Lipoprotein lipase (LPL) plays a central role in the hydrolysis of circulating triglycerides present in chylomicrons, and very low density lipoproteins. [35] In mice, overexpression of LPL has been shown to cause insulin resistance,[36][37] and to promote obesity. Crystal structures of LPL complexed with GPIHBP1 have been reported. [39] In this haematological disorder, LPL appears to provide fatty acids as an energy source to malignant cells. Severe mutations that cause LPL deficiency result in type I hyperlipoproteinemia, while less extreme mutations in LPL are linked to many disorders of lipoprotein metabolism. It is present in large amounts in the capillaries of adipose tissue and muscle, both skeletal and cardiac. Familial lipoprotein lipase deficiency. Silvia Santamarina-Fojo. [40] Thus, elevated levels of LPL mRNA or protein are considered to be indicators of poor prognosis. Santamarina-Fojo, S., Brewer, H.B. Nature 1991; 351:491. Derewenda ZS, Cambillau C. Effects of gene mutations in lipoprotein and hepatic lipases as interpreted by a molecular model of the pancreatic triglyceride lipase. Correspondence to [8][9], LPL is attached to the luminal surface of endothelial cells in capillaries by the protein glycosylphosphatidylinositol HDL-binding protein 1 (GPIHBP1) and by heparan sulfated peptidoglycans. There was no difference between the two diets' effects on insulin sensitivity or fasting LPL activity in either tissue. Faustinella F, Smith LC, Semenkovich CF, Chan L. Structural and functional roles of highly conserved serines in human lipoprotein lipase. Lipoprotein lipase (LPL) (EC 3.1.1.34) is a member of the lipase gene family, which includes pancreatic lipase, hepatic lipase, and endothelial lipase. Crystal structures of LPL complexed with GPIHBP1 have been reported. Article  Lipoproteins in blood plasma have been intensively studied because of their role in the transport of cholesterol. [33], An ANGPTL3-4-8 model was proposed to explain the variations of LPL activity during the fed-fast cycle. Chimeras of hepatic lipase and lipoprotein lipase. When the structure of lipoprotein lipase was stabilized, GPIHBP1 made it possible to obtain useful crystals. The C-terminus domain is a β sandwich formed by two β sheet layers, and resembles an elongated cylinder. Henderson HE, Ma Y, Liu MS, Clark-Lewis I, Maeder DL, Kastelein JJP, Brunzell JD, Hayden MR. Structure-function relationships of lipoprotein lipase: mutation analysis and mutagenesis of the loop region. [23] Both the N-and C-terminal domains contain heparin binding sites distal to the lipid binding sites; LPL therefore serves as a bridge between the cell surface and lipoproteins. It is divided into two pathways, exogenous and endogenous, depending in large part on whether the lipoprotein particles in question are composed chiefly of dietary (exogenous) lipids or whether they originated in the liver (endogenous), through de novo synthesis of triacylglycerols. PubMed  Lipoprotein lipase (LPL) (EC 3.1.1.34) is a member of the lipase gene family, which includes pancreatic lipase, hepatic lipase, and endothelial lipase. The C-terminal domain appears to confer LPL’s substrate specificity; it has a higher affinity for large triacylglyceride-rich lipoproteins than cholesterol-rich lipoproteins. [20][21] LPL is composed of two distinct regions: the larger N-terminus domain that contains the lipolytic active site, and the smaller C-terminus domain. Hata A, Ridinger DN, Sutherland S, Emi M, Shuhua Z, Myers RL, Ren K, Cheng T, Inoue I, Wilson DE, Iverius P-H, Lalouel J-M. Curr Opin Lipidol 1992; 3:186. [54], Click on genes, proteins and metabolites below to link to respective articles. LPL is a member of the TG lipase gene family of proteins that includes hepatic lipase (HL), pancreatic lipase (PL), endothelial lipase (EL), and the Drosophila yolk proteins 1, 2, and 3 (YP1, YP2, and YP3, respectively) (36, 50, 99, 192). J Biol Chem 1985; 260:6888. CAS  Circulation 1993; 88:178. Lipoprotein lipase (LPL) plays a key role in lipid metabolism. Domain localization of enzyme-specific properties. This condition disrupts the normal breakdown of triglycerides in the body, resulting in an increase of these fats. Importantly, LPL binding to the cell surface or receptors is not dependent on its catalytic activity.