Razlika između verzija stranice "Lipoprotein lipaza"

'''Lipoprotein-lipaza''' ('''LPL''') ({{EC number|3.1.1.34}}) je [[enzim]] koji je kod [[ljudi]] [[kodon|kodiran]] [[gen]]om '''LPL'''. Čan je porodice [[lipaza|lipaznih]] gena, koja uključuje [[gušteračna lipaza|gušteračnu]], [[jetrena lipaza|jetrenu]] i [[endotelna lipaza|endotelnu lipazu]]. Topiv je u vodi a [[hidroliza|hidrolizita]] [[triglicerid]]e u [[lipoprotein]]e, poput onih koji se nalaze u [[hilomikron]]ima i [[lipoprotein vrlo niske gustoće| lipoproteinima vrlo niske gustoće (VLDL)]], u dvije slobodne [[masne kiseline]] i jednu [[monoacilglicerol]] molekulu. Također je uključen u podstcanje ćelijske apsorpcije [[hilomikron]]skih ostataka, lipoproteina bogatih [[olesterol]]om i slobodnih masnih kiselina.<ref name="Mead-2002"/><ref name="Rinninger-1998">{{cite journal |vauthors=Rinninger F, Kaiser T, Mann WA, Meyer N, Greten H, Beisiegel U | title = Lipoprotein lipase mediates an increase in the selective uptake of high density lipoprotein-associated cholesteryl esters by hepatic cells in culture | journal = J. Lipid Res. | volume = 39 | issue = 7 | pages = 1335–48 |date=Julyjuli 1998 | doi = 10.1016/S0022-2275(20)32514-1 | pmid = 9684736 | doi-access = free }}</ref><ref name="Ma-1994">{{cite journal |vauthors=Ma Y, Henderson HE, Liu MS, Zhang H, Forsythe IJ, Clarke-Lewis I, Hayden MR, Brunzell JD | title = Mutagenesis in four candidate heparin binding regions (residues 279-282, 291-304, 390-393, and 439-448) and identification of residues affecting heparin binding of human lipoprotein lipase | journal = J. Lipid Res. | volume = 35 | issue = 11 | pages = 2049–59 |date=Novembernovembar 1994 | doi = 10.1016/S0022-2275(20)39951-X | pmid = 7868983 | doi-access = free }}</ref> LPL zahtijeva [[ApoC-II]] kao kofaktor.<ref name="pmid16314153">{{cite journal |vauthors=Kim SY, Park SM, Lee ST | title = Apolipoprotein C-II is a novel substrate for matrix metalloproteinases | journal = Biochem. Biophys. Res. Commun. | volume = 339 | issue = 1 | pages = 47–54 |date=Januaryjanuar 2006 | pmid = 16314153 | doi = 10.1016/j.bbrc.2005.10.182 }}</ref><ref name="Kinnunen-1977">{{cite journal |vauthors=Kinnunen PK, Jackson RL, Smith LC, Gotto AM, Sparrow JT | title = Activation of lipoprotein lipase by native and synthetic fragments of human plasma apolipoprotein C-II | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 74 | issue = 11 | pages = 4848–51 |date=Novembernovembar 1977 | pmid = 270715 | pmc = 432053 | doi = 10.1073/pnas.74.11.4848 | bibcode = 1977PNAS...74.4848K | doi-access = free }}</ref>

LPL je pričvršćen na lumensku površinu [[endotel|endotelnih ćelija]] u [[kapilar]]ima, HDL-vezujućim glikozilfosfatidilinozitol proteinom 1 (GPIHBP1) i heparan-sulfatiranim peptidoglikanima.<ref>{{cite journal | vauthors = Meneghetti MC, Hughes AJ, Rudd TR, Nader HB, Powell AK, Yates EA, Lima MA | title = Heparan sulfate and heparin interactions with proteins | journal = Journal of the Royal Society, Interface | volume = 12 | issue = 110 | pages = 0589 | date = Septemberseptembar 2015 | pmid = 26289657 | pmc = 4614469 | doi = 10.1098/rsif.2015.0589 }}</ref> Najraširenije je u [[masno tkivo|masnom]], [[srčani mišić|srčanom]] i [[skeletni mišić|skeletnomišićnom]] tkivu, kao i u [[mliječna žlijezda|mliječnim žlijezdama]] u [[dojenje|laktaciji]].<ref name="Wang-1992">{{cite journal | vauthors = Wang CS, Hartsuck J, McConathy WJ | title = Structure and functional properties of lipoprotein lipase | journal = Biochimica et Biophysica Acta | volume = 1123 | issue = 1 | pages = 1–17 | date = Januaryjanuar 1992 | pmid = 1730040 | doi = 10.1016/0005-2728(92)90119-M | url = https://epub.ub.uni-muenchen.de/3772/1/82.pdf }}</ref><ref name="Wong-2002">{{cite journal | vauthors = Wong H, Schotz MC | title = The lipase gene family | journal = Journal of Lipid Research | volume = 43 | issue = 7 | pages = 993–9 | date = Julyjuli 2002 | pmid = 12091482 | doi = 10.1194/jlr.R200007-JLR200 | doi-access = free }}</ref><ref name="Braun-1992">{{cite journal | vauthors = Braun JE, Severson DL | title = Regulation of the synthesis, processing and translocation of lipoprotein lipase | journal = The Biochemical Journal | volume = 287 ( Pt 2) | issue = 2 | pages = 337–47 | date = Octoberoktobar 1992 | pmid = 1445192 | pmc = 1133170 | doi = 10.1042/bj2870337}}</ref>

