Arylacetamide deacetylase attenuates fatty-acid-induced triacylglycerol accumulation in rat hepatoma cells

Mobilization of hepatic triacylglycerol stores provides substrates for mitochondrial β-oxidation and assembly of VLDLs; however, the identity of lipolytic enzymes involved in the regulation of this process remains largely unknown. Arylacetamide deacetylase (AADA) shares homology with hormone-sensitive lipase and therefore could potentially participate in hepatic lipid metabolism, including the regulation of hepatic triacylglycerol levels. We have established McArdle-RH7777 (rat hepatoma) cell lines stably expressing mouse AADA cDNA and performed metabolic labeling as well as lipid mass analyses. Expression of AADA cDNA in McArdle-RH7777 cells significantly reduced intracellular triacylglycerol levels and apolipoprotein B secretion and increased fatty acid oxidation. Mobilization of hepatic triacylglycerol stores provides substrates for mitochondrial β-oxidation and assembly of VLDLs; however, the identity of lipolytic enzymes involved in the regulation of this process remains largely unknown. Arylacetamide deacetylase (AADA) shares homology with hormone-sensitive lipase and therefore could potentially participate in hepatic lipid metabolism, including the regulation of hepatic triacylglycerol levels. We have established McArdle-RH7777 (rat hepatoma) cell lines stably expressing mouse AADA cDNA and performed metabolic labeling as well as lipid mass analyses. Expression of AADA cDNA in McArdle-RH7777 cells significantly reduced intracellular triacylglycerol levels and apolipoprotein B secretion and increased fatty acid oxidation. Hydrolysis of hepatic intracellular triacylglycerol (TG) stores generates substrates for β-oxidation and lipid resynthesis, some of which are utilized for the assembly of VLDLs (1Wiggins D. Gibbons G.F. The lipolysis/esterification cycle of hepatic triacylglycerol. Its role in the secretion of very-low-density lipoprotein and its response to hormones and sulphonylureas.Biochem. J. 1992; 284: 457-462Google Scholar, 2Yang L.Y. Kuksis A. Myher J.J. Steiner G. Origin of triacylglycerol moiety of plasma very low density lipoproteins in the rat: structural studies.J. Lipid Res. 1995; 36: 125-136Google Scholar, 3Lankester D.L. Brown A.M. Zammit V.A. Use of cytosolic triacylglycerol hydrolysis products and of exogenous fatty acid for the synthesis of triacylglycerol secreted by cultured rat hepatocytes.J. Lipid Res. 1998; 39: 1889-1895Google Scholar). The assembly of VLDL involves both cotranslational and posttranslational addition of lipids to apolipoprotein B (apoB) (4Boren J. Rustaeus S. Olofsson S.O. Studies on the assembly of apolipoprotein B-100- and B-48-containing very low density lipoproteins in McA-RH7777 cells.J. Biol. Chem. 1994; 269: 25879-25888Google Scholar, 5Rustaeus S. Stillemark P. Lindberg K. Gordon D. Olofsson S.O. The microsomal triglyceride transfer protein catalyzes the post-translational assembly of apolipoprotein B-100 very low density lipoprotein in McA-RH7777 cells.J. Biol. Chem. 1998; 273: 5196-5203Google Scholar, 6Olofsson S.O. Stillemark-Billton P. Asp L. Intracellular assembly of VLDL: two major steps in separate cell compartments.Trends Cardiovasc. Med. 2000; 10: 338-345Google Scholar, 7Fisher E.A. Ginsberg H.N. Complexity in the secretory pathway: the assembly and secretion of apolipoprotein B-containing lipoproteins.J. Biol. Chem. 2002; 277: 17377-17380Google Scholar). The transfer of lipids to nascent apoB particles is facilitated by the microsomal triglyceride transfer protein (8Yao Z. McLeod R.S. Synthesis and secretion of hepatic apolipoprotein B-containing lipoproteins.Biochim. Biophys. Acta. 1994; 1212: 152-166Google Scholar, 9Mitchell D.M. Zhou M. Pariyarath R. Wang H. Aitchison J.D. Ginsberg H.N. Fisher E.A. Apoprotein B100 has a prolonged interaction with the translocon during which its lipidation and translocation change from dependence on the microsomal triglyceride transfer protein to independence.Proc. Natl. Acad. Sci. USA. 1998; 95: 14733-14738Google Scholar). Microsomal triglyceride transfer protein is also responsible for the formation of apoB-free endoplasmic reticulum (ER) lumenal lipid droplets (10Raabe M. Veniant M.M. Sullivan M.A. Zlot C.H. Bjorkegren J. Nielsen L.B. Wong J.S. Hamilton R.L. Young S.G. Analysis of the role of microsomal triglyceride transfer protein in the liver of tissue-specific knockout mice.J. Clin. Invest. 