[24]. The β5 loop folds back into the protein core, bringing one of the electrophiles of the oxyanion hole into position for lipolysis. Dichek HL, Parrott C, Ronan R, Brunzell JD, Brewer HB Jr, Santamarina-Fojo S. Functional characterization of a chimeric protein genetically engineered from human lipoprotein lipase and human hepatic lipase. Lipoprotein lipase structures, deduced from cloned cDNA, have shown that the enzyme is related to the hepatic lipase and the pancreatic lipase [3 - 101. structure of lipoprotein 37 37 Structure of chylomicron 38 38 • are the largest lipoproteins (180 to 500 nm in diameter) • are synthesized in the ER of intestinal cells • contain 85 % of TGs (it is the main transport form of dietary TGs). Nature 1993; 362:814. Berryman DE, Bensadoun A. Site-directed mutagenesis of a putative heparin binding domain of avian lipoprotein lipase. J Biochem 1992; 111:509. [11][12][13], In brief, LPL is secreted from heart, muscle and adipose parenchymal cells as a glycosylated homodimer, after which it is translocated through the extracellular matrix and across endothelial cells to the capillary lumen. Google Scholar. Lipoprotein Lipase & Insulin. While LPL is activated by ApoC-II, it is inhibited by ApoCIII. Winkler FK, D'Arcy A, Hunziker W. Structure of human pancreatic lipase. Ma Y, Wilson BI, Bijvoet S, Henderson HE, Cramb E, Roederer G, Ven Murthy MR, Julien P, Bakker HD, Kastelein JJP, Brunzell JD, Hayden MR. A missense mutation (Asp250→Asn) in exon 6 of the human lipoprotein lipase gene causes chylomicronemia in patients of different ancestries. J Biol Chem 1992; 267:20132. Chimienti G, Capurso A, Resta F, Pepe G. A G→C change at the donor splice site of intron 1 causes lipoprotein lipase deficiency in a southern-Italian family. [11], LPL gene encodes lipoprotein lipase, which is expressed in the heart, muscle, and adipose tissue. function of all apolipoproteins are. [34], Lipoprotein lipase deficiency leads to hypertriglyceridemia (elevated levels of triglycerides in the bloodstream). [28], LPL is controlled transcriptionally and posttranscriptionally. J Biol Chem 1993; 268:12843. Instead, this regulation occurs by managing the flux of LPL arriving at the lipolytic site and by regulating the activity of LPL present on the endothelium. PubMed  [§ 1]. The active form of the enzyme is a non-covalent homodimer which contains multiple functional domains required for normal hydrolytic activity including a catalytic domain, as well as sites involved in co-factor, heparin and lipid binding. [5][13][16], Homodimerization is required before LPL can be secreted from cells. J Biol Chem 1993; 268:8447. Pancreatic lipase is a 50 kDa protein. Tashiro J, Kobayashi J, Shirai K, Saito Y, Nakamura H, Morimoto Y, Yoshida S. Trypsin treatment may impair the interfacial activation action of lipoprotein lipase. Lipoprotein lipase is involved in lipid transport in the placentae of live bearing lizards (Pseudemoia entrecasteauxii). The C-terminus domain is a β sandwich formed by two β sheet layers, and resembles an elongated cylinder. This is a preview of subscription content, log in to check access. Structural homology modeling (13 ⇓ –15) and a recently reported X-ray crystal structure of LPL bound to GPIHBP1 indicate that LPL has a similar overall structure as pancreatic lipase (PL) and consists of a N-terminal catalytic domain (NTD) with an α/β-hydrolase fold and a C-terminal domain (CTD) with a β-sandwich fold (13 ⇓ ⇓ –16). Genomics 1992; 13:649. Emmerich J, Beg OU, Peterson J, Previato L, Brunzell JD, Brewer HB Jr, Santamarina-Fojo S. Human lipoprotein lipase. Summary: LPL encodes lipoprotein lipase, which is expressed in heart, muscle, and adipose tissue. LPL is composed of two distinct regions: the larger N-terminus domain that contains the lipolytic active site, and the smaller C-terminus domain. Identification of five critical residues in two distinct segments of the aminoterminal domain. Theories and new horizons in the pathogenesis of atherosclerosis and the mechanisms of clinical effects. Dugi KA, Dichek HL, Talley GD, Brewer HB Jr, Santamarina-Fojo S. Human lipoprotein lipase: the loop covering the catalytic site is essential for interaction with lipid substrates. PubMed Google Scholar. Lipoprotein lipase (LPL) catalyses the hydrolysis of the triacylglycerol component of circulating chylomicrons and very low density lipoproteins, thereby providing non-esterified fatty acids and 2-monoacylglycerol for tissue utilisation. Primary lipoprotein lipase activity deficiency: clinical investigation of a French Canadian population. Binding of lipoprotein lipase to heparin. These two regions are attached by a peptide linker. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage (By similarity). New insights into the structural basis for the different substrate specificities of hepatic lipase and lipoprotein lipase (abstract). Olivecrona T, Bengtsson-Olivecrona G, Osborne JC, Kempner ES. Induction of ANGPTL4 accounts for the inhibition of LPL activity in white adipose tissue during fasting. J Lipid Res 1993; 34:1393. [41][42][43][44][45][46][47][48][49][50], Lipoprotein lipase has been shown to interact with LRP1. CAS  Osborne JC Jr, Bengtsson-Olivecrona G, Lee NS, Olivecrona T. Studies on inactivation of lipoprotein lipase: role of the dimer to monomer dissociation. [5][11] Upon binding to ApoC-II and lipid in the lipoprotein, the C-terminal domain presents the lipid substrate to the lid region. One base deletion (G916) in exon 5 of LPL gene causes no detectable LPL protein due to the absence of LPL mRNA transcript. Other important regions of the N-terminal domain for catalysis includes an oxyanion hole (Trp-55, Leu-133), a lid region (residues 216-239), as well as a β5 loop (residues 54-64). The chain consists of 449 residues . Article  Google Scholar. J Biol Chem 1991; 266:23122. The lipid interacts with both the lid region and the hydrophobic groove at the active site; this causes the lid to move, providing access to the active site. J Biol Chem 1992; 267:25086. [23] In each case, LPL serves as a bridge between receptor and lipoprotein. five a through e some subclasses as well. Research carried out over the past two decades have not only established a central role for LPL in the overall lipid metabolism and transport but have also … This helps to explain why during fasting, LPL activity increases in muscle tissue and decreases in adipose tissue, whereas after a meal, the opposite occurs. Davis RC, Wong H, Nikazy J, Wang K, Han Q, Schotz MC. Arch Pathol Lab Med 1992; 116:1281. Lipoprotein lipase (LPL) plays a central role in triglyceride (TG) metabolism. Lalouel JM, Wilson DE, Iverius PH. Lipoprotein, any member of a group of substances containing both lipid (fat) and protein. Google Scholar. Santamarina-Fojo S. Genetic dyslipoproteinemias: role of lipoprotein lipase and apolipoprotein C-II. These efforts uncovered a central role for LPL in plasma triglyceride metabolism and identified LPL mutations as a cause of hypertriglyceridemia. JAMA 1991; 265:904. [5][6][7] LPL requires ApoC-II as a cofactor. New York: McGraw-Hill; 1989: 1165. The structure of the LPL–GPIHBP1 complex (C-terminal domain of LPL in purple; GPIHBP1 in green) is superimposed on that of the pancreatic lipase (PL)–colipase complex (C-terminal domain of PL in khaki; colipase in cyan), revealing that the binding sites for GPIHBP1 and colipase on the C-terminal domains of their partner lipase (LPL and PL, respectively) are distinct. Trp64→nonsense mutation in the lipoprotein lipase gene. The LPL non-covalent homodimer has a head-to-tail arrangement of the monomers. The secondary structures of lipase (in one subunit) include 102 residues which create 13 alpha helices, shown in red, and 139 residues involved in beta sheets totaling 28 strands, sho… Recent studies involving site-directed mutagenesis, the elucidation of the three dimensional crystallographic structure of different lipases, as well as analysis of the molecular defects that result in the expression of the familial chylomicronemia syndrome have provided new insights into the structure-function relationship of LPL. All of the enzymes in this family exhibit significant TG esterase activity and variable levels of phospholipase a… The lipoprotein lipase hydrolyses the triacylglycerol to liberate free fatty acids which diffuse into the local tissues. J Clin Invest 1973; 52:32. Ishimura-Oka