Dužina [[polipeptid]]nog lanca je 455 [[aminokiselina]], а [[molekularna masa|molekulska težina]] 53.162 [[dalton (jedinica)|Da]].<ref name="UniProt">{{cite web|url=http://www.uniprot.org/uniprot/P06858#sequences |title=UniProt, P06858 |language=eng. |accessdateaccess-date=19. 9. 2021-09-19}}</ref>

:'''W''': [[Triptofan]]<br/>

Prijavljene su [[kristalne strukture]] LPL kompleksa sa GPIHBP1.<ref name="pmid30559189">{{PDB|6E7K}}; {{cite journal | vauthors = Birrane G, Beigneux AP, Dwyer B, Strack-Logue B, Kristensen KK, Francone OL, Fong LG, Mertens HD, Pan CQ, Ploug M, Young SG, Meiyappan M | display-authors = 6 | title = Structure of the lipoprotein lipase-GPIHBP1 complex that mediates plasma triglyceride hydrolysis | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 116 | issue = 5 | pages = 1723–1732 | date = Januaryjanuar 2019 | pmid = 30559189 | pmc = 6358717 | doi = 10.1073/pnas.1817984116 | doi-access = free }}</ref><ref name="pmid31072929">{{PDB|6OAU|6OAZ|6OB0}}; {{cite journal | vauthors = Arora R, Nimonkar AV, Baird D, Wang C, Chiu CH, Horton PA, Hanrahan S, Cubbon R, Weldon S, Tschantz WR, Mueller S, Brunner R, Lehr P, Meier P, Ottl J, Voznesensky A, Pandey P, Smith TM, Stojanovic A, Flyer A, Benson TE, Romanowski MJ, Trauger JW | display-authors = 6 | title = Structure of lipoprotein lipase in complex with GPIHBP1 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 116 | issue = 21 | pages = 10360–10365 | date = Maymaj 2019 | pmid = 31072929 | pmc = 6534989 | doi = 10.1073/pnas.1820171116 | doi-access = free }}</ref> LPL se sastoji od dvije različite regije: većeg [[N-terminal]]nog domena koji sadrži lipolizno [[aktivno mjesto]] i manji [[C-terminal]]ni domen. Ove dvije regije povezane su [[peptid]]nim linkerom. N-krajnji domen ima [[alfa/beta hidrolazno savijanje|α/β hidrolazno savijanje]], koje je globulasta struktura sa centralnim [[beta-list|β listom]] okruženim [[alfa-heliks|α heliksima]]. [[C-terminal]]ni domen je β sendvič, formiran od dva β sloja i podsjeća na izduženi cilindar.

