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      FAT SIGNALS - Lipases and Lipolysis in Lipid Metabolism and Signaling

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          Abstract

          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.

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          Genetic variation in PNPLA3 confers susceptibility to nonalcoholic fatty liver disease

          Stefano Romeo, Julia Kozlitina, Chao Xing … (2008)
          Nonalcoholic fatty liver disease (NAFLD) is a burgeoning health problem of unknown etiology that varies in prevalence among ethnic groups. To identify genetic variants contributing to differences in hepatic fat content, we performed a genome-wide association scan of nonsynonymous sequence variations (n=9,229) in a multiethnic population. An allele in PNPLA3 (rs738409; I148M) was strongly associated with increased hepatic fat levels (P=5.9×10−10) and with hepatic inflammation (P=3.7×10−4). The allele was most common in Hispanics, the group most susceptible to NAFLD; hepatic fat content was > 2-fold higher in PNPLA3-148M homozygotes than in noncarriers. Resequencing revealed another allele associated with lower hepatic fat content in African-Americans, the group at lowest risk of NAFLD. Thus, variation in PNPLA3 contributes to ethnic and inter-individual differences in hepatic fat content and susceptibility to NAFLD.
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            Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase.

            Robert Zimmermann, Juliane G. Strauss, Guenter Haemmerle … (2004)
            Mobilization of fatty acids from triglyceride stores in adipose tissue requires lipolytic enzymes. Dysfunctional lipolysis affects energy homeostasis and may contribute to the pathogenesis of obesity and insulin resistance. Until now, hormone-sensitive lipase (HSL) was the only enzyme known to hydrolyze triglycerides in mammalian adipose tissue. Here, we report that a second enzyme, adipose triglyceride lipase (ATGL), catalyzes the initial step in triglyceride hydrolysis. It is interesting that ATGL contains a "patatin domain" common to plant acyl-hydrolases. ATGL is highly expressed in adipose tissue of mice and humans. It exhibits high substrate specificity for triacylglycerol and is associated with lipid droplets. Inhibition of ATGL markedly decreases total adipose acyl-hydrolase activity. Thus, ATGL and HSL coordinately catabolize stored triglycerides in adipose tissue of mammals.
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              Identification of a lipokine, a lipid hormone linking adipose tissue to systemic metabolism.

              Haiming Cao, Kristin A. Gerhold, Jared Mayers … (2008)
              Dysregulation of lipid metabolism in individual tissues leads to systemic disruption of insulin action and glucose metabolism. Utilizing quantitative lipidomic analyses and mice deficient in adipose tissue lipid chaperones aP2 and mal1, we explored how metabolic alterations in adipose tissue are linked to whole-body metabolism through lipid signals. A robust increase in de novo lipogenesis rendered the adipose tissue of these mice resistant to the deleterious effects of dietary lipid exposure. Systemic lipid profiling also led to identification of C16:1n7-palmitoleate as an adipose tissue-derived lipid hormone that strongly stimulates muscle insulin action and suppresses hepatosteatosis. Our data reveal a lipid-mediated endocrine network and demonstrate that adipose tissue uses lipokines such as C16:1n7-palmitoleate to communicate with distant organs and regulate systemic metabolic homeostasis.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Cell Metab
                Journal ID (iso-abbrev): Cell Metab
                Title: Cell Metabolism
                Publisher: Cell Press
                ISSN (Print): 1550-4131
                ISSN (Electronic): 1932-7420
                Publication date PMC-release: 07 March 2012
                Publication date (Print): 07 March 2012
                Volume: 15
                Issue: 3
                Pages: 279-291
                Affiliations
                [1 ]Institute of Molecular Biosciences, University of Graz, Austria
                Author notes
                [∗ ]Corresponding author rudolf.zechner@ 123456uni-graz.at
                Article
                Publisher ID: CMET1055
                DOI: 10.1016/j.cmet.2011.12.018
                PMC ID: 3314979
                PubMed ID: 22405066
                SO-VID: 86ce38a4-5825-4255-b635-5e1b0ab98c24
                Copyright © © 2012 ELL & Excerpta Medica.
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                This document may be redistributed and reused, subject to certain conditions.

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                ScienceOpen disciplines: Cell biology
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                ScienceOpen disciplines: Cell biology

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