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Volumn 5, Issue JANUARY2016, 2016, Pages

The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain

Author keywords

[No Author keywords available]

Indexed keywords

ENTEROPEPTIDASE; ESTERASE; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED HIGH DENSITY LIPOPROTEIN BINDING PROTEIN 1; HIGH DENSITY LIPOPROTEIN; LIPOPROTEIN LIPASE; UNCLASSIFIED DRUG; GPIHBP1 PROTEIN, HUMAN; LIPOPROTEIN RECEPTOR; PROTEIN BINDING;

EID: 84958559658     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.12095.001     Document Type: Article
Times cited : (91)

References (58)
  • 6
    • 84929965815 scopus 로고    scopus 로고
    • Chylomicronaemia-current diagnosis and future therapies
    • Brahm AJ, Hegele RA. 2015. Chylomicronaemia-current diagnosis and future therapies. Nature Reviews Endocrinology 11: 352-362. doi: 10. 1038/nrendo. 2015. 26.
    • (2015) Nature Reviews Endocrinology , vol.11 , pp. 352-362
    • Brahm, A.J.1    Hegele, R.A.2
  • 7
    • 84931319675 scopus 로고    scopus 로고
    • JCL roundtable: Hypertriglyceridemia due to defects in lipoprotein lipase function
    • Brown WV, Goldberg IJ, Young SG. 2015. JCL roundtable: hypertriglyceridemia due to defects in lipoprotein lipase function. Journal of Clinical Lipidology 9: 274-280. doi: 10. 1016/j. jacl. 2015. 03. 009.
    • (2015) Journal of Clinical Lipidology , vol.9 , pp. 274-280
    • Brown, W.V.1    Goldberg, I.J.2    Young, S.G.3
  • 8
    • 84928825565 scopus 로고    scopus 로고
    • A 3-day-old neonate with severe hypertriglyceridemia from novel mutations of the GPIHBP1 gene
    • Buonuomo PS, Bartuli A, Rabacchi C, Bertolini S, Calandra S. 2015. A 3-day-old neonate with severe hypertriglyceridemia from novel mutations of the GPIHBP1 gene. Journal of Clinical Lipidology 9: 265-270. doi: 10. 1016/j. jacl. 2014. 10. 003.
    • (2015) Journal of Clinical Lipidology , vol.9 , pp. 265-270
    • Buonuomo, P.S.1    Bartuli, A.2    Rabacchi, C.3    Bertolini, S.4    Calandra, S.5
  • 9
    • 0032413609 scopus 로고    scopus 로고
    • Detailed characterization of the binding site of the lipoprotein lipase-specific monoclonal antibody 5D2
    • Chang SF, Reich B, Brunzell JD, Will H. 1998. Detailed characterization of the binding site of the lipoprotein lipase-specific monoclonal antibody 5D2. Journal of Lipid Research 39: 2350-2359.
    • (1998) Journal of Lipid Research , vol.39 , pp. 2350-2359
    • Chang, S.F.1    Reich, B.2    Brunzell, J.D.3    Will, H.4
  • 10
    • 0022244859 scopus 로고
    • Purification and characterization of human lipoprotein lipase and hepatic triglyceride lipase reactivity with monoclonal antibodies to hepatic triglyceride lipase
    • Cheng CF, Bensadoun A, Bersot T, Hsu JS, Melford KH. 1985. Purification and characterization of human lipoprotein lipase and hepatic triglyceride lipase. reactivity with monoclonal antibodies to hepatic triglyceride lipase. The Journal of Biological Chemistry 260: 10720-10727.
    • (1985) The Journal of Biological Chemistry , vol.260 , pp. 10720-10727
    • Cheng, C.F.1    Bensadoun, A.2    Bersot, T.3    Hsu, J.S.4    Melford, K.H.5
  • 12
    • 24044538903 scopus 로고    scopus 로고
    • IUPred: Web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content
    • Dosztanyi Z, Csizmok V, Tompa P, Simon I. 2005. IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 21: 3433-3434.