Ukratko, LPL se luče [[parenhim|parenhimske ćelije]] [[srce|srca]], [[mišić]]a i [[masno tkivo|masnog tkiva]], kao [[glikozilacija|glikozilirani]] homodimer, nakon čega se translocira kroz [[vanćelijski matriks]] i, preko [[endotel]]nih ćelija, u lumen [[kapilar]]a . Nakon translacije, novosintetizirani protein se glikozilira u [[endoplazmatski retikulum|endoplazmatskom retikulumu]]. Mjesta [[glikozilacija]] LPL-a su Asn-43, Asn-257 i Asn-359.<ref name="Mead-2002">{{cite journal |vauthors=Mead JR, Irvine SA, Ramji DP | title = Lipoprotein lipase: structure, function, regulation, and role in disease | journal = J. Mol. Med. | volume = 80 | issue = 12 | pages = 753–69 |date=Decemberdecembar 2002 | pmid = 12483461 | doi = 10.1007/s00109-002-0384-9 | s2cid = 40089672 }}</ref> [[Glukozidaze]] zatim uklanjaju terminalne ostatke glukoze; nekad se vjerovalo da je ovo podrezivanje glukoze odgovorno za konformacijske promjene potrebne da LPL formira homodimere i postane katalitski aktivan.<ref name="Mead-2002" /><ref name="Braun-1992" /><ref name="Semb-1989">{{cite journal |vauthors=Semb H, Olivecrona T | title = The relation between glycosylation and activity of guinea pig lipoprotein lipase | journal = J. Biol. Chem. | volume = 264 | issue = 7 | pages = 4195–200 |date=Marchmart 1989 | doi = 10.1016/S0021-9258(19)84982-7 | pmid = 2521859 | doi-access = free }}</ref><ref name="Wong-1994">{{cite journal |vauthors=Wong H, Davis RC, Thuren T, Goers JW, Nikazy J, Waite M, Schotz MC | title = Lipoprotein lipase domain function | journal = J. Biol. Chem. | volume = 269 | issue = 14 | pages = 10319–23 |date=Aprilapril 1994 | doi = 10.1016/S0021-9258(17)34063-2 | pmid = 8144612 | doi-access = free }}</ref> U [[Golgijev aparat|Golgijevom aparatu]], [[oligosaharidi]] se dalje mijenjaju, kako bi rezultirali ili dva složena lanca, ili dva složena i jednim lancem sa visokom [[manoza|manozom]].<ref name="Mead-2002" /><ref name="Braun-1992" /> In the final protein, carbohydrates account for about 12% of the molecular mass (55-58 kDa).<ref name="Mead-2002" /><ref name="Braun-1992" /><ref name="Vannier-1989">{{cite journal |vauthors=Vannier C, Ailhaud G | title = Biosynthesis of lipoprotein lipase in cultured mouse adipocytes. II. Processing, subunit assembly, and intracellular transport | journal = J. Biol. Chem. | volume = 264 | issue = 22 | pages = 13206–16 |date=Augustaugust 1989 | doi = 10.1016/S0021-9258(18)51616-1 | pmid = 2753912 | doi-access = free }}</ref>

Prije nego što se LPL može izlučiti iz ćrlija, potrebna je homodimerizacija.<ref name="Vannier-1989" /><ref name="Ong-1989">{{cite journal |vauthors=Ong JM, Kern PA | title = The role of glucose and glycosylation in the regulation of lipoprotein lipase synthesis and secretion in rat adipocytes | journal = J. Biol. Chem. | volume = 264 | issue = 6 | pages = 3177–82 |date=Februaryfebruar 1989 | doi = 10.1016/S0021-9258(18)94047-0 | pmid = 2644281 | doi-access = free }}</ref> Nakon sekrecije, LPL se prenosi kroz [[endotel]]ne ćelije i uvodi u lumen kapilara, pomoću proteina [[glikozilfosfatidilinositol]]skog usidrenog proteina velike gustoće koji veže lipoprotein 1.<ref name="pmid17403372">{{cite journal |vauthors=Beigneux AP, Davies BS, Gin P, Weinstein MM, Farber E, Qiao X, Peale F, Bunting S, Walzem RL, Wong JS, Blaner WS, Ding ZM, Melford K, Wongsiriroj N, Shu X, de Sauvage F, Ryan RO, Fong LG, Bensadoun A, Young SG | title = Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons. | journal = Cell Metabolism | volume = 5 | issue = 4 | pages = 279–291 | year = 2007 | pmid = 17403372 | doi=10.1016/j.cmet.2007.02.002 | pmc=1913910}}</ref><ref name="pmid20620994">{{cite journal | vauthors = Davies BS, Beigneux AP, Barnes RH, Tu Y, Gin P, Weinstein MM, Nobumori C, Nyrén R, Goldberg I, Olivecrona G, Bensadoun A, Young SG, Fong LG | title = GPIHBP1 is responsible for the entry of lipoprotein lipase into capillaries | journal = Cell Metabolism | volume = 12 | issue = 1 | pages = 42–52 | date = Julyjuli 2010 | pmid = 20620994 | pmc = 2913606 | doi = 10.1016/j.cmet.2010.04.016 }}</ref>

