Chylomicronemia with low postheparin lipoprotein lipase levels in the setting of GPIHBP1 defects

Circulation: Cardiovascular Genetics

Volumn 3, Issue 2, 2010, Pages 169-178

  Franssen, Remco ^a   Young, Stephen G ^b   Peelman, Frank ^c,d   Hertecant, Jozef ^e   Sierts, Jeroen A ^a   Schimmel, Alinda W M ^a   Bensadoun, André ^f   Kastelein, John J P ^a   Fong, Loren G ^b   Dallinga Thie, Geesje M ^a   Beigneux, Anne P ^b  

^a ACADEMIC MEDICAL CENTER   (Netherlands)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^d GHENT UNIVERSITY   (Belgium)

^e TAWAM HOSPITAL   (United Arab Emirates)

^f Department of Obstetrics Gynecology   (United States)

Author keywords

GPIHBP1; Lipoprotein lipase; Triglycerides

Indexed keywords

BINDING PROTEIN; CYSTEINE; GLUTAMINE; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED HIGH DENSITY LIPOPROTEIN BINDING PROTEIN 1; HEPARIN; LIPOPROTEIN LIPASE; LYMPHOCYTE ANTIGEN; LYMPHOCYTE ANTIGEN 6; PROLINE; TRIACYLGLYCEROL; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CHILD; CHO CELL; CONTROLLED STUDY; DISEASE SEVERITY; DISULFIDE BOND; ENZYME BINDING; ENZYME BLOOD LEVEL; HOMOZYGOSITY; HOMOZYGOTE; HUMAN; HUMAN CELL; HYPERTRIGLYCERIDEMIA; LIPID METABOLISM; MALE; MISSENSE MUTATION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEFECT; PROTEIN DOMAIN; PROTEIN STRUCTURE; TRIACYLGLYCEROL BLOOD LEVEL;

AMINO ACID SUBSTITUTION; ANIMALS; CARRIER PROTEINS; CHILD, PRESCHOOL; CHO CELLS; CHYLOMICRONS; CRICETINAE; CRICETULUS; EXONS; HEPARIN; HOMOZYGOTE; HUMANS; LIPOPROTEIN LIPASE; MALE; MUTATION, MISSENSE; TRIGLYCERIDES;

CRICETULUS GRISEUS; MUS;

EID: 77952575107     PISSN: 1942325X     EISSN: 19423268     Source Type: Journal    
DOI: 10.1161/CIRCGENETICS.109.908905     Document Type: Article

References (28)