    • (2005) Bioinformatics , vol.21 , pp. 3433-3434
    • Dosztanyi, Z.1    Csizmok, V.2    Tompa, P.3    Simon, I.4
  • 13
    • 0030848555 scopus 로고    scopus 로고
    • A single Ser259Arg mutation in the gene for lipoprotein lipase causes chylomicronemia in moroccans of berber ancestry
    • Foubert L, Bruin T, Gennes JLD, Ehrenborg E, Furioli J, Kastelein J, Benlian P, Hayden M. 1997. A single Ser259Arg mutation in the gene for lipoprotein lipase causes chylomicronemia in moroccans of berber ancestry. Human Mutation 10: 179-185. doi: 10. 1002/(SICI)1098-1004(1997)10: 3<179:: AID-HUMU1>3. 0. CO; 2-E.
    • (1997) Human Mutation , vol.10 , pp. 179-185
    • Foubert, L.1    Bruin, T.2    Gennes, J.L.D.3    Ehrenborg, E.4    Furioli, J.5    Kastelein, J.6    Benlian, P.7    Hayden, M.8
  • 16
    • 0029912304 scopus 로고    scopus 로고
    • A mutation in the lipoprotein lipase gene is the molecular basis of chylomicronemia in a colony of domestic cats
    • Ginzinger DG, Lewis ME, Ma Y, Jones BR, Liu G, Jones SD. 1996. A mutation in the lipoprotein lipase gene is the molecular basis of chylomicronemia in a colony of domestic cats. Journal of Clinical Investigation 97: 1257-1266. doi: 10. 1172/JCI118541.
    • (1996) Journal of Clinical Investigation , vol.97 , pp. 1257-1266
    • Ginzinger, D.G.1    Lewis, M.E.2    Ma, Y.3    Jones, B.R.4    Liu, G.5    Jones, S.D.6
  • 17
    • 84891365639 scopus 로고    scopus 로고
    • Fixed charges in the gel matrix of sensor chips and dissociation in diffusion gradients influence the detection of fast protein-protein interactions
    • Glaser RW, Schö nherr R, Heinemann SH. 2014. Fixed charges in the gel matrix of sensor chips and dissociation in diffusion gradients influence the detection of fast protein-protein interactions. Biosystems 116: 27-35. doi: 10. 1016/j. biosystems. 2013. 09. 009.
    • (2014) Biosystems , vol.116 , pp. 27-35
    • Glaser, R.W.1    Schö nherr, R.2    Heinemann, S.H.3
  • 19
    • 12144288162 scopus 로고    scopus 로고
    • Characterization of low-glycosylated forms of soluble human urokinase receptor expressed in drosophila schneider 2 cells after deletion of glycosylation-sites
    • Gårdsvoll H, Werner F, Søndergaard L, Danø K, Ploug M. 2004. Characterization of low-glycosylated forms of soluble human urokinase receptor expressed in drosophila schneider 2 cells after deletion of glycosylation-sites. Protein Expression and Purification 34: 284-295. doi: 10. 1016/j. pep. 2003. 12. 002.
    • (2004) Protein Expression and Purification , vol.34 , pp. 284-295
    • Gårdsvoll, H.1    Werner, F.2    Søndergaard, L.3    Danø, K.4    Ploug, M.5
  • 21
    • 33846419101 scopus 로고    scopus 로고
    • A new tagging system for production of recombinant proteins in drosophila S2 cells using the third domain of the urokinase receptor
    • Gårdsvoll H, Hansen LV, Jørgensen TJD, Ploug M. 2007. A new tagging system for production of recombinant proteins in drosophila S2 cells using the third domain of the urokinase receptor. Protein Expression and Purification 52: 384-394. doi: 10. 1016/j. pep. 2006. 11. 013.
    • (2007) Protein Expression and Purification , vol.52 , pp. 384-394
    • Gårdsvoll, H.1    Hansen, L.V.2    Jørgensen, T.J.D.3    Ploug, M.4
  • 22
    • 80052987387 scopus 로고    scopus 로고
    • Conformational regulation of urokinase receptor function: Impact of receptor occupancy and epitope-mapped monoclonal antibodies on lamellipodia induction
    • Gardsvoll H, Jacobsen B, Kriegbaum MC, Behrendt N, Engelholm L, Ostergaard S, Ploug M. 2011. Conformational regulation of urokinase receptor function: impact of receptor occupancy and epitope-mapped monoclonal antibodies on lamellipodia induction. Journal of Biological Chemistry 286: 33544-33556. doi: 10. 1074/jbc. M111. 220087.