[[Aktivno mjesto]] LPL-a sastoji se od konzervirane trijade Ser-132, Asp-156 i His-241. Ostala važna područja N-terminalnog domena za katalizu uključuju [[oksijanska rupa|oksijanionsku rupu]] (Trp-55, Leu-133), područje poklopca (ostaci 216-239), kao i petlju β5 (ostaci 54-64 ). <ref name="Mead-2002" /><ref name="Wang-1992" /><ref name="Wong-1994" /> Mjesto vezivanja ApoC-II još je nepoznato, ali se predviđa da su za nastanak ove interakcije potrebni ostaci i na N- i na C-terminalnim domenama. C-terminalni domen daje specifičnost LPL supstrata; ima veći afinitet za velike lipoproteine bogate triacilgliceridima od lipoproteina bogatih [[holesterol]]om.<ref name="Lookene-2000">{{cite journal |vauthors=Lookene A, Nielsen MS, Gliemann J, Olivecrona G | title = Contribution of the carboxy-terminal domain of lipoprotein lipase to interaction with heparin and lipoproteins | journal = Biochem. Biophys. Res. Commun. | volume = 271 | issue = 1 | pages = 15–21 |date=Aprilapril 2000 | pmid = 10777674 | doi = 10.1006/bbrc.2000.2530 }}</ref> C-terminalni domen je također važan za vezivanje za receptore [[LDL]].<ref name="Medh-1996">{{cite journal |vauthors=Medh JD, Bowen SL, Fry GL, Ruben S, Andracki M, Inoue I, Lalouel JM, Strickland DK, Chappell DA | title = Lipoprotein lipase binds to low density lipoprotein receptors and induces receptor-mediated catabolism of very low density lipoproteins in vitro | journal = J. Biol. Chem. | volume = 271 | issue = 29 | pages = 17073–80 |date=Julyjuli 1996 | pmid = 8663292 | doi = 10.1074/jbc.271.29.17073 | doi-access = free }}</ref> I N- i C-terminalni domeni sadrže [[heparin]]ska mjesta vezivanja, distalno od mjesta vezivanja lipida; LPL stoga služi kao most između ćelijske površine i lipoproteina. Važno je da vezanje LPL-a na ćelijskuu površinu ili receptore ne ovisi o njegovoj katalitskoj aktivnosti.<ref name="Beisiegel-1991">{{cite journal |vauthors=Beisiegel U, Weber W, Bengtsson-Olivecrona G | title = Lipoprotein lipase enhances the binding of chylomicrons to low density lipoprotein receptor-related protein | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 88 | issue = 19 | pages = 8342–6 |date=Octoberoktobar 1991 | pmid = 1656440 | pmc = 52504 | doi = 10.1073/pnas.88.19.8342 | bibcode = 1991PNAS...88.8342B | doi-access = free }}</ref>

Za svaki LPL dimer mogu se vezati po dvije molekule ApoC-II.<ref name="McIlhargey-2003">{{cite journal |vauthors=McIlhargey TL, Yang Y, Wong H, Hill JS | title = 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 | journal = J. Biol. Chem. | volume = 278 | issue = 25 | pages = 23027–35 |date=Junejuni 2003 | pmid = 12682050 | doi = 10.1074/jbc.M300315200 | doi-access = free }}</ref> Procjenjuje se da na jedan lipoprotein može istovremeno djelovati do četrdeset LPL dimera.<ref name="Mead-2002"/> Što se tiče kinetike, vjeruje se da je puštanje proizvoda u promet u [[korak ograničavanja brzine|koraka ograničavanja brzine reakcije]]. <Refref name = "Wang-1992" />

LPL gen kodira lipoprotein-lipazu koja se eksprimira u [[srce|srcu]], [[mišić]]ima i [[masno tkivo|masnom tkivu]].<ref name="Protein Atlas">{{cite web |last1=Protein Atlas |first1=Protein Atlas |title=Tissue expression of LPL - Summary - The Human Protein Atlas |url=https://www.proteinatlas.org/ENSG00000175445-LPL/tissue |website=www.proteinatlas.org |publisher=The Human Protein Atlas |access-date=25. July7. 2019}}</ref><ref name="Gene Cards">{{cite web |last1=Gene Cards |first1=Gene Cards |title=Human Gene Database |url=https://www.genecards.org/cgi-bin/carddisp.pl?gene=LPL |website=www.genecards.org |publisher=GeneCardsSuite |access-date=25. July7. 2019}}</ref> LPL funkcionira kao homodimer i ima dvostruke funkcije triglicerid-[[hidrolaze]] i [[ligand]]/premošćujućeg faktora za receptorski posredovanu apsorpciju lipoproteina. Putem katalize, VLDL se pretvara u [[Lipoprotein srednje gustoće|IDL]], a zatim u LDL. Teške [[mutacije]] koje uzrokuju nedostatak LPL rezultiraju hiperlipoproteinemijom tipa I, dok su manje ekstremne mutacije u LPL povezane s mnogim poremećajima [[metabolizam|metabolizma]] [[lipoprotein]]a.<ref>{{cite web | title = Entrez Gene: LPL lipoprotein lipase| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4023}}</ref>

