메뉴 건너뛰기




Volumn 58, Issue 1, 2017, Pages 216-225

Mobility of "HSPG-bound" LPL explains how LPL is able to reach GPIHBP1 on capillaries

Author keywords

Chemistry; Endothelial cells; Glycosylphosphatidylinositolanchored high density lipoprotein binding protein; Heparan sulfate proteoglycan; Lipids; Lipolysis and fatty acid metabolism; Lipoprotein lipase; Supplementary chylomicrons; Triglycerides

Indexed keywords

AGAROSE; BINDING PROTEIN; CD31 ANTIGEN; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED HIGH DENSITY LIPOPROTEIN BINDING PROTEIN 1; LIPOPROTEIN LIPASE; PROTEOHEPARAN SULFATE; UNCLASSIFIED DRUG; CHYLOMICRON; CULTURE MEDIUM; GPI-HBP1 PROTEIN, MOUSE; LIPOPROTEIN RECEPTOR;

EID: 85009813255     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.M072520     Document Type: Article
Times cited : (38)

References (41)
  • 1
    • 0005026320 scopus 로고
    • Clearing factor, a heparin-activated lipoprotein lipase. II. Substrate specificity and activation of coconut oil
    • Korn, E. D. 1955. Clearing factor, a heparin-activated lipoprotein lipase. II. Substrate specificity and activation of coconut oil. J. Biol. Chem. 215: 15-26.
    • (1955) J. Biol. Chem. , vol.215 , pp. 15-26
    • Korn, E.D.1
  • 2
    • 84873766944 scopus 로고
    • Clearing factor, a heparin-activated lipoprotein lipase. I. Isolation and characterization of the enzyme from normal rat heart
    • Korn, E. D. 1955. Clearing factor, a heparin-activated lipoprotein lipase. I. Isolation and characterization of the enzyme from normal rat heart. J. Biol. Chem. 215: 1-14.
    • (1955) J. Biol. Chem. , vol.215 , pp. 1-14
    • Korn, E.D.1
  • 3
    • 0000717112 scopus 로고
    • Idiopathic hyperlipemia: Metabolic studies in an affected family
    • Havel, R. J., and R. S. Gordon, Jr. 1960. Idiopathic hyperlipemia: metabolic studies in an affected family. J. Clin. Invest. 39: 1777-1790.
    • (1960) J. Clin. Invest. , vol.39 , pp. 1777-1790
    • Havel, R.J.1    Gordon, R.S.2
  • 4
    • 0036906508 scopus 로고    scopus 로고
    • Lipoprotein lipase: Genetics, lipid uptake, and regulation
    • Merkel, M., R. H. Eckel, and I. J. Goldberg. 2002. Lipoprotein lipase: genetics, lipid uptake, and regulation. J. Lipid Res. 43: 1997-2006.
    • (2002) J. Lipid Res , vol.43 , pp. 1997-2006
    • Merkel, M.1    Eckel, R.H.2    Goldberg, I.J.3
  • 5
    • 0028149288 scopus 로고
    • 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
    • Ma, Y., H. E. Henderson, M. S. Liu, H. Zhang, I. J. Forsythe, I. Clarke- Lewis, M. R. Hayden, and J. D. Brunzell. 1994. 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. J. Lipid Res. 35: 2049-2059.
    • (1994) J. Lipid Res. , vol.35 , pp. 2049-2059
    • Ma, Y.1    Henderson, H.E.2    Liu, M.S.3    Zhang, H.4    Forsythe, I.J.5    Lewis I.C.-.6    Hayden, M.R.7    Brunzell, J.D.8
  • 6
    • 0031919847 scopus 로고    scopus 로고
    • Identification of the epitope of a monoclonal antibody that inhibits heparin binding of lipoprotein lipase: New evidence for a carboxylterminal heparin-binding domain
    • Sendak, R. A., K. Melford, A. Kao, and A. Bensadoun. 1998.Identification of the epitope of a monoclonal antibody that inhibits heparin binding of lipoprotein lipase: new evidence for a carboxylterminal heparin-binding domain. J. Lipid Res. 39: 633-646.
    • (1998) J. Lipid Res. , vol.39 , pp. 633-646
    • Sendak, R.A.1    Melford, K.2    Kao, A.3    Bensadoun, A.4
  • 7
    • 0034728777 scopus 로고    scopus 로고
    • Contribution of the carboxy-terminal domain of lipoprotein lipase to interaction with heparin and lipoproteins
    • Lookene, A., M. S. Nielsen, J. Gliemann, and G. Olivecrona. 2000. Contribution of the carboxy-terminal domain of lipoprotein lipase to interaction with heparin and lipoproteins. Biochem. Biophys. Res. Commun. 271: 15-21.