    • (2011) Journal of Biological Chemistry , vol.286 , pp. 33544-33556
    • Gardsvoll, H.1    Jacobsen, B.2    Kriegbaum, M.C.3    Behrendt, N.4    Engelholm, L.5    Ostergaard, S.6    Ploug, M.7
  • 23
    • 84887331252 scopus 로고    scopus 로고
    • The urokinase receptor homolog haldisin is a novel differentiation marker of stratum granulosum in squamous epithelia
    • Gardsvoll H, Kriegbaum MC, Hertz EP, Alpizar-Alpizar W, Ploug M. 2013. The urokinase receptor homolog haldisin is a novel differentiation marker of stratum granulosum in squamous epithelia. Journal of Histochemistry & Cytochemistry 61: 802-813. doi: 10. 1369/0022155413501879.
    • (2013) Journal of Histochemistry & Cytochemistry , vol.61 , pp. 802-813
    • Gardsvoll, H.1    Kriegbaum, M.C.2    Hertz, E.P.3    Alpizar-Alpizar, W.4    Ploug, M.5
  • 27
    • 0032509854 scopus 로고    scopus 로고
    • A novel Glu421Lys substitution in the lipoprotein lipase gene in pregnancy-induced hypertriglyceridemic pancreatitis
    • Henderson H, Leisegang F, Hassan F, Hayden M, Marais D. 1998. A novel Glu421Lys substitution in the lipoprotein lipase gene in pregnancy-induced hypertriglyceridemic pancreatitis. Clinica Chimica Acta 269: 1-12. doi: 10. 1016/S0009-8981(97)00144-7.
    • (1998) Clinica Chimica Acta , vol.269 , pp. 1-12
    • Henderson, H.1    Leisegang, F.2    Hassan, F.3    Hayden, M.4    Marais, D.5
  • 29
    • 84925251625 scopus 로고    scopus 로고
    • DISOPRED3: Precise disordered region predictions with annotated protein-binding activity
    • Jones DT, Cozzetto D. 2015. DISOPRED3: precise disordered region predictions with annotated protein-binding activity. Bioinformatics 31: 857-863.
    • (2015) Bioinformatics , vol.31 , pp. 857-863
    • Jones, D.T.1    Cozzetto, D.2
  • 30
    • 9744223518 scopus 로고    scopus 로고
    • Dynamics of urokinase receptor interaction with peptide antagonists studied by amide hydrogen exchange and mass spectrometry
    • Jørgensen TJ, Gårdsvoll H, Danø K, Roepstorff P, Ploug M. 2004. Dynamics of urokinase receptor interaction with peptide antagonists studied by amide hydrogen exchange and mass spectrometry. Biochemistry 43: 15044-15057.
    • (2004) Biochemistry , vol.43 , pp. 15044-15057
    • Jørgensen, T.J.1    Gårdsvoll, H.2    Danø, K.3    Roepstorff, P.4    Ploug, M.5
  • 33
    • 0036379409 scopus 로고    scopus 로고
    • Molecular modeling of the dimeric structure of human lipoprotein lipase and functional studies of the carboxyl-terminal domain
    • Kobayashi Y, Nakajima T, Inoue I. 2002. Molecular modeling of the dimeric structure of human lipoprotein lipase and functional studies of the carboxyl-terminal domain. Eur J Biochem 269: 4701-4710.
    • (2002) Eur J Biochem , vol.269 , pp. 4701-4710
    • Kobayashi, Y.1    Nakajima, T.2    Inoue, I.3
  • 34
    • 84873766944 scopus 로고
    • Clearing factor, a heparin-activated lipoprotein lipase i. isolation and characterization of the enzyme from normal rat heart
    • Korn ED. 1955. Clearing factor, a heparin-activated lipoprotein lipase. i. isolation and characterization of the enzyme from normal rat heart. The Journal of Biological Chemistry 215: 1-14.