LPL [[izozimi]] se različito reguliraju, ovisno o tkivu. Naprimjer, poznato je da [[insulin]] aktivira LPL u [[adipocit]]ima i njegovo postavljanje u [[endotel]] kapilara. Nasuprot tome, pokazalo se da insulin smanjuje ekspresiju mišićnih LPL.<ref name="pmid2677048">{{cite journal |vauthors=Kiens B, Lithell H, Mikines KJ, Richter EA | title = Effects of insulin and exercise on muscle lipoprotein lipase activity in man and its relation to insulin action | journal = J. Clin. Invest. | volume = 84 | issue = 4 | pages = 1124–9 |date=Octoberoktobar 1989 | pmid = 2677048 | pmc = 329768 | doi = 10.1172/JCI114275 }}</ref> Umjesto toga, mišićne i [[miokard]]ne LPL aktiviraju [[glukagon]] i [[adrenalin]]. Ovo pomaže objašnjnu zašto se tokom posta aktivnost LPL povećava u mišićnom tkivu, a smanjuje u masnom tkivu, dok se nakon obroka događa suprotno.<ref name="Mead-2002" /><ref name="Braun-1992" />

U skladu s tim, makronutrijenti u prehrani različito utiču na aktivnost LPL masti i mišića. Nakon 16 dana na dijeti s visokim udjelom ugljikohidrata ili s visokim udjelom masti, aktivnost LPL značajno se povećala u oba tkiva, šestr sati nakon obroka bilo kojeg sastava, ali došlo je i do značajno većeg porasta LPL u masnom tkivu, kao odgovor na dijetu s visokim udjelom ugljikohidrata u odnosu na ishranu bogatu mastima. Nije bilo razlike između učinaka dviju dijeta na osjetljivost na insulin ili aktivnost LPL natašte u bilo kojem tkivu.<ref name=Yost>{{cite journal |vauthors=Yost TJ, Jensen DR, Haugen BR, Eckel RH | title = Effect of dietary macronutrient composition on tissue-specific lipoprotein lipase activity and insulin action in normal-weight subjects | journal = Am. J. Clin. Nutr. | volume = 68 | issue = 2 | pages = 296–302 |date=Augustaugust 1998 | pmid = 9701186 | doi = 10.1093/ajcn/68.2.296| url = http://ajcn.nutrition.org/content/68/2/296.full.pdf | doi-access = free }}</ref>

Koncentracija LPL prikazana na površini endotelnih ćelija ne može se regulirati endotelnim ćelijama, jer niti sintetiziraju niti razgrađuju LPL. Umjesto toga, do ove regulacije dolazi upravljanjem protokom LPL-a koji stiže na lipolitsko mjesto i reguliranjem aktivnosti LPL-a prisutnog na endotelu. Ključni protein uključen u kontrolu aktivnosti LPL je [[ANGPTL4]], koji služi kao lokalni inhibitor LPL. Indukcija [[ANGPTL4]] objašnjava inhibiciju aktivnosti LPL -a u bijelom masnom tkivu tokom gladovanja. Sve veći dokazi impliciraju [[ANGPTL4]] u fiziološkoj regulaciji aktivnosti LPL u različitim tkivima. <ref name="pmid24397894">{{cite journal |vauthors=Dijk W, Kersten S | title = Regulation of lipoprotein lipase by Angptl4. | journal = Trends Endocrinol. Metab. | volume = 25 | issue = 3 | pages = 146–155 | year = 2014 | pmid = 24397894 | doi = 10.1016/j.tem.2013.12.005 | s2cid = 10273285 }}</ref>

Za objašnjenje varijacija aktivnosti LPL-a tokom ciklusa brzog hranjenja, predložen je model ANGPTL3-4-8.<ref name="PMID 27053679">{{cite journal | vauthors = Zhang R | title = The ANGPTL3-4-8 model, a molecular mechanism for triglyceride trafficking. | journal = Open Biol. | volume = 6 | issue = 4 | pages = 150272 | date = Aprilapril 2016 | pmid = 27053679 | doi = 10.1098/rsob.150272 | pmc=4852456}}</ref> Konkretno, hranjenje inducira ANGPTL8, aktivirajući put ANGPTL8-ANGPTL3, koji inhibira LPL u srčanim i skeletnim mišićima, čime se cirkulirajući trigliceridi stavljaju na raspolaganje za unos u bijelo masno tkivo, u kojem je aktivnost LPL povećana zbog smanjenja ANGPTL4; obrnuto je za vrijeme posta, koji potiskuje ANGPTL8, ali inducira ANGPTL4, usmjeravajući tako trigliceride u mišiće. Model predlaže opći okvir za reguliranje prometa triglicerida.<ref name= "PMID 27053679"/>

