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      Retinyl ester hydrolases and their roles in vitamin A homeostasis

      review-article
      , , , , , *
      Biochimica et Biophysica Acta
      Elsevier Pub. Co
      13cIMH, 13-cis isomerohydrolase, ARAT, acyl-CoA:retinol acyltransferase, AREH, acid retinyl ester hydrolase, ATGL, adipose triglyceride lipase, BBB, blood-brain-barrier, BPL-B, brush-border phospholipase B, CE, cholesteryl ester, CEL, carboxyl ester lipase, CES, carboxylesterase, CGI-58, comparative gene identification 58, CM, chylomicron, CRBP1, cellular retinol-binding protein 1, DGAT1, acyl-CoA:diacylglycerol acyltransferase 1, ER, endoplasmic reticulum, Es2, esterase 2, Es3, esterase 3, Es4, esterase 4, Es10, esterase 10, Es22, esterase 22, FA, fatty acid, GPIHBP1, glycosylphosphatidylinositol-anchored high-density-lipoprotein binding protein 1 , GS2, gene sequence 2, HL, hepatic lipase, HSC, hepatic stellate cell, HSL, hormone-sensitive lipase, HSPG, heparan sulphate proteoglycan, ko, knock-out, LD, lipid droplet, LRAT, lecithin:retinol acyltransferase, LRP-1, low-density lipoprotein-receptor protein 1, LPL, lipoprotein lipase, MG, monoacylglycerol, MGL, monoglyceride lipase, NREH, neutral retinyl ester hydrolase, PL, phospholipid, PLRP2, pancreatic lipase-related protein 2, PNPLA, patatin-like phospholipase domain containing, PTL, pancreatic triglyceride lipase, RA, retinoic acid, RARα/β, retinoic acid receptor alpha/beta, RBP4, retinol-binding protein 4, RPE, retinal pigment epithelium, RXRα/β/γ, retinoid X receptor alpha/beta/gamma, RE, retinyl ester, REH, retinyl ester hydrolase, STRA6, stimulated by retinoic acid gene 6, STS, steroid sulfatase, TG, triacylglycerol, TIP47, tail-interacting protein of 47 kDa, VLDL, very low-density lipoprotein, wt, wild-type, Vitamin A, Retinyl ester hydrolase, Lipid droplet, Mobilization, Neutral lipid, Store

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          Abstract

          In mammals, dietary vitamin A intake is essential for the maintenance of adequate retinoid (vitamin A and metabolites) supply of tissues and organs. Retinoids are taken up from animal or plant sources and subsequently stored in form of hydrophobic, biologically inactive retinyl esters (REs). Accessibility of these REs in the intestine, the circulation, and their mobilization from intracellular lipid droplets depends on the hydrolytic action of RE hydrolases (REHs). In particular, the mobilization of hepatic RE stores requires REHs to maintain steady plasma retinol levels thereby assuring constant vitamin A supply in times of food deprivation or inadequate vitamin A intake. In this review, we focus on the roles of extracellular and intracellular REHs in vitamin A metabolism. Furthermore, we will discuss the tissue-specific function of REHs and highlight major gaps in the understanding of RE catabolism. This article is part of a Special Issue entitled Retinoid and Lipid Metabolism.

          Highlights

          ► For the maintenance of constant vitamin A supply retinyl ester hydrolases are required. ► This review summarizes the current knowledge on the roles of retinyl ester hydrolyses in vitamin A metabolism. ► In addition, it discusses tissue-specific functions of retinyl ester hydrolases and highlights major gaps in the understanding of retinyl ester catabolism.

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          Most cited references185

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          Liver fibrosis.

          Liver fibrosis is the excessive accumulation of extracellular matrix proteins including collagen that occurs in most types of chronic liver diseases. Advanced liver fibrosis results in cirrhosis, liver failure, and portal hypertension and often requires liver transplantation. Our knowledge of the cellular and molecular mechanisms of liver fibrosis has greatly advanced. Activated hepatic stellate cells, portal fibroblasts, and myofibroblasts of bone marrow origin have been identified as major collagen-producing cells in the injured liver. These cells are activated by fibrogenic cytokines such as TGF-beta1, angiotensin II, and leptin. Reversibility of advanced liver fibrosis in patients has been recently documented, which has stimulated researchers to develop antifibrotic drugs. Emerging antifibrotic therapies are aimed at inhibiting the accumulation of fibrogenic cells and/or preventing the deposition of extracellular matrix proteins. Although many therapeutic interventions are effective in experimental models of liver fibrosis, their efficacy and safety in humans is unknown. This review summarizes recent progress in the study of the pathogenesis and diagnosis of liver fibrosis and discusses current antifibrotic strategies.
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            Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase.

            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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              Adipose triglyceride lipase-mediated lipolysis of cellular fat stores is activated by CGI-58 and defective in Chanarin-Dorfman Syndrome.