1999; 103: 1287-1298Google Scholar, 11Kulinski A. Rustaeus S. Vance J.E. Microsomal triacylglycerol transfer protein is required for lumenal accretion of triacylglycerol not associated with ApoB, as well as for ApoB lipidation.J. Biol. Chem. 2002; 277: 31516-31525Google Scholar, 12Wang Y. Tran K. Yao Z. The activity of microsomal triglyceride transfer protein is essential for accumulation of triglyceride within microsomes in McA-RH7777 cells. A unified model for the assembly of very low density lipoproteins.J. Biol. Chem. 1999; 274: 27793-27800Google Scholar). These lipid droplets are believed to serve as lipid donors for bulk lipidation of primordial apoB-containing particles (10Raabe M. Veniant M.M. Sullivan M.A. Zlot C.H. Bjorkegren J. Nielsen L.B. Wong J.S. Hamilton R.L. Young S.G. Analysis of the role of microsomal triglyceride transfer protein in the liver of tissue-specific knockout mice.J. Clin. Invest. 1999; 103: 1287-1298Google Scholar, 12Wang Y. Tran K. Yao Z. The activity of microsomal triglyceride transfer protein is essential for accumulation of triglyceride within microsomes in McA-RH7777 cells. A unified model for the assembly of very low density lipoproteins.J. Biol. Chem. 1999; 274: 27793-27800Google Scholar, 13Wang H. Gilham D. Lehner R. Proteomic and lipid characterization of apolipoprotein B-free luminal lipid droplets from mouse liver microsomes: implications for very low density lipoprotein assembly.J. Biol. Chem. 2007; 282: 33218-33226Google Scholar). One enzyme that has been implicated to play a role in the hydrolysis of stored TG pools and assembly of VLDL is an ER-associated triacylglycerol hydrolase (TGH) (14Lehner R. Vance D.E. Cloning and expression of a cDNA encoding a hepatic microsomal lipase that mobilizes stored triacylglycerol.Biochem. J. 1999; 343: 1-10Google Scholar, 15Gilham D. Ho S. Rasouli M. Martres P. Vance D.E. Lehner R. Inhibitors of hepatic microsomal triacylglycerol hydrolase decrease very low density lipoprotein secretion.FASEB J. 2003; 17: 1685-1687Google Scholar, 16Gilham D. Alam M. Gao W. Vance D.E. Lehner R. Triacylglycerol hydrolase is localized to the endoplasmic reticulum by an unusual retrieval sequence where it participates in VLDL assembly without utilizing VLDL lipids as substrates.Mol. Biol. Cell. 2005; 16: 984-996Google Scholar, 17Dolinsky V.W. Douglas D.N. Lehner R. Vance D.E. Regulation of the enzymes of hepatic microsomal triacylglycerol lipolysis and re-esterification by the glucocorticoid dexamethasone.Biochem. J. 2004; 378: 967-974Google Scholar, 18Gilham D. Lehner R. The physiological role of triacylglycerol hydrolase in lipid metabolism.Rev. Endocr. Metab. Disord. 2004; 5: 303-309Google Scholar, 19Dolinsky V.W. Gilham D. Alam M. Vance D.E. Lehner R. Triacylglycerol hydrolase: role in intracellular lipid metabolism.Cell. Mol. Life Sci. 2004; 61: 1633-1651Google Scholar, 20Wei E. Alam M. Sun F. Agellon L.B. Vance D.E. Lehner R. Apolipoprotein B and triacylglycerol secretion in human triacylglycerol hydrolase transgenic mice.J. Lipid Res. 2007; 48: 2597-2606Google Scholar). Inhibition of TGH leads to decreased TG mobilization and apoB secretion from hepatocytes (15Gilham D. Ho S. Rasouli M. Martres P. Vance D.E. Lehner R. Inhibitors of hepatic microsomal triacylglycerol hydrolase decrease very low density lipoprotein secretion.FASEB J. 2003; 17: 1685-1687Google Scholar). However, treatment of hepatocytes with a TGH-specific inhibitor reduced secretion of TG and apoB to a lesser extent than the general lipase inhibitor, diethyl p-nitrophenyl phosphate (E600), suggesting that other lipases may also contribute to VLDL assembly (15Gilham D. Ho S. Rasouli M. Martres P. Vance D.E. Lehner R. Inhibitors of hepatic microsomal triacylglycerol hydrolase decrease very low density lipoprotein secretion.FASEB J. 2003; 17: 1685-1687Google Scholar). The fact that perinatal rat hepatocytes are capable of TG secretion in the absence of TGH expression in this particular developmental stage provides further support for the existence of additional lipases (21Coleman R.A. Haynes E.B. Sand T.M. Davis R.A. Developmental coordinate expression of triacylglycerol and small molecular weight apoB synthesis and secretion by rat hepatocytes.J. Lipid Res. 1988; 29: 33-42Google Scholar, 22Lehner R. Cui Z. Vance D.E. Subcellullar localization, developmental expression and characterization of a liver triacylglycerol hydrolase.Biochem. J. 1999; 338: 761-768Google Scholar). In addition to VLDL assembly, fatty acids released from intracellular stores can be utilized for energy production via β-oxidation in the mitochondria. Unlike the well-described roles of adipose triglyceride lipase (ATGL) and hormone-sensitive lipase (HSL) in the mobilization of TG stores in adipose tissue (23Zimmermann R. Strauss J.G. Haemmerle G. Schoiswohl G. Birner-Gruenberger R. Riederer M. Lass A. Neuberger G. Eisenhaber F. Hermetter A. et al.Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase.Science. 2004; 306: 1383-1386Google Scholar, 24Haemmerle G. Lass A. Zimmermann R. Gorkiewicz G. Meyer C. Rozman J. Heldmaier G. Maier R. Theussl C. Eder S. et al.Defective lipolysis and altered energy in adipose triglyceride lipase.Science. Scholar, C. H. hormone-sensitive lipase and 2000; Scholar, lipase Metab. the identity of hepatic lipases β-oxidation is Arylacetamide deacetylase (AADA) shares sequence homology with M. D. P. Meyer R. liver of a involved in the metabolic of with sequence to hormone-sensitive Biol. Chem. 1994; 269: and a M. D. P. Meyer R. liver of a involved in the metabolic of with sequence to hormone-sensitive Biol. Chem. 1994; 269: Scholar, Gibbons G.F. of the for a microsomal and for Biol. Chem. Scholar). et Gibbons G.F. of the for a microsomal and for Biol. Chem. have that hepatic AADA levels a with an to hepatic VLDL secretion in In this AADA lipid in McArdle-RH7777 p-nitrophenyl acid and from from acid from from the mouse and from the from and from to the cDNA sequence of mouse The sequence of the of the cDNA The to the These to the AADA cDNA from a mouse liver cDNA performed for for and for for The the of and the cDNA as a to a cDNA encoding the mouse AADA protein with a the The for sequence of the of AADA and the The for to the the sequence the and the with the and The cDNA from this and and and expression from cultured in and in cells with of cells in with for to for and for protein by cell and in from to of and by and for to cell The to for to cell in D. C. D.L. and of enzymes in 2003; Scholar). in to a cell in and to and with for The in and by transfer to by with and hydrolase in from and cell lines by the hydrolysis of and D. Lehner R. to lipase and activity in 2005; 36: Scholar). from cells expressing human TGH as a for both and lipase D. Alam M. Gao W. Vance D.E. Lehner R. Triacylglycerol hydrolase is localized to the endoplasmic reticulum by an unusual retrieval sequence where it participates in VLDL assembly without utilizing VLDL lipids as substrates.Mol. Biol. Cell. 2005; 16: 984-996Google Scholar, D. D.N. Vance D.E. Lehner R. and fatty acid treatment of hepatocytes not in in activity of triacylglycerol Biophys. Acta. 2005; Scholar). with to the of cells with for with to and as to lipid with and in and by and microsomal from by lipids in and for to and and as and cell lines to in for with of to (14Lehner R. Vance D.E. Cloning and expression of a cDNA encoding a hepatic microsomal lipase that mobilizes stored triacylglycerol.Biochem. J. 1999; 343: 1-10Google in the absence of cells with in of the and by from cell and and by D. V.A. Ho S. G. Agellon L.B. R. Lehner R. lipid to apolipoprotein formation and VLDL secretion from hepatocytes.J. Lipid Res. 2004; Scholar). and cell lines to in for with of to and as to lipid from cell to lipase some cells and for analyses. the of the cells with fatty acid and with of for additional which the from cell also in the of to lipase cells and for as The for to cell cells with in the and by and lipids by the of and J. M. A for the and of from Biol. Chem. in the of lipid The lipids on and with a as (14Lehner R. Vance D.E. Cloning and expression of a cDNA encoding a hepatic microsomal lipase that mobilizes stored triacylglycerol.Biochem. J. 1999; 343: 1-10Google Scholar, 15Gilham D. Ho S. Rasouli M. Martres P. Vance D.E. Lehner R. Inhibitors of hepatic microsomal triacylglycerol hydrolase decrease very low density lipoprotein secretion.FASEB J. 2003; 17: 1685-1687Google by to of and and by from the metabolic labeling for of released from the cells during of and of acid to of from cell for an of the for These from by et and fatty acid in McA-RH7777 cells rat to Biophys. Acta. 2004; Scholar). the of and for to cell ApoB from to of cell in