1. Wang H, Eckel RH. Lipoprotein lipase: from gene to obesity. Am J Physiol Endocrinol Metab. 2009;297:E271-E288.
2. Williams KJ. Molecular processes that handle-and mishandle-dietary lipids. J Clin Invest. 2008;118:3247-3259.
3. Young SG, Davies BS, Fong LG, Gin P, Weinstein MM, Bensadoun A, Beigneux AP. GPIHBP1: an endothelial cell molecule important for the lipolytic processing of chylomicrons. Curr Opin Lipidol. 2007;18: 389-396.
4. 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 FJ, Ryan RO, Fong LG, Bensadoun A, Young SG. Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons. Cell Metab. 2007;5:279-291.
5. Beigneux AP, Davies BS, Bensadoun A, Fong LG, Young SG. GPIHBP1, a GPI-anchored protein required for the lipolytic processing of triglyceride- rich lipoproteins. J Lipid Res. 2009;50(suppl):S57-S62.
6. Weinstein MM, Yin L, Beigneux AP, Davies BS, Gin P, Estrada K, Melford K, Bishop JR, Esko JD, Dallinga-Thie GM, Fong LG, Bensadoun A, Young SG. Abnormal patterns of lipoprotein lipase release into the plasma in GPIHBP1-deficient mice. J Biol Chem. 2008;283: 34511-34518.
7. Sonnenburg WK, Yu D, Lee EC, Xiong W, Gololobov G, Key B, Gay J, Wilganowski N, Hu Y, Zhao S, Schneider M, Ding ZM, Zambrowicz BP, Landes G, Powell DR, Desai U. Glycosylphosphatidylinositol-anchored HDL-binding protein stabilizes lipoprotein lipase and prevents its inhibition by angiopoietin-like 3 and angiopoietin-like 4. J Lipid Res. 2009; 50:2421-2429.
8. Beigneux AP, Franssen R, Bensadoun A, Gin P, Melford K, Peter J, Walzem RL, Weinstein MM, Davies BS, Kuivenhoven JA, Kastelein JJ, Fong LG, Dallinga-Thie GM, Young SG. Chylomicronemia with a mutant GPIHBP1 (Q115P) that cannot bind lipoprotein lipase. Arterioscler Thromb Vasc Biol. 2009;29:956-962.
9. Levels JH, Marquart JA, Abraham PR, Van den Ende AE, Molhuizen HO, van Deventer SJ, Meijers JC. Lipopolysaccharide is transferred from high-density to low-density lipoproteins by lipopolysaccharide-binding protein and phospholipid transfer protein. Infect Immun. 2005;73: 2321-2326.
10. Kastelein JJP, Jukema JW, Zwinderman AH, Clee S, Van Boven AJ, Jansen H, Rabelink TJ, Peters RJG, Lie KI, Liu G, Bruschke AVG, Hayden MR. Lipoprotein lipase activity is associated with severity of angina pectoris. REGRESS Study Group. Circulation. 2000;102: 1629-1633.
11. Bensadoun A. Sandwich immunoassay for measurement of human hepatic lipase. Methods Enzymol. 1996;263:333-338.
12. Brunzell JD, Porte D Jr, Bierman EL. Abnormal lipoprotein-lipasemediated plasma triglyceride removal in untreated diabetes mellitus associated with hypertriglyceridemia. Metabolism. 1979;28:901-907.
13. Gin P, Beigneux AP, Davies B, Young MF, Ryan RO, Bensadoun A, Fong LG, Young SG. Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to GPIHBP1 containing a G56R amino acid substitution. Biochim Biophys Acta. 2007;1771:1464-1468.
14. Esko JD, Stewart TE, Taylor WH. Animal cell mutants defective in glycosaminoglycan biosynthesis. Proc Natl Acad Sci U S A. 1985;82: 3197-3201.
15. Brunzell JD. Clinical practice. Hypertriglyceridemia. N Engl J Med. 2007;357:1009-1017.
16. Beigneux AP, Gin P, Davies BS, Weinstein MM, Bensadoun A, Fong LG, Young SG. Highly conserved cysteines within the Ly6 domain of GPIHBP1 are crucial for the binding of lipoprotein lipase. J Biol Chem. 2009;284:30240-30247.
17. Olivecrona G, Ehrenborg E, Semb H, Makoveichuk E, Lindberg A, Hayden MR, Gin P, Davies BSJ, Weinstein MM, Fong LG, Beigneux AP, Young SG, Olivecrona T, Hernell O. Mutation of conserved cysteines in the Ly6 domain of GPIHBP1 in familial chylomicronemia. J. Lipid Res. 2009 [Epub ahead of print].
18. Fry BG, Wuster W, Kini RM, Brusic V, Khan A, Venkataraman D, Rooney AP. Molecular evolution and phylogeny of elapid snake venom three-finger toxins. J Mol Evol. 2003;57:110-129.
19. Mallya M, Campbell RD, Aguado B. Characterization of the five novel Ly-6 superfamily members encoded in the MHC, and detection of cells expressing their potential ligands. Protein Sci. 2006;15:2244-2256.
20. Huang Y, Fedarovich A, Tomlinson S, Davies C. Crystal structure of CD59: implications for molecular recognition of the complement proteins C8 and C9 in the membrane-attack complex. Acta Crystallogr D Biol Crystallogr. 2007;63(pt 6):714-721.
21. Kjaergaard M, Hansen LV, Jacobsen B, Gardsvoll H, Ploug M. Structureand ligand interactions of the urokinase receptor (uPAR). Front Biosci. 2008;13:5441-5461.
22. Galat A, Gross G, Drevet P, Sato A, Menez A. Conserved structural determinants in three-fingered protein domains. FEBS J. 2008;275: 3207-3225.
23. Marchler-Bauer A, Anderson JB, Chitsaz F, Derbyshire MK, DeWeese-Scott C, Fong JH, Geer LY, Geer RC, Gonzales NR, Gwadz M, He S, Hurwitz DI, Jackson JD, Ke Z, Lanczycki CJ, Liebert CA, Liu C, Lu F, Lu S, Marchler GH, Mullokandov M, Song JS, Tasneem A, Thanki N, Yamashita RA, Zhang D, Zhang N, Bryant SH. CDD: specific functional annotation with the Conserved Domain Database. Nucleic Acids Res. 2009;37:D205-D210.
24. Eswar N, Eramian D, Webb B, Shen MY, Sali A. Protein structure modeling with MODELLER. Methods Mol Biol. 2008;426:145-159.
25. Fletcher CM, Harrison RA, Lachmann PJ, Neuhaus D. Structure of a soluble, glycosylated form of the human complement regulatory protein CD59. Structure. 1994;2:185-199.
26. Petranka J, Zhao J, Norris J, Tweedy NB, Ware RE, Sims PJ, Rosse WF. Structure-function relationships of the complement regulatory protein, CD59. Blood Cells Mol Dis. 1996;22:281-296.
27. Charfeddine C, Mokni M, Ben MR, Elkares R, Bouchlaka C, Boubaker S, Ghedamsi S, Baccouche D, Ben OA, Dellagi K, Abdelhak S. A novel missense mutation in the gene encoding SLURP-1 in patients with Mal de Meleda from northern Tunisia. Br J Dermatol. 2003;149:1108-1115.
28. Williams KJ. Some things just have to be done in vivo: GPIHBP1, caloric delivery, and the generation of remnant lipoproteins. Arterioscler Thromb Vasc Biol. 2009;29:792-795.