    • (2000) Biochem. Biophys. Res. Commun. , vol.271 , pp. 15-21
    • Lookene, A.1    Nielsen, M.S.2    Gliemann, J.3    Olivecrona, G.4
  • 8
    • 0027532544 scopus 로고
    • Binding of lipoprotein lipase to heparin. Identification of five critical residues in two distinct segments of the amino-terminal domain
    • Hata, A., D. N. Ridinger, S. Sutherland, M. Emi, Z. Shuhua, R. L. Myers, K. Ren, T. Cheng, I. Inoue, D. E. Wilson, et al. 1993. Binding of lipoprotein lipase to heparin. Identification of five critical residues in two distinct segments of the amino-terminal domain. J. Biol. Chem. 268: 8447-8457.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8447-8457
    • Hata, A.1    Ridinger, D.N.2    Sutherland, S.3    Emi, M.4    Shuhua, Z.5    Myers, R.L.6    Ren, K.7    Cheng, T.8    Inoue, I.9    Wilson, D.E.10
  • 9
    • 0031473195 scopus 로고    scopus 로고
    • Lipolysis of very low density lipoproteins by heparan sulfate proteoglycan-bound lipoprotein lipase
    • de Man, F. H., F. de Beer, A. van der Laarse, A. H. Smelt, and L. M. Havekes. 1997. Lipolysis of very low density lipoproteins by heparan sulfate proteoglycan-bound lipoprotein lipase. J. Lipid Res. 38: 2465-2472.
    • (1997) J. Lipid Res. , vol.38 , pp. 2465-2472
    • De Man, F.H.1    De Beer, F.2    Van Der Laarse, A.3    Smelt, A.H.4    Havekes, L.M.5
  • 11
    • 33947573537 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchored high-density lipoproteinbinding protein 1 plays a critical role in the lipolytic processing of chylomicrons
    • Beigneux, A. P., B. S. Davies, P. Gin, M. M. Weinstein, E. Farber, X. Qiao, F. Peale, S. Bunting, R. L. Walzem, J. S. Wong, et al. 2007. Glycosylphosphatidylinositol-anchored high-density lipoproteinbinding protein 1 plays a critical role in the lipolytic processing of chylomicrons. Cell Metab. 5: 279-291.
    • (2007) Cell Metab , vol.5 , pp. 279-291
    • Beigneux, A.P.1    Davies, B.S.2    Gin, P.3    Weinstein, M.M.4    Farber, E.5    Qiao, X.6    Peale, F.7    Bunting, S.8    Walzem, R.L.9    Wong, J.S.10
  • 18
    • 79960633816 scopus 로고    scopus 로고
    • Childhoodonset chylomicronaemia with reduced plasma lipoprotein lipase activity and mass: Identification of a novel GPIHBP1 mutation
    • Coca-Prieto, I., O. Kroupa, P. Gonzalez-Santos, J. Magne, G. Olivecrona, E. Ehrenborg, and P. Valdivielso. 2011. Childhoodonset chylomicronaemia with reduced plasma lipoprotein lipase activity and mass: identification of a novel GPIHBP1 mutation. J. Intern. Med. 270: 224-228.
    • (2011) J. Intern. Med. , vol.270 , pp. 224-228
    • Coca-Prieto, I.1    Kroupa, O.2    Gonzalez-Santos, P.3    Magne, J.4    Olivecrona, G.5    Ehrenborg, E.6    Valdivielso, P.7
  • 19
    • 84904184110 scopus 로고    scopus 로고
    • Multimerization of glycosylphosphatidylinositolanchored high density lipoprotein-binding protein 1 (GPIHBP1) and familial chylomicronemia from a serine-to-cysteine substitution in GPIHBP1 Ly6 domain
    • Plengpanich, W., S. G. Young, W. Khovidhunkit, A. Bensadoun, H. Karnman, M. Ploug, H. Gardsvoll, C. S. Leung, O. Adeyo, M. Larsson, et al. 2014. Multimerization of glycosylphosphatidylinositolanchored high density lipoprotein-binding protein 1 (GPIHBP1) and familial chylomicronemia from a serine-to-cysteine substitution in GPIHBP1 Ly6 domain. J. Biol. Chem. 289: 19491-19499.
    • (2014) J. Biol. Chem. , vol.289 , pp. 19491-19499
    • Plengpanich, W.1    Young, S.G.2    Khovidhunkit, W.3    Bensadoun, A.4    Karnman, H.5    Ploug, M.6    Gardsvoll, H.7    Leung, C.S.8    Adeyo, O.9    Larsson, M.10
  • 24
    • 84958559658 scopus 로고    scopus 로고
    • The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain
    • Mysling, S., K. K. Kristensen, M. Larsson, A. P. Beigneux, H. Gardsvoll, L. G. Fong, A. Bensadouen, T. J. Jorgensen, S. G. Young, and M. Ploug. 2016. The acidic domain of the endothelial membrane protein GPIHBP1 stabilizes lipoprotein lipase activity by preventing unfolding of its catalytic domain. eLife. 5: e12095.
    • (2016) ELife , vol.5 , pp. e12095
    • Mysling, S.1    Kristensen, K.K.2    Larsson, M.3    Beigneux, A.P.4    Gardsvoll, H.5    Fong, L.G.6    Bensadouen, A.7    Jorgensen, T.J.8    Young, S.G.9    Ploug, M.10
  • 26
    • 33744932475 scopus 로고    scopus 로고
    • Interaction of lipoprotein lipase and receptor-associated protein
    • Page, S., A. Judson, K. Melford, and A. Bensadoun. 2006. Interaction of lipoprotein lipase and receptor-associated protein. J. Biol. Chem. 281: 13931-13938.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13931-13938
    • Page, S.1    Judson, A.2    Melford, K.3    Bensadoun, A.4
  • 27
    • 84924203151 scopus 로고    scopus 로고
    • GPIHBP1 missense mutations often cause multimerization of GPIHBP1 and thereby prevent lipoprotein lipase binding
    • Beigneux, A. P., L. G. Fong, A. Bensadoun, B. S. Davies, M. Oberer, H. Gardsvoll, M. Ploug, and S. G. Young. 2015. GPIHBP1 missense mutations often cause multimerization of GPIHBP1 and thereby prevent lipoprotein lipase binding. Circ. Res. 116: 624-632.
    • (2015) Circ. Res. , vol.116 , pp. 624-632
    • Beigneux, A.P.1    Fong, L.G.2    Bensadoun, A.3    Davies, B.S.4    Oberer, M.5    Gardsvoll, H.6    Ploug, M.7    Young, S.G.8
  • 29
    • 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., L. V. Hansen, T. J. Jørgensen, and M. Ploug. 2007. A new tagging system for production of recombinant proteins in Drosophila S2 cells using the third domain of the urokinase receptor. Protein Expr. Purif. 52: 384-394.
    • (2007) Protein Expr. Purif. , vol.52 , pp. 384-394
    • Gårdsvoll, H.1    Hansen, L.V.2    Jørgensen, T.J.3    Ploug, M.4
  • 30
    • 0037155921 scopus 로고    scopus 로고
    • Maturation of lipoprotein lipase in the endoplasmic reticulum. Concurrent formation of functional dimers and inactive aggregates
    • Ben-Zeev, O., H. Z. Mao, and M. H. Doolittle. 2002. Maturation of lipoprotein lipase in the endoplasmic reticulum. Concurrent formation of functional dimers and inactive aggregates. J. Biol. Chem. 277: 10727-10738.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10727-10738
    • Ben-Zeev, O.1    Mao, H.Z.2    Doolittle, M.H.3
  • 31
    • 79960110847 scopus 로고    scopus 로고
    • Differential effects of murine and human factor X on adenovirus transduction via cell-surface heparan sulfate
    • Zaiss, A. K., R. Lawrence, D. Elashoff, J. D. Esko, and H. R. Herschman. 2011. Differential effects of murine and human factor X on adenovirus transduction via cell-surface heparan sulfate. J. Biol. Chem. 286: 24535-24543.
    • (2011) J. Biol. Chem. , vol.286 , pp. 24535-24543
    • Zaiss, A.K.1    Lawrence, R.2    Elashoff, D.3    Esko, J.D.4    Herschman, H.R.5
  • 32
    • 0001021338 scopus 로고
    • Assay of lipoprotein lipase and hepatic lipase
    • R. E. Skinner and C. A. Converse Oxford University Press, Oxford, UK
    • Bengtsson-Olivecrona, G., and T. Olivecrona. 1992. Assay of lipoprotein lipase and hepatic lipase. In Lipoprotein Analysis: A Practical Approach. R. E. Skinner and C. A. Converse, editors. Oxford University Press, Oxford, UK. 169-185.
    • (1992) Lipoprotein Analysis: A Practical Approach , pp. 169-185
    • Bengtsson-Olivecrona, G.1    Olivecrona, T.2
  • 33
    • 71049179343 scopus 로고    scopus 로고
    • Highly conserved cysteines within the Ly6 domain of GPIHBP1 are crucial for the binding of lipoprotein lipase