[[Nedostatak lipoprotein lipaze]] dovodi do [[hipertrigliceridemija|hipertrigliceridemije]] (povišenih nivoa [[triglicerid]]a u [[krvotok]]u).<ref name="pmid17706445">{{cite journal |vauthors=Okubo M, Horinishi A, Saito M, Ebara T, Endo Y, Kaku K, Murase T, Eto M | title = A novel complex deletion-insertion mutation mediated by Alu repetitive elements leads to lipoprotein lipase deficiency | journal = Mol. Genet. Metab. | volume = 92 | issue = 3 | pages = 229–33 |date=Novembernovembar 2007 | pmid = 17706445 | doi = 10.1016/j.ymgme.2007.06.018 }}</ref> U miševa je pokazano da prekomjerna ekspresija LPL uzrokuje [[otpornost na insulin]],<ref name="pmid11334409">{{cite journal|vauthors=Ferreira LD, Pulawa LK, Jensen DR, Eckel RH | title=Overexpressing human lipoprotein lipase in mouse skeletal muscle is associated with insulin resistance. | journal=Diabetes | year= 2001 | volume= 50 | issue= 5 | pages= 1064–8 | doi= 10.2337/diabetes.50.5.1064| pmid=11334409 | doi-access= free }}</ref><ref name="pmid11390966">{{cite journal |vauthors=Kim JK, Fillmore JJ, Chen Y, Yu C, Moore IK, Pypaert M, etal | title=Tissue-specific overexpression of lipoprotein lipase causes tissue-specific insulin resistance. | journal=Proc Natl Acad Sci U S A | year= 2001 | volume= 98 | issue= 13 | pages= 7522–7 | pmid=11390966 | doi=10.1073/pnas.121164498 | pmc=34701 | bibcode=2001PNAS...98.7522K | doi-access=free }}</ref> i podstiče [[gojaznost]].<ref name="pmid22562834"/>

Odgovor na visoku razinu LPL masnog tkiva pri dijeti bogatoj ugljikohidratima može predisponirati povećanje masnoće. Jedno istraživanje pokazalo je da su ispitanici dobili više tjelesne masti u sljedeće četiri godine ako su, nakon dijete s visokim udjelom ugljikohidrata i obroka bogatog ugljikohidratima, odgovorili povećanjem aktivnosti LPL masnog tkiva po adipocitu ili smanjenjem koštanog tkiva mišićna LPL aktivnost po gramu tkiva.<ref name=Ferland,2012>{{cite journal |vauthors=Ferland A, Château-Degat ML, Hernandez TL, Eckel RH | title = Tissue-specific responses of lipoprotein lipase to dietary macronutrient composition as a predictor of weight gain over 4 years | journal = Obesity (Silver Spring) | volume = 20 | issue = 5 | pages = 1006–11 |date=Maymaj 2012 | pmid = 22262159 | doi = 10.1038/oby.2011.372 | s2cid = 40167321 | doi-access = free }}</ref>