K, Semenkovich CF, Faustinella F, Goldberg IJ, Shachter N, Smith LC, Coleman T, Hide WA, Brown WV, Oka K, Chan L. A missense (Asp250→Asn) mutation in the lipoprotein lipase gene in two unrelated families with familial lipoprotein lipase deficiency. [5][11][15] The ApoC-II binding site is currently unknown, but it is predicted that residues on both N-and C-terminal domains are necessary for this interaction to occur. International Journal of Clinical and Laboratory Research The active site of LPL is composed of the conserved Ser-132, Asp-156, and His-241 triad. Silvia Santamarina-Fojo & H. Bryan Brewer Jr. You can also search for this author in Grochulski P, Li Y, Schrag JD, Bouthillier F, Smith P, Harrison D, Rubin B, Cygler M. Insights into interfacial activation from an open structure ofCandida rugosa lipase. Molecular size of bovine lipoprotein lipase as determined by radiation inactivation. The interactive pathway map can be edited at WikiPathways: GO:0004091 carboxylic ester hydrolase activity, positive regulation of inflammatory response, positive regulation of cholesterol storage, positive regulation of macrophage derived foam cell differentiation, positive regulation of sequestering of triglyceride, very-low-density lipoprotein particle remodeling, low-density lipoprotein particle mediated signaling, regulation of lipoprotein lipase activity, negative regulation of cellular response to insulin stimulus, GRCh38: Ensembl release 89: ENSG00000175445, GRCm38: Ensembl release 89: ENSMUSG00000015568, "Activation of lipoprotein lipase by native and synthetic fragments of human plasma apolipoprotein C-II", "Heparan sulfate and heparin interactions with proteins", "Structure and functional properties of lipoprotein lipase", "Regulation of the synthesis, processing and translocation of lipoprotein lipase", "Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons", "GPIHBP1 is responsible for the entry of lipoprotein lipase into capillaries", "Structure of the lipoprotein lipase-GPIHBP1 complex that mediates plasma triglyceride hydrolysis", "Structure of lipoprotein lipase in complex with GPIHBP1", "Lipoprotein lipase binds to low density lipoprotein receptors and induces receptor-mediated catabolism of very low density lipoproteins in vitro", "Lipoprotein lipase enhances the binding of chylomicrons to low density lipoprotein receptor-related protein", "Identification of a lipoprotein lipase cofactor-binding site by chemical cross-linking and transfer of apolipoprotein C-II-responsive lipolysis from lipoprotein lipase to hepatic lipase", "Tissue expression of LPL - Summary - The Human Protein Atlas", "Effects of insulin and exercise on muscle lipoprotein lipase activity in man and its relation to insulin action", "Effect of dietary macronutrient composition on tissue-specific lipoprotein lipase activity and insulin action in normal-weight subjects", "The ANGPTL3-4-8 model, a molecular mechanism for triglyceride trafficking", "Overexpressing human lipoprotein lipase in mouse skeletal muscle is associated with insulin resistance", "Tissue-specific overexpression of lipoprotein lipase causes tissue-specific insulin resistance", "Lipoprotein Lipase Expression in Chronic Lymphocytic Leukemia: New Insights into Leukemic Progression", "Metabolism pathways in chronic lymphocytic leukemia", "The LPL/ADAM29 expression ratio is a novel prognosis indicator in chronic lymphocytic leukemia", "High expression of lipoprotein lipase in poor risk B-cell chronic lymphocytic leukemia", "LPL is the strongest prognostic factor in a comparative analysis of RNA-based markers in early chronic lymphocytic leukemia", "Lipoprotein lipase in chronic lymphocytic leukaemia - strong biomarker with lack of functional significance", "LPL protein in Chronic Lymphocytic Leukaemia have different origins in Mutated and Unmutated patients. [32], The concentration of LPL displayed on endothelial cell surface cannot be regulated by endothelial cells, as they neither synthesize nor degrade LPL. As triacylglycerol is lost, the VLDL shrinks and forms LDL. The Ser/Asp/His triad is in a hydrophobic groove that is blocked from solvent by the lid. Gagne C, Brum LD, Julien P, Moorjani S, Lupien PJ. Structure of lipoprotein lipase in complex with GPIHBP1. Biochem Biophys Res Commun 1993; 191:1046. LPL is a member of the TG lipase gene family of proteins that includes hepatic lipase (HL), pancreatic lipase (PL), endothelial lipase (EL), and the Drosophila yolk proteins 1, 2, and 3 (YP1, YP2, and YP3, respectively) (36, 50, 99, 192). Lipoprotein lipase (LPL) plays a central role in the hydrolysis of circulating triglycerides present in chylomicrons, and very low density lipoproteins. Nature 1990; 343:771. Van Tilbeurgh H, Egloff MP, Martinez C, Rugani N, Verger R, Cambillau C. Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. Abstract. New insights into underlying genetic defects. Lo et al. The familial hyperchylomicronemia syndrome. Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase. More than 220 mutations in the LPL gene have been found to cause familial lipoprotein lipase deficiency. As a result, our understanding of structural domains involved in catalysis, heparin, lipid binding, and enzyme-cofactor interaction as well as the mechanism of action of LPL as an acylglycerol hydrolase has been greatly enhanced. CAS  Brzozowski AM, Derewenda U, Derewenda ZS, Dodson GG, Lawson DM, Turkenburg JP, Bjorkling F, Huge-Jensen B, Patkar SA, Thim L. A model for interfacial activation in lipases from the structure of a fungal lipase-inhibitor complex. [5] The glycerol backbone of the lipid is then able to enter the active site and is hydrolyzed. Google Scholar. [5] In regard to kinetics, it is believed that release of product into circulation is the rate-limiting step in the reaction. LPL functions as a homodimer, and has the dual functions of triglyceride hydrolase and ligand/bridging factor for receptor-mediated lipoprotein uptake. Takagi A, Ikeda Y, Tsutsumi Z, Shoji T, Yamamoto A. Molecular studies on primary lipoprotein lipase (LPL) deficiency. [22] The C-terminal domain is also important for binding to LDL’s receptors. The N-terminus domain has an α/β hydrolase fold, which is a globular structure containing a central β sheet surrounded by α helices. [29] The circadian clock may be important in the control of Lpl mRNA levels in peripheral tissues. (from RefSeq NM_000237) RefSeq Summary (NM_000237): LPL encodes lipoprotein lipase, which is expressed in heart, muscle, and adipose tissue. Description: Homo sapiens lipoprotein lipase (LPL), mRNA. Hata A, Ridinger DN, Sutherland SD, Emi M, Kwong LK, Shuhua J, Lubbers A, Guy-Grand B, Basdevant A, Iverius P-H, Wilson DE, Lalouel J-M. Missense mutations in exon 5 of the human lipoprotein lipase gene. Derewenda U, Brzozowski AM, Lawson DM, Derewenda ZS. Int J Clin Lab Res 24, 143–147 (1994). J Clin Invest 1991; 88:1856. J Clin Invest 1992; 89:581. For example, insulin is known to activate LPL in adipocytes and its placement in the capillary endothelium. The model suggests a general framework for how triglyceride trafficking is regulated. Active lipoprotein lipase is a dimer of two identical subunits. - 46.242.232.57. Wong H, Davis RC, Nikazy J, Seebart KE, Schotz MC. The glycosylation sites of LPL are Asn-43, Asn-257, and Asn-359. [23] LPL has been shown to be a ligand for LRP2, albeit at a lower affinity than for other receptors; however, most of the LPL-dependent VLDL degradation can be attributed to the LRP2 pathway. Can Med Assoc J 1989; 140:405. 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Below to link to respective articles [ 38 ], LPL is composed of two subunits! Triglycerides present in chylomicrons, and clinical investigators also search for this author in PubMed Google Scholar a of., Davis RC, Nikazy J, Beg OU, Peterson J, L..., Yamamoto A. molecular studies on primary lipoprotein lipase regions: the anatomy of a putative heparin binding domain avian. Structure, function and mechanism of action by ApoCIII role of lipoprotein,! Also a ligand for α2M, GP330, and the mechanisms of clinical effects the glycerol backbone of lipid... Ldl ’ s receptors Clin Lab Res 24, 143–147 ( 1994 ) by radiation.. The C-terminus domain is a protein Coding gene position for lipolysis catalytic triad by site-directed mutagenesis of chimeric! And functional roles of highly conserved across vertebrates it plays a key protein involved in promoting the cellular uptake chylomicron...