    • Beigneux, A. P., P. Gin, B. S. J. Davies, M. M. Weinstein, A. Bensadoun, L. G. Fong, and S. G. Young. 2009. Highly conserved cysteines within the Ly6 domain of GPIHBP1 are crucial for the binding of lipoprotein lipase. J. Biol. Chem. 284: 30240-30247.
    • (2009) J. Biol. Chem. , vol.284 , pp. 30240-30247
    • Beigneux, A.P.1    Gin, P.2    Davies, B.S.J.3    Weinstein, M.M.4    Bensadoun, A.5    Fong, L.G.6    Young, S.G.7
  • 34
    • 79959256960 scopus 로고    scopus 로고
    • Over-expression of human lipoprotein lipase in mouse mammary glands leads to reduction of milk triglyceride and delayed growth of suckling pups
    • Wang, Y., J. Tong, S. Li, R. Zhang, L. Chen, Y. Wang, M. Zheng, M. Wang, G. Liu, Y. Dai, et al. 2011. Over-expression of human lipoprotein lipase in mouse mammary glands leads to reduction of milk triglyceride and delayed growth of suckling pups. PLoS One. 6: e20895.
    • (2011) PLoS One , vol.6 , pp. e20895
    • Wang, Y.1    Tong, J.2    Li, S.3    Zhang, R.4    Chen, L.5    Wang, Y.6    Zheng, M.7    Wang, M.8    Liu, G.9    Dai, Y.10
  • 35
    • 0026648812 scopus 로고
    • Kinetics of basic fibroblast growth factor binding to its receptor and heparan sulfate proteoglycan: A mechanism for cooperactivity
    • Nugent, M. A., and E. R. Edelman. 1992. Kinetics of basic fibroblast growth factor binding to its receptor and heparan sulfate proteoglycan: a mechanism for cooperactivity. Biochemistry. 31: 8876-8883.
    • (1992) Biochemistry , vol.31 , pp. 8876-8883
    • Nugent, M.A.1    Edelman, E.R.2
  • 36
    • 0029809050 scopus 로고    scopus 로고
    • Interaction of lipoprotein lipase with heparin fragments and with heparan sulfate: Stoichiometry, stabilization, and kinetics
    • Lookene, A., O. Chevreuil, P. Ostergaard, and G. Olivecrona.1996. Interaction of lipoprotein lipase with heparin fragments and with heparan sulfate: stoichiometry, stabilization, and kinetics. Biochemistry. 35: 12155-12163.
    • (1996) Biochemistry , vol.35 , pp. 12155-12163
    • Lookene, A.1    Chevreuil, O.2    Ostergaard, P.3    Olivecrona, G.4
  • 37
    • 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., M. Larsson, O. Kovrov, S. Kasvandik, G. Olivecrona, and A. Lookene. 2015. Evidence for two distinct binding sites for lipoprotein lipase on glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1 (GPIHBP1). J. Biol. Chem. 290: 13919-13934.
    • (2015) J. Biol. Chem. , vol.290 , pp. 13919-13934
    • Reimund, M.1    Larsson, M.2    Kovrov, O.3    Kasvandik, S.4    Olivecrona, G.5    Lookene, A.6
  • 40
    • 84974544966 scopus 로고    scopus 로고
    • Angiopoietin-like 4 promotes intracellular degradation of lipoprotein lipase in adipocytes
    • Dijk, W., A. P. Beigneux, M. Larsson, A. Bensadoun, S. G. Young, and S. Kersten. 2016. Angiopoietin-like 4 promotes intracellular degradation of lipoprotein lipase in adipocytes. J. Lipid Res. 57: 1670-1683.
    • (2016) J. Lipid Res. , vol.57 , pp. 1670-1683
    • Dijk, W.1    Beigneux, A.P.2    Larsson, M.3    Bensadoun, A.4    Young, S.G.5    Kersten, S.6
  • 41
    • 84940056597 scopus 로고    scopus 로고
    • A two-channel detection method for autofluorescence correction and efficient on-bead screening of one-bead one-compound combinatorial libraries using the COPAS fluorescence activated bead sorting system
    • Hintersteiner, M., and M. Auer. 2013. A two-channel detection method for autofluorescence correction and efficient on-bead screening of one-bead one-compound combinatorial libraries using the COPAS fluorescence activated bead sorting system. Methods Appl. Fluoresc. 1: 017001.
    • (2013) Methods Appl. Fluoresc. , vol.1 , pp. 017001
    • Hintersteiner, M.1    Auer, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.