid hormone biosynthesis in adrenal cortical, testis, and ovarian cells, for surfactant synthesis in lung, and for secretion of the lipid component of milk from mammary epithelial cells (Murphy 2001). In addition, the accumulation of cholesterol esters in lipid droplets in macrophages leads to the formation of foam cells, which play a major role in the development of atherosclerotic lesions. In each cell type, some of the proteins that are associated with the surfaces of lipid droplets regulate the accumulation and mobilization of the lipids that fulfill these functions.To date, only a few lipid droplet-associated proteins have been identified. Adipophilin is a ubiquitously expressed protein in all mammalian cell types and is found only in lipid droplets and in no other subcellular compartment (Brasaemle et al. 1997b;Heid et al. 1998). Perilipin, a structurally related protein, associates with lipid droplets in adipocytes and steriodogenic cells (Greenberg et al. 1991; BlanchetteMackie et al. 1995;Servetnick et al. 1995). In these cells it restricts the access of hormone-sensitive lipase and other cytosolic lipases to the lip...

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mentioning

confidence: 99%

Fixation Methods for the Study of Lipid Droplets by Immunofluorescence Microscopy

DiDonato

Brasaemle

2003

J Histochem Cytochem.

132

124

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“…All five members of the perilipin family of proteins were detected in MLD of piglets in our study with mainly distinct localizations. The first member, PLIN1, was originally discovered in adipocytes ( 35 ) surrounding lipid droplets ( 36 ). Other PLINs were consecutively detected.…”

Section: Discussionmentioning

confidence: 99%

“…However, PLIN1 starts to promote triglyceride hydrolysis when it is phosphorylated by protein kinase A (38). In previous experiments, PLIN1 was discovered to be around large adipocytes (35,39) and was thought to be restricted within white and brown adipose tissue or steroidogenic cells (40,41).…”

Section: Different Localizations Of Perilipins Within M Longissimus Suggest Diverse Functionsmentioning

confidence: 99%

Distinct Roles of Perilipins in the Intramuscular Deposition of Lipids in Glutamine-Supplemented, Low-, and Normal-Birth-Weight Piglets

Zhao

Albrecht

et al. 2021

Front. Vet. Sci.

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Piglets with low birth weight (LBW) usually have reduced muscle mass and increased lipid deposition compared with their normal-birth-weight (NBW) littermates. Supplementation of piglets with amino acids during the first days of life may improve muscle growth and simultaneously alter the intramuscular lipid deposition. The aim of the current study was to investigate the influence of glutamine (Gln) supplementation during the early suckling period on lipid deposition in the longissimus muscle (MLD) and the role of different perilipin (PLIN) family members in this process. Four groups were generated consisting of 72 male LBW piglets and 72 NBW littermates. Piglets were supplemented with either 1 g Gln/kg body weight or an isonitrogenous amount of alanine (Ala) between days post natum (dpn) 1 and 12. Twelve piglets per group were slaughtered at 5, 12, and 26 dpn, and muscle tissue was collected. Perilipins were localized by immunohistochemistry in muscle sections. The mRNA and protein abundances of PLIN family members and related lipases were quantified by quantitative RT-PCR (qPCR) and western blots, respectively. While PLIN1 was localized around lipid droplets in mature and developing adipocytes, PLIN2 was localized at intramyocellular lipid droplets, PLIN3 and 4 at cell membranes of muscle fibers and adipocytes, and PLIN5 in the cytoplasm of undefined cells. The western blot results indicated higher protein abundances of PLIN2, 3, 4, and 5 in LBW piglets (p < 0.05) at 5 dpn compared with their NBW littermates independent of supplementation, while not directly reflecting the mRNA expression levels. The mRNA abundance of PLIN2 was lower while PLIN4 was higher in piglets at 26 dpn in comparison with piglets at 5 dpn (p < 0.01). Relative mRNA expression of LPL and CGI-58 was lowest in piglets at 5 dpn (p < 0.001). However, ATGL mRNA was not influenced by birth weight or supplementation, but the Spearman correlation coefficient analysis revealed close correlations with PLIN2, 4, and 5 mRNA at 5 and 26 dpn (r > 0.5, p < 0.001). The results indicated the importance of birth weight and age for intramuscular lipid deposition and different roles of PLIN family members in this process, but no clear modulating effect of Gln supplementation.

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“…TAG and cholesterol esters, while a peripheral monolayer is composed of phospholipids with attached proteins with structural and functional roles as depicted in Figure 1 [1]. Perilipins were initially localized in the phospholipid monolayer of LDs in the 1990s [4][5][6] and it was not until 2010 that the "perilipin family protein: PAT protein" was suggested to unify the name of this family [7]. Perilipins are a family comprising five distinct proteins, whose expression varies depending on the tissue.…”

Section: Introductionmentioning

confidence: 99%

Understanding the Role of Perilipin 5 in Non-Alcoholic Fatty Liver Disease and Its Role in Hepatocellular Carcinoma: A Review of Novel Insights

Sanchez

Krizanac

Weiskirchen

et al. 2021

IJMS

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Consumption of high-calorie foods, such as diets rich in fats, is an important factor leading to the development of steatohepatitis. Several studies have suggested how lipid accumulation creates a lipotoxic microenvironment for cells, leading cells to deregulate their transcriptional and translational activity. This deregulation induces the development of liver diseases such as non-alcoholic fatty liver disease (NAFLD) and subsequently also the appearance of hepatocellular carcinoma (HCC) which is one of the deadliest types of cancers worldwide. Understanding its pathology and studying new biomarkers with better specificity in predicting disease prognosis can help in the personalized treatment of the disease. In this setting, understanding the link between NAFLD and HCC progression, the differentiation of each stage in between as well as the mechanisms underlying this process, are vital for development of new treatments and in exploring new therapeutic targets. Perilipins are a family of five closely related proteins expressed on the surface of lipid droplets (LD) in several tissues acting in several pathways involved in lipid metabolism. Recent studies have shown that Plin5 depletion acts protectively in the pathogenesis of liver injury underpinning the importance of pathways associated with PLIN5. PLIN5 expression is involved in pro-inflammatory cytokine regulation and mitochondrial damage, as well as endoplasmic reticulum (ER) stress, making it critical target of the NAFLD-HCC studies. The aim of this review is to dissect the recent findings and functions of PLIN5 in lipid metabolism, metabolic disorders, and NAFLD as well as the progression of NAFLD to HCC.

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Perilipin, a major hormonally regulated adipocyte-specific phosphoprotein associated with the periphery of lipid storage droplets

Cited by 719 publications

References 34 publications

Fixation Methods for the Study of Lipid Droplets by Immunofluorescence Microscopy

Fixation Methods for the Study of Lipid Droplets by Immunofluorescence Microscopy

Distinct Roles of Perilipins in the Intramuscular Deposition of Lipids in Glutamine-Supplemented, Low-, and Normal-Birth-Weight Piglets

Understanding the Role of Perilipin 5 in Non-Alcoholic Fatty Liver Disease and Its Role in Hepatocellular Carcinoma: A Review of Novel Insights

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