    • (1955) The Journal of Biological Chemistry , vol.215 , pp. 1-14
    • Korn, E.D.1
  • 36
    • 84888335913 scopus 로고    scopus 로고
    • Apolipoproteins c-i and c-III inhibit lipoprotein lipase activity by displacement of the enzyme from lipid droplets
    • Larsson M, Vorrsjo E, Talmud P, Lookene A, Olivecrona G. 2013. Apolipoproteins c-i and c-III inhibit lipoprotein lipase activity by displacement of the enzyme from lipid droplets. Journal of Biological Chemistry 288: 33997-34008. doi: 10. 1074/jbc. M113. 495366.
    • (2013) Journal of Biological Chemistry , vol.288 , pp. 33997-34008
    • Larsson, M.1    Vorrsjo, E.2    Talmud, P.3    Lookene, A.4    Olivecrona, G.5
  • 37
    • 77951216201 scopus 로고    scopus 로고
    • Structure-based engineering of species selectivity in the interaction between urokinase and its receptor: Implication for preclinical cancer therapy
    • Lin L, Gardsvoll H, Huai Q, Huang M, Ploug M. 2010. Structure-based engineering of species selectivity in the interaction between urokinase and its receptor: implication for preclinical cancer therapy. Journal of Biological Chemistry 285: 10982-10992. doi: 10. 1074/jbc. M109. 093492.
    • (2010) Journal of Biological Chemistry , vol.285 , pp. 10982-10992
    • Lin, L.1    Gardsvoll, H.2    Huai, Q.3    Huang, M.4    Ploug, M.5
  • 39
    • 0029809050 scopus 로고    scopus 로고
    • Interaction of lipoprotein lipase with heparin fragments and with heparan sulfate: Stoichiometry, stabilization, and kinetics
    • Lookene A, Chevreuil O, Østergaard P, Olivecrona G. 1996. Interaction of lipoprotein lipase with heparin fragments and with heparan sulfate: stoichiometry, stabilization, and kinetics. Biochemistry 35: 12155-12163. doi: 10. 1021/bi960008e.
    • (1996) Biochemistry , vol.35 , pp. 12155-12163
    • Lookene, A.1    Chevreuil, O.2    Østergaard, P.3    Olivecrona, G.4
  • 42
    • 0022366273 scopus 로고
    • Studies on inactivation of lipoprotein lipase: Role of the dimer to monomer dissociation
    • Osborne JC, Bengtsson-Olivecrona G, Lee NS, Olivecrona T. 1985. Studies on inactivation of lipoprotein lipase: role of the dimer to monomer dissociation. Biochemistry 24: 5606-5611. doi: 10. 1021/bi00341a048.
    • (1985) Biochemistry , vol.24 , pp. 5606-5611
    • Osborne, J.C.1    Bengtsson-Olivecrona, G.2    Lee, N.S.3    Olivecrona, T.4
  • 43
    • 84901245913 scopus 로고    scopus 로고
    • Probing the structure of human protein disulfide isomerase by chemical cross-linking combined with mass spectrometry
    • Peng L, Rasmussen MI, Chailyan A, Houen G, Højrup P. 2014. Probing the structure of human protein disulfide isomerase by chemical cross-linking combined with mass spectrometry. Journal of Proteomics 108: 1-16. doi: 10. 1016/j. jprot. 2014. 04. 037.
    • (2014) Journal of Proteomics , vol.108 , pp. 1-16
    • Peng, L.1    Rasmussen, M.I.2    Chailyan, A.3    Houen, G.4    Højrup, P.5
  • 45
    • 0037967310 scopus 로고    scopus 로고
    • Structure-function relationships in the interaction between the urokinase-type plasminogen activator and its receptor
    • Ploug M. 2003. Structure-function relationships in the interaction between the urokinase-type plasminogen activator and its receptor. Current Pharmaceutical Design 9: 1499-1528. doi: 10. 2174/1381612033454630.
    • (2003) Current Pharmaceutical Design , vol.9 , pp. 1499-1528
    • Ploug, M.1
  • 46
    • 0028068081 scopus 로고
    • A novel missense mutation in the c-terminal domain of lipoprotein lipase (glu410->val) leads to enzyme inactivation and familial chylomicronemia
    • Previato L, Guardamagna O, Dugi KA, Ronan R, Talley GD, Santamarina-Fojo S, Brewer HB. 1994. A novel missense mutation in the c-terminal domain of lipoprotein lipase (glu410->val) leads to enzyme inactivation and familial chylomicronemia. Journal of Lipid Research 35: 1552-1560.