              Adipose triglyceride lipase (ATGL) was recently identified as an important triacylglycerol (TG) hydrolase promoting the catabolism of stored fat in adipose and nonadipose tissues. We now demonstrate that efficient ATGL enzyme activity requires activation by CGI-58. Mutations in the human CGI-58 gene are associated with Chanarin-Dorfman Syndrome (CDS), a rare genetic disease where TG accumulates excessively in multiple tissues. CGI-58 interacts with ATGL, stimulating its TG hydrolase activity up to 20-fold. Alleles of CGI-58 carrying point mutations associated with CDS fail to activate ATGL. Moreover, CGI-58/ATGL coexpression attenuates lipid accumulation in COS-7 cells. Antisense RNA-mediated reduction of CGI-58 expression in 3T3-L1 adipocytes inhibits TG mobilization. Finally, expression of functional CGI-58 in CDS fibroblasts restores lipolysis and reverses the abnormal TG accumulation typical for CDS. These data establish an important biochemical function for CGI-58 in the lipolytic degradation of fat, implicating this lipolysis activator in the pathogenesis of CDS.
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                Author and article information

                Journal
                Biochim Biophys Acta
                Biochim. Biophys. Acta
                Biochimica et Biophysica Acta
                Elsevier Pub. Co
                0006-3002
                January 2012
                January 2012
                : 1821
                : 1
                : 113-123
                Affiliations
                Institute of Molecular Biosciences, University of Graz, Heinrichstrasse 31A, 8010 Graz, Austria
                Author notes
                [* ]Corresponding author. Tel.: + 43 316 380 1926; fax: + 43 316 380 9016. achim.lass@ 123456uni-graz.at
                Article
                BBAMCB57085
                10.1016/j.bbalip.2011.05.001
                3242165
                21586336
                7e1bd5d7-283c-43ee-ac76-663e3df26fc6
                © 2012 Elsevier B.V.

                This document may be redistributed and reused, subject to certain conditions.

                History
                : 17 February 2011
                : 28 April 2011
                : 2 May 2011
                Categories
                Review

                Biochemistry
                es3, esterase 3,rxrα/β/γ, retinoid x receptor alpha/beta/gamma,ld, lipid droplet,retinyl ester hydrolase,bpl-b, brush-border phospholipase b,ra, retinoic acid,rbp4, retinol-binding protein 4,atgl, adipose triglyceride lipase,tg, triacylglycerol,13cimh, 13-cis isomerohydrolase,neutral lipid,lrat, lecithin:retinol acyltransferase,sts, steroid sulfatase,arat, acyl-coa:retinol acyltransferase,plrp2, pancreatic lipase-related protein 2,gs2, gene sequence 2,hsc, hepatic stellate cell,ptl, pancreatic triglyceride lipase,bbb, blood-brain-barrier,reh, retinyl ester hydrolase,nreh, neutral retinyl ester hydrolase,mg, monoacylglycerol,ce, cholesteryl ester,cel, carboxyl ester lipase,stra6, stimulated by retinoic acid gene 6,es4, esterase 4,pl, phospholipid,re, retinyl ester,vldl, very low-density lipoprotein,lipid droplet,cm, chylomicron,hl, hepatic lipase,store,ces, carboxylesterase,vitamin a,lpl, lipoprotein lipase,mobilization,lrp-1, low-density lipoprotein-receptor protein 1,rarα/β, retinoic acid receptor alpha/beta,areh, acid retinyl ester hydrolase,tip47, tail-interacting protein of 47 kda,cgi-58, comparative gene identification 58,crbp1, cellular retinol-binding protein 1,gpihbp1, glycosylphosphatidylinositol-anchored high-density-lipoprotein binding protein 1,mgl, monoglyceride lipase,es2, esterase 2,pnpla, patatin-like phospholipase domain containing,ko, knock-out,rpe, retinal pigment epithelium,er, endoplasmic reticulum,hsl, hormone-sensitive lipase,dgat1, acyl-coa:diacylglycerol acyltransferase 1,wt, wild-type,fa, fatty acid,es10, esterase 10,es22, esterase 22,hspg, heparan sulphate proteoglycan
                Biochemistry
                es3, esterase 3, rxrα/β/γ, retinoid x receptor alpha/beta/gamma, ld, lipid droplet, retinyl ester hydrolase, bpl-b, brush-border phospholipase b, ra, retinoic acid, rbp4, retinol-binding protein 4, atgl, adipose triglyceride lipase, tg, triacylglycerol, 13cimh, 13-cis isomerohydrolase, neutral lipid, lrat, lecithin:retinol acyltransferase, sts, steroid sulfatase, arat, acyl-coa:retinol acyltransferase, plrp2, pancreatic lipase-related protein 2, gs2, gene sequence 2, hsc, hepatic stellate cell, ptl, pancreatic triglyceride lipase, bbb, blood-brain-barrier, reh, retinyl ester hydrolase, nreh, neutral retinyl ester hydrolase, mg, monoacylglycerol, ce, cholesteryl ester, cel, carboxyl ester lipase, stra6, stimulated by retinoic acid gene 6, es4, esterase 4, pl, phospholipid, re, retinyl ester, vldl, very low-density lipoprotein, lipid droplet, cm, chylomicron, hl, hepatic lipase, store, ces, carboxylesterase, vitamin a, lpl, lipoprotein lipase, mobilization, lrp-1, low-density lipoprotein-receptor protein 1, rarα/β, retinoic acid receptor alpha/beta, areh, acid retinyl ester hydrolase, tip47, tail-interacting protein of 47 kda, cgi-58, comparative gene identification 58, crbp1, cellular retinol-binding protein 1, gpihbp1, glycosylphosphatidylinositol-anchored high-density-lipoprotein binding protein 1, mgl, monoglyceride lipase, es2, esterase 2, pnpla, patatin-like phospholipase domain containing, ko, knock-out, rpe, retinal pigment epithelium, er, endoplasmic reticulum, hsl, hormone-sensitive lipase, dgat1, acyl-coa:diacylglycerol acyltransferase 1, wt, wild-type, fa, fatty acid, es10, esterase 10, es22, esterase 22, hspg, heparan sulphate proteoglycan

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