Pokazalo se da je ekspresija LPL prognostički prediktor u [[Hronična limfocitna leukemija|hroničnu limfocitnu leukemiju]].<ref>{{cite journal | vauthors = Prieto D, Oppezzo P | title = Lipoprotein Lipase Expression in Chronic Lymphocytic Leukemia: New Insights into Leukemic Progression | journal = Molecules | volume = 22 | issue = 12 | pages = 2083 | date = Decemberdecembar 2017 | pmid = 29206143 | pmc = 6149886 | doi = 10.3390/molecules22122083 | doi-access = free }}</ref> Čini se da u ovom [[krv]]nom poremećaju LPL daje [[masne kiseline]], kao izvor energije malignim ćelijama.<ref>{{cite journal | vauthors = Rozovski U, Hazan-Halevy I, Barzilai M, Keating MJ, Estrov Z | title = Metabolism pathways in chronic lymphocytic leukemia | journal = Leukemia & Lymphoma | volume = 57 | issue = 4 | pages = 758–65 | date = 8. December12. 2015 | pmid = 26643954 | pmc = 4794359 | doi = 10.3109/10428194.2015.1106533 }}</ref> Stoga se povišeni nivoi LPL-ove [[iRNK]] ili [[protein]]a smatraju pokazateljima loše prognoze.<ref>{{cite journal | vauthors = Oppezzo P, Vasconcelos Y, Settegrana C, Jeannel D, Vuillier F, Legarff-Tavernier M, Kimura EY, Bechet S, Dumas G, Brissard M, Merle-Béral H, Yamamoto M, Dighiero G, Davi F | title = The LPL/ADAM29 expression ratio is a novel prognosis indicator in chronic lymphocytic leukemia | journal = Blood | volume = 106 | issue = 2 | pages = 650–7 | date = Julyjuli 2005 | pmid = 15802535 | doi = 10.1182/blood-2004-08-3344 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Heintel D, Kienle D, Shehata M, Kröber A, Kroemer E, Schwarzinger I, Mitteregger D, Le T, Gleiss A, Mannhalter C, Chott A, Schwarzmeier J, Fonatsch C, Gaiger A, Döhner H, Stilgenbauer S, Jäger U | title = High expression of lipoprotein lipase in poor risk B-cell chronic lymphocytic leukemia | journal = Leukemia | volume = 19 | issue = 7 | pages = 1216–23 | date = Julyjuli 2005 | pmid = 15858619 | doi = 10.1038/sj.leu.2403748 | doi-access = free }}</ref><ref>{{cite journal | vauthors = van't Veer MB, Brooijmans AM, Langerak AW, Verhaaf B, Goudswaard CS, Graveland WJ, van Lom K, Valk PJ | title = The predictive value of lipoprotein lipase for survival in chronic lymphocytic leukemia | journal = Haematologica | volume = 91 | issue = 1 | pages = 56–63 | date = Januaryjanuar 2006 | pmid = 16434371 }}</ref><ref>{{cite journal | vauthors = Nückel H, Hüttmann A, Klein-Hitpass L, Schroers R, Führer A, Sellmann L, Dührsen U, Dürig J | title = Lipoprotein lipase expression is a novel prognostic factor in B-cell chronic lymphocytic leukemia | journal = Leukemia & Lymphoma | volume = 47 | issue = 6 | pages = 1053–61 | date = Junejuni 2006 | pmid = 16840197 | doi = 10.1080/10428190500464161 | s2cid = 20532204 }}</ref><ref>{{cite journal | vauthors = Mansouri M, Sevov M, Fahlgren E, Tobin G, Jondal M, Osorio L, Roos G, Olivecrona G, Rosenquist R | title = Lipoprotein lipase is differentially expressed in prognostic subsets of chronic lymphocytic leukemia but displays invariably low catalytical activity | journal = Leukemia Research | volume = 34 | issue = 3 | pages = 301–6 | date = Marchmart 2010 | pmid = 19709746 | doi = 10.1016/j.leukres.2009.07.032 }}</ref><ref>{{cite journal | vauthors = Kaderi MA, Kanduri M, Buhl AM, Sevov M, Cahill N, Gunnarsson R, Jansson M, Smedby KE, Hjalgrim H, Jurlander J, Juliusson G, Mansouri L, Rosenquist R | title = LPL is the strongest prognostic factor in a comparative analysis of RNA-based markers in early chronic lymphocytic leukemia | journal = Haematologica | volume = 96 | issue = 8 | pages = 1153–60 | date = Augustaugust 2011 | pmid = 21508119 | pmc = 3148909 | doi = 10.3324/haematol.2010.039396 }}</ref><ref>{{cite journal | vauthors = Porpaczy E, Tauber S, Bilban M, Kostner G, Gruber M, Eder S, Heintel D, Le T, Fleiss K, Skrabs C, Shehata M, Jäger U, Vanura K | title = Lipoprotein lipase in chronic lymphocytic leukaemia - strong biomarker with lack of functional significance | journal = Leukemia Research | volume = 37 | issue = 6 | pages = 631–6 | date = Junejuni 2013 | pmid = 23478142 | doi = 10.1016/j.leukres.2013.02.008 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Mátrai Z, Andrikovics H, Szilvási A, Bors A, Kozma A, Ádám E, Halm G, Karászi É, Tordai A, Masszi T | title = Lipoprotein Lipase as a Prognostic Marker in Chronic Lymphocytic Leukemia | journal = Pathology Oncology Research | volume = 23 | issue = 1 | pages = 165–171 | date = Januaryjanuar 2017 | pmid = 27757836 | doi = 10.1007/s12253-016-0132-z | s2cid = 22647616 }}</ref><ref>{{cite journal | vauthors = Prieto D, Seija N, Uriepero A, Souto-Padron T, Oliver C, Irigoin V, Guillermo C, Navarrete MA, Inés Landoni A, Dighiero G, Gabus R, Giordano M, Oppezzo P | title = LPL protein in Chronic Lymphocytic Leukaemia have different origins in Mutated and Unmutated patients. Advances for a new prognostic marker in CLL | journal = British Journal of Haematology | volume = 182 | issue = 4 | pages = 521–525 | date = Augustaugust 2018 | pmid = 29953583 | doi = 10.1111/bjh.15427 | doi-access = free }}</ref><ref>{{cite journal | vauthors = Rombout A, Verhasselt B, Philippé J | title = Lipoprotein lipase in chronic lymphocytic leukemia: function and prognostic implications | journal = European Journal of Haematology | volume = 97 | issue = 5 | pages = 409–415 | date = Novembernovembar 2016 | pmid = 27504855 | doi = 10.1111/ejh.12789 | doi-access = free }}</ref>