of and of protein A to and the for by and with in by and to with in and with of by with of by to mouse AADA by of with the acids of mouse AADA to with an of of the in by of of the and and stored by to and with in for to in in from cell lines mouse liver by and to The with and of mouse by of of of by of to cell from the cell by in of of and of to of cell and for and on for of with of and the other with of for and in and by AADA by with cell from the cell by in One of to of cell by of to of and of to the other for for in and by AADA by with by the and Use the of and in with of the on from for a and to a cycle in the from by of the hepatocytes from on in with and with in for with in for and to with and mouse in in for with and in in for with the on with and stored by a and by the of in cells performed from in and inhibitor The to for to A performed by in from to of and in and K. G. Cui Z. J. L. Yao Z. Intracellular assembly of very low density lipoproteins apolipoprotein B100 in rat McA-RH7777 cells.J. Biol. Chem. 2002; 277: Scholar). The this with and for and for in a in to a the the on of the and to for from the and from to by the addition of of to the of the and for The for to the The and the in of for and by to and for an and a and two cell by the are as as with of and AADA with a protein in mouse hepatocytes as by and The by density of mouse liver where AADA with protein and from AADA cDNA encoding the to the a and stably which not AADA of cell from cells with and with the acid of mouse AADA an of molecular mass that not in from the The levels of AADA protein in the two cell lines for further lines and significantly than that in mouse liver expression of AADA in cells could not be for The levels of AADA in cells with liver not to increased of the AADA to of expression as by not AADA in cells to the as by with AADA of cell from cells with increased AADA in that the AADA is a with a AADA cDNA utilized and to in microsomes from cells with AADA and microsomal increased both of substrates The in activity of AADA substrates to that in microsomes from cells expressing levels of TGH protein on of of lipids for cytosolic as are not substrates for AADA the to to the microsomes also not in hydrolysis of lipids with microsomes from cells. We therefore to lipolytic AADA activity of the of AADA not hydrolysis of TG not however, to increased the of the AADA microsomes with in microsomes not altered during this from AADA cells that with also with cells. The of the in AADA by with the hydrolase that to in and A protein to AADA in cell not in cell that the AADA is a and that the in in and substrates are to the activity of AADA than to its role in cells stably with human TGH cDNA utilized as a for the TGH is a and has been in D. C. D.L. and of enzymes in 2003; Scholar). of cells with to accumulation of TG However, cells significantly TG than the cells in intracellular TG the with the lipase inhibitor that the decrease in TG levels in cells to lipolytic activity of the enzyme than on fatty acid TG acid the and AADA cells not to be during and of the cells with not The of the of AADA on lipolysis than synthesis further by levels of and synthesis the cell lines in TG levels cell addition of in the in increased of TG accumulation in cell lines by cells and by suggesting that TG mobilization in the cells has been and TG synthesis is in and cells. the of cells in the absence of exogenous the TG in the absence of the lipase of the TG in the and this in the and cells that AADA not participate in the of TG on of in the has also of The in TG labeling also by the decrease in TG mass in cells treatment with for with cells. In with the from metabolic labeling both AADA cell lines to significantly intracellular TG addition of to the in intracellular TG levels AADA and cell a in intracellular TG accumulation and cells intracellular levels increased in cell lines in the of exogenous and not cell lines levels These further support the role of AADA in the regulation of TG levels. The decrease in intracellular TG levels in cells could have been to increased secretion of this lipid as of apoB-containing to AADA expressing cells secreted TG in apoB-containing of of apoB that expression of AADA to decreased secretion In of lipids from metabolic labeling that TG secretion also in cells of TG secreted during the from with decrease and decrease from and that AADA cells not secreted