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      Deciphering the Role of Lipid Droplets in Cardiovascular Disease : A Report From the 2017 National Heart, Lung, and Blood Institute Workshop

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          Abstract

          Lipid droplets (LDs) are distinct and dynamic organelles that affect the health of cells and organs. Much progress has been made in understanding how these structures are formed, how they interact with other cellular organelles, how they are used for storage of triacylglycerol in adipose tissue, and how they regulate lipolysis. Our understanding of the biology of LDs in the heart and vascular tissue is relatively primitive in comparison with LDs in adipose tissue and liver. The National Heart, Lung, and Blood Institute convened a working group to discuss how LDs affect cardiovascular diseases. The goal of the working group was to examine the current state of knowledge on the cell biology of LDs, including current methods to study them in cells and organs and reflect on how LDs influence the development and progression of cardiovascular diseases. This review summarizes the working group discussion and recommendations on research areas ripe for future investigation that will likely improve our understanding of atherosclerosis and heart function.

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          FAT SIGNALS - Lipases and Lipolysis in Lipid Metabolism and Signaling

          Rudolf Zechner, Robert Zimmermann, Thomas O. Eichmann … (2012)
          Lipolysis is defined as the catabolism of triacylglycerols stored in cellular lipid droplets. Recent discoveries of essential lipolytic enzymes and characterization of numerous regulatory proteins and mechanisms have fundamentally changed our perception of lipolysis and its impact on cellular metabolism. New findings that lipolytic products and intermediates participate in cellular signaling processes and that “lipolytic signaling” is particularly important in many nonadipose tissues unveil a previously underappreciated aspect of lipolysis, which may be relevant for human disease.
          Article 0 comments Cited 372 times – based on 0 reviews     Review now
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            ATGL-mediated fat catabolism regulates cardiac mitochondrial function via PPAR-α and PGC-1.

            Guenter Haemmerle, Tarek Moustafa, Gerald Woelkart … (2011)
            Peroxisome proliferator-activated receptors (PPARs) are nuclear hormone receptors that regulate genes involved in energy metabolism and inflammation. For biological activity, PPARs require cognate lipid ligands, heterodimerization with retinoic X receptors, and coactivation by PPAR-γ coactivator-1α or PPAR-γ coactivator-1β (PGC-1α or PGC-1β, encoded by Ppargc1a and Ppargc1b, respectively). Here we show that lipolysis of cellular triglycerides by adipose triglyceride lipase (patatin-like phospholipase domain containing protein 2, encoded by Pnpla2; hereafter referred to as Atgl) generates essential mediator(s) involved in the generation of lipid ligands for PPAR activation. Atgl deficiency in mice decreases mRNA levels of PPAR-α and PPAR-δ target genes. In the heart, this leads to decreased PGC-1α and PGC-1β expression and severely disrupted mitochondrial substrate oxidation and respiration; this is followed by excessive lipid accumulation, cardiac insufficiency and lethal cardiomyopathy. Reconstituting normal PPAR target gene expression by pharmacological treatment of Atgl-deficient mice with PPAR-α agonists completely reverses the mitochondrial defects, restores normal heart function and prevents premature death. These findings reveal a potential treatment for the excessive cardiac lipid accumulation and often-lethal cardiomyopathy in people with neutral lipid storage disease, a disease marked by reduced or absent ATGL activity.
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              The perilipin family of lipid droplet proteins: Gatekeepers of intracellular lipolysis.

              Carole Sztalryd, Dawn Brasaemle (2017)
              Lipid droplets in chordates are decorated by two or more members of the perilipin family of lipid droplet surface proteins. The perilipins sequester lipids by protecting lipid droplets from lipase action. Their relative expression and protective nature is adapted to the balance of lipid storage and utilization in specific cells. Most cells of the body have tiny lipid droplets with perilipins 2 and 3 at the surfaces, whereas specialized fat-storing cells with larger lipid droplets also express perilipins 1, 4, and/or 5. Perilipins 1, 2, and 5 modulate lipolysis by controlling the access of lipases and co-factors of lipases to substrate lipids stored within lipid droplets. Although perilipin 2 is relatively permissive to lipolysis, perilipins 1 and 5 have distinct control mechanisms that are altered by phosphorylation. Here we evaluate recent progress toward understanding functions of the perilipins with a focus on their role in regulating lipolysis and autophagy. This article is part of a Special Issue entitled: Recent Advances in Lipid Droplet Biology edited by Rosalind Coleman and Matthijs Hesselink.
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                Author and article information

                Journal
                Title: Circulation
                Abbreviated Title: Circulation
                Publisher: Ovid Technologies (Wolters Kluwer Health)
                ISSN (Print): 0009-7322
                ISSN (Electronic): 1524-4539
                Publication date Created: July 17 2018
                Publication date (Print): July 17 2018
                Volume: 138
                Issue: 3
                Pages: 305-315
                Affiliations
                [1 ]New York University, New York City (I.J.G., E.A.F.).
                [2 ]University of California, Los Angeles (K.R.).
                [3 ]Washington University in St. Louis, MO (N.A.A., J.E.S.).
                [4 ]University of Texas Southwestern Medical Center, Dallas (P.E.B.).
                [5 ]University of North Carolina at Chapel Hill (S.C.).
                [6 ]National Institutes of Health/National, Heart, Lung, and Blood Institute, Bethesda, MD (Z.S.G., M.O., L.S.-L., J.C.).
                [7 ]Wayne State University, Detroit, MI (J.G.G.).
                [8 ]The Ohio State University Wexner Medical Center, Columbus (E.D.L.).
                [9 ]University of Colorado Denver (R.M.).
                [10 ]Yale University, Howard Hughes Medical Institute, New Haven, CT (G.I.S.).
                [11 ]Harvard University, Howard Hughes Medical Institute, Boston, MA (T.C.W.).
                Article
                DOI: 10.1161/CIRCULATIONAHA.118.033704
                PMC ID: 6056021
                PubMed ID: 30012703
                SO-VID: 5797979b-51ee-497e-8384-8b68b2d7b5c4
                Copyright © © 2018
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