Pokazalo se da lipoprotein-lipaza [[interakcija protein-protein | stupa u interakciju]] sa [[LRP1]]. <ref name="pmid7510694">{{cite journal |vauthors=Williams SE, Inoue I, Tran H, Fry GL, Pladet MW, Iverius PH, Lalouel JM, Chappell DA, Strickland DK | title = The carboxyl-terminal domain of lipoprotein lipase binds to the low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor (LRP) and mediates binding of normal very low density lipoproteins to LRP | journal = J. Biol. Chem. | volume = 269 | issue = 12 | pages = 8653–8 |date=Marchmart 1994 | doi = 10.1016/S0021-9258(17)37017-5 | pmid = 7510694 | doi-access = free }}</ref><ref name="pmid7989348">{{cite journal |vauthors=Nykjaer A, Nielsen M, Lookene A, Meyer N, Røigaard H, Etzerodt M, Beisiegel U, Olivecrona G, Gliemann J | title = A carboxyl-terminal fragment of lipoprotein lipase binds to the low density lipoprotein receptor-related protein and inhibits lipase-mediated uptake of lipoprotein in cells | journal = J. Biol. Chem. | volume = 269 | issue = 50 | pages = 31747–55 |date=Decemberdecembar 1994 | doi = 10.1016/S0021-9258(18)31759-9 | pmid = 7989348 | doi-access = free }}</ref><ref name="pmid1281473">{{cite journal |vauthors=Chappell DA, Fry GL, Waknitz MA, Iverius PH, Williams SE, Strickland DK | title = The low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor binds and mediates catabolism of bovine milk lipoprotein lipase | journal = J. Biol. Chem. | volume = 267 | issue = 36 | pages = 25764–7 |date=Decemberdecembar 1992 | doi = 10.1016/S0021-9258(18)35675-8 | pmid = 1281473 | doi-access = free }}</ref> Također je [[ligand]] za [[α2M]], [[GP330]] i VLDL receptore.<ref name="Medh-1996"/> Pokazalo se da je LPL [[ligand]] za [[LRP2]], iako sa manjim afinitetom nego za druge receptore; međutim, većina degradacije VLDL-a ovisne o LPL-u može se pripisati putu LRP2.<ref name="Medh-1996"/> U svakom slučaju, LPL služi kao most između receptora i lipoproteina.

LPL gen je visoko konzerviran kod [[kičmenjak]]a. Lipoprotein-lipaza je uključena u transport lipida u posteljicu živih guštera (''[[Pseudemoia entrecasteauxii]]'').<ref name="pmid23939756">{{cite journal | vauthors = Griffith OW, Ujvari B, Belov K, Thompson MB | title = Placental lipoprotein lipase (LPL) gene expression in a placentotrophic lizard, Pseudemoia entrecasteauxii | journal = Journal of Experimental Zoology Part B: Molecular and Developmental Evolution | volume = 320 | issue = 7 | pages = 465–70 | date = Novembernovembar 2013 | pmid = 23939756 | doi = 10.1002/jez.b.22526 }}</ref>

*{{cite journal |vauthors=Lichtenstein L, Berbée JF, van Dijk SJ, van Dijk KW, Bensadoun A, Kema IP, Voshol PJ, Müller M, Rensen PC, Kersten S | title = Angptl4 upregulates cholesterol synthesis in liver via inhibition of LPL- and HL-dependent hepatic cholesterol uptake | journal = Arterioscler. Thromb. Vasc. Biol. | volume = 27 | issue = 11 | pages = 2420–7 |date=Novembernovembar 2007 | pmid = 17761937 | doi = 10.1161/ATVBAHA.107.151894 | doi-access = free }}

*{{cite journal |vauthors=Lichtenstein L, Mattijssen F, de Wit NJ, Georgiadi A, Hooiveld GJ, van der Meer R, He Y, Qi L, Köster A, Tamsma JT, Tan NS, Müller M, Kersten S | title = Angptl4 protects against severe proinflammatory effects of saturated fat by inhibiting fatty acid uptake into mesenteric lymph node macrophages | journal = Cell Metab. | volume = 12 | issue = 6 | pages = 580–92 |date=Decemberdecembar 2010 | pmid = 21109191 | pmc = 3387545 | doi = 10.1016/j.cmet.2010.11.002 }}