a decreased of also a of secretion of the other during the which the secretion of cell lines secreted of TG that the of the not that AADA not the of secretion of stored TG from cells. These that the increased hydrolysis of lipids in AADA cell lines not to increased of substrates for VLDL In to the released fatty acids from TG utilized for fatty acid the of released the the of the of fatty acid in cells. The of in expression of which an in fatty acid to AADA expression the in the absence of exogenous fatty the levels of fatty acids released from stores for decreased by a the cell suggesting that AADA has role a very role in the mobilization of TG stores for this of during the the in β-oxidation in AADA and the levels in both and AADA cells. it that in the of exogenous fatty AADA activity additional of the fatty acids for which from hydrolysis of TG and this mobilization could be by lipase the of exogenous fatty acids for β-oxidation in the of is the in and AADA this provides additional that fatty acid by both and AADA cells is as in the cell labeling and lipid mass of fatty acids to the liver from adipose tissue during is a and the liver this energy to acids that the liver are TG which substrates for the assembly of VLDL are utilized for in the of substrates that are by other during that are from β-oxidation the with an energy and hepatic VLDL secretion provides fatty acids for energy production in the The of TG secreted with VLDL is from hepatic TG stores a process that involves lipolysis and (1Wiggins D. Gibbons G.F. The lipolysis/esterification cycle of hepatic triacylglycerol. Its role in the secretion of very-low-density lipoprotein and its response to hormones and sulphonylureas.Biochem. J. 1992; 284: 457-462Google Scholar, 2Yang L.Y. Kuksis A. Myher J.J. Steiner G. Origin of triacylglycerol moiety of plasma very low density lipoproteins in the rat: structural studies.J. Lipid Res. 1995; 36: 125-136Google Scholar, 3Lankester D.L. Brown A.M. Zammit V.A. Use of cytosolic triacylglycerol hydrolysis products and of exogenous fatty acid for the synthesis of triacylglycerol secreted by cultured rat hepatocytes.J. Lipid Res. 1998; 39: 1889-1895Google Scholar). the mobilization of TG for VLDL secretion may an is of the molecular the lipases responsible for this A adipose tissue lipase is not in the liver S. C. of hormone-sensitive lipase in Expression of an protein and of Lipid Res. Scholar). expression of this enzyme in hepatocytes in increased mobilization of TG and the released fatty acids to for β-oxidation than for and VLDL assembly D. J. Gibbons G.F. of a human cell stably with hormone-sensitive J. 1999; Scholar, Schoiswohl G. R. of hormone-sensitive lipase and adipose triglyceride lipase fatty acid of fatty and Biol. Chem. Scholar). has tissue expression than (23Zimmermann R. Strauss J.G. Haemmerle G. Schoiswohl G. Birner-Gruenberger R. Riederer M. Lass A. Neuberger G. Eisenhaber F. Hermetter A. et al.Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase.Science. 2004; 306: 1383-1386Google however, its hepatic expression is also very and the role of this enzyme in hepatic lipid remains G. Lass A. Zimmermann R. Gorkiewicz G. Meyer C. Rozman J. Heldmaier G. Maier R. Theussl C. Eder S. et al.Defective lipolysis and altered energy in adipose triglyceride lipase.Science. Scholar). is by a lipid protein A. Zimmermann R. Haemmerle G. Riederer M. Schoiswohl G. M. P. Strauss J.G. Gorkiewicz G. R. triglyceride lipolysis of stores is by and in Metab. and that of in cells increased VLDL secretion J.D. A.M. D.L. the assembly and secretion of apolipoprotein B lipoproteins by rat Biophys. Acta. Scholar, S. A. G. L. mobilization of triglyceride for lipoprotein secretion in cells.J. Lipid Res. 2007; 48: Scholar). is the is to the regulation of that may be in cells on and in hepatic cells D. J. Gibbons G.F. of a human cell stably with hormone-sensitive J. 1999; Scholar, Schoiswohl G. R. of hormone-sensitive lipase and adipose triglyceride lipase fatty acid of fatty and Biol. Chem. it is that the of the lipases may the of the released fatty hydrolysis of TG stores by as and may fatty acids to for D. J. Gibbons G.F. of a human cell stably with hormone-sensitive J. 1999; Scholar, Schoiswohl G. R. of hormone-sensitive lipase and adipose triglyceride lipase fatty acid of fatty and Biol. Chem. of fatty acids in the could in of the lipolytic products