    • (1994) Journal of Lipid Research , vol.35 , pp. 1552-1560
    • Previato, L.1    Guardamagna, O.2    Dugi, K.A.3    Ronan, R.4    Talley, G.D.5    Santamarina-Fojo, S.6    Brewer, H.B.7
  • 47
    • 84930221886 scopus 로고    scopus 로고
    • Evidence for two distinct binding sites for lipoprotein lipase on glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (gPIHBP1)
    • Reimund M, Larsson M, Kovrov O, Kasvandik S, Olivecrona G, Lookene A. 2015. Evidence for two distinct binding sites for lipoprotein lipase on glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (gPIHBP1). Journal of Biological Chemistry 290: 13919-13934. doi: 10. 1074/jbc. M114. 634626.
    • (2015) Journal of Biological Chemistry , vol.290 , pp. 13919-13934
    • Reimund, M.1    Larsson, M.2    Kovrov, O.3    Kasvandik, S.4    Olivecrona, G.5    Lookene, A.6
  • 49
    • 0028871814 scopus 로고
    • Evaluation of comparative protein modeling by MODELLER
    • Sali A, Potterton L, Yuan F, van Vlijmen H, Karplus M. 1995. Evaluation of comparative protein modeling by MODELLER. Proteins 23: 318-326. doi: 10. 1002/prot. 340230306.
    • (1995) Proteins , vol.23 , pp. 318-326
    • Sali, A.1    Potterton, L.2    Yuan, F.3    van Vlijmen, H.4    Karplus, M.5
  • 50
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M. 1996. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Analytical Chemistry 68: 850-858. doi: 10. 1021/ac950914h.
    • (1996) Analytical Chemistry , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 51
    • 16344373015 scopus 로고    scopus 로고
    • Protein homology detection by HMM-HMM comparison
    • Soding J. 2005. Protein homology detection by HMM-HMM comparison. Bioinformatics 21: 951-960. doi: 10. 1093/bioinformatics/bti125.
    • (2005) Bioinformatics , vol.21 , pp. 951-960
    • Soding, J.1
  • 54
    • 84865346866 scopus 로고    scopus 로고
    • Size-exclusion chromatography in structural analysis of intrinsically disordered proteins
    • Uversky VN. 2012. Size-exclusion chromatography in structural analysis of intrinsically disordered proteins. Methods Mol Biol 896: 179-194. doi: 10. 1007/978-1-4614-3704-8_11.
    • (2012) Methods Mol Biol , vol.896 , pp. 179-194
    • Uversky, V.N.1
  • 56
    • 84863125697 scopus 로고    scopus 로고
    • Crystal structure of the urokinase receptor in a ligand-free form
    • Xu X, Gårdsvoll H, Yuan C, Lin L, Ploug M, Huang M. 2012. Crystal structure of the urokinase receptor in a ligand-free form. J Mol Biol 416: 629-641.
    • (2012) J Mol Biol , vol.416 , pp. 629-641
    • Xu, X.1    Gårdsvoll, H.2    Yuan, C.3    Lin, L.4    Ploug, M.5    Huang, M.6
  • 57
    • 84874900503 scopus 로고    scopus 로고
    • Biochemistry and pathophysiology of intravascular and intracellular lipolysis
    • Young SG, Zechner R. 2013. Biochemistry and pathophysiology of intravascular and intracellular lipolysis. Genes Dev 27: 459-484.
    • (2013) Genes Dev , vol.27 , pp. 459-484
    • Young, S.G.1    Zechner, R.2
  • 58
    • 84924163857 scopus 로고    scopus 로고
    • Stabilizing a flexible interdomain hinge region harboring the SMB binding site drives uPAR into its closed conformation
    • Zhao B, Gandhi S, Yuan C, Luo Z, Li R, Gårdsvoll H, de Lorenzi V. 2015. Stabilizing a flexible interdomain hinge region harboring the SMB binding site drives uPAR into its closed conformation. J Mol Biol 427: 1389-1403.
    • (2015) J Mol Biol , vol.427 , pp. 1389-1403
    • Zhao, B.1    Gandhi, S.2    Yuan, C.3    Luo, Z.4    Li, R.5    Gårdsvoll, H.6    de Lorenzi, V.7


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