by to support VLDL two lipases have been AADA and a role of TGH in hepatic VLDL assembly has been (14Lehner R. Vance D.E. Cloning and expression of a cDNA encoding a hepatic microsomal lipase that mobilizes stored triacylglycerol.Biochem. J. 1999; 343: 1-10Google Scholar, 16Gilham D. Alam M. Gao W. Vance D.E. Lehner R. Triacylglycerol hydrolase is localized to the endoplasmic reticulum by an unusual retrieval sequence where it participates in VLDL assembly without utilizing VLDL lipids as substrates.Mol. Biol. Cell. 2005; 16: 984-996Google Scholar, 17Dolinsky V.W. Douglas D.N. Lehner R. Vance D.E. Regulation of the enzymes of hepatic microsomal triacylglycerol lipolysis and re-esterification by the glucocorticoid dexamethasone.Biochem. J. 2004; 378: 967-974Google Scholar, 20Wei E. Alam M. Sun F. Agellon L.B. Vance D.E. Lehner R. Apolipoprotein B and triacylglycerol secretion in human triacylglycerol hydrolase transgenic mice.J. Lipid Res. 2007; 48: 2597-2606Google very is the of AADA its in M. D. P. Meyer R. liver of a involved in the metabolic of with sequence to hormone-sensitive Biol. Chem. 1994; 269: Scholar). its sequence homology to including and its expression in responsible for lipid metabolism, AADA to have a role in hepatic lipid Gibbons G.F. of the for a microsomal and for Biol. Chem. Scholar). can a of including as well as G. P. P. lipase of rat adipose and some Biol. Chem. that AADA could also a of has that AADA activity and lipid and that cells expressing AADA cDNA have decreased not levels. of a lipase inhibitor the in intracellular TG levels AADA and cell which also that the in TG in cells is to The of of TG the and an that TG stored in lipid droplets is not to AADA shares with and activity not in activity of AADA TG AADA shares sequence identity identity in the with as which has been to hydrolase activity H. M. M. M. M. S. M. K. Y. S. et of a enzyme from Biol. Chem. Scholar). on a model where AADA within the However, the this that AADA other in the of is also a for and not in levels synthesis in cells. is a where of enzyme within the to decreased TG not has been in in the expression of and acid Wang S. S. R.A. have reduced weight and liver triacylglycerol and altered fatty acid Cell. Biol. 2002; Scholar, L. Davis R. Young S.G. K. and to Lipid Res. Scholar, K. P. The protein roles in lipid and Scholar). can be by the of additional encoding for synthesis via the K. P. The protein roles in lipid and Scholar, R.A. of triacylglycerol synthesis and Lipid Res. 2004; Scholar, L. H. Wang S. T.M. K. R.A. of a as the enzyme in mice.J. Lipid Res. Scholar, J. M. J. D.N. K. as with tissue expression Biol. Chem. 2007; 282: Scholar). is also that AADA is to support the not of this is to TG which fatty acids and are in be that than AADA could also as a and an in of pools of within a cell has been on the of of the fatty acid J. R.A. of rat fatty acid in rat hepatocytes.J. Biol. Chem. Scholar). of the have been to participate in the synthesis of a lipid lipid J. R.A. of rat fatty acid in rat hepatocytes.J. Biol. Chem. suggesting a formation of a and an is that could a lipolytic enzyme as an additional hydrolysis of pools associated with TG not be to the synthesis of other lipids and However, from cells not increased activity with not suggesting that is not a for the The decrease of TG levels in cells by secretion of TG and increased fatty acid oxidation. AADA not to participate in the cycle in support of VLDL assembly, AADA activity to the of TG cytosolic lipid and of lipase activity by has fatty acid in cells to levels in cells. is the that a hydrolase has been to the of fatty acids for In that expression of levels than in the intracellular TG and fatty acid oxidation. that AADA is an additional hydrolase TGH that within the the of AADA and TGH in TG In of a role for AADA in VLDL assembly Gibbons G.F. of the for a microsomal and for Biol. Chem. that AADA as a of VLDL assembly and TG is the liver an enzyme be to it is that the enzyme has a role in and of fatty acids on AADA further as a for and hepatic The Gao for lipid by for and the of the Lehner for during the and for of this deacetylase apolipoprotein B adipose triglyceride lipase diethyl p-nitrophenyl phosphate endoplasmic reticulum hormone-sensitive lipase McArdle-RH7777 acid p-nitrophenyl triacylglycerol triacylglycerol hydrolase

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