Relationship between structure and biochemical phenotype of lecithin:cholesterol acyltransferase (LCAT) mutants causing fish-eye disease

Journal of Lipid Research

Volumn 41, Issue 5, 2000, Pages 752-761

  Vanloo, Berlinda ^a   Peelman, Frank ^a   Deschuymere, Kristof ^a   Taveirne, Josee ^a   Verhee, Annick ^b   Gouyette, Catherine ^c   Labeur, Christine ^a   Vandekerckhove, Joël ^b   Tavernier, Jan ^b   Rosseneu, Maryvonne ^a  

^a GHENT UNIVERSITY   (Belgium)

^b DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^c INSTITUT PASTEUR   (France)

Author keywords

Acyltransferase; Apolipoprotein A I; Cholesterol; Enzyme lipase; Esterase; HDL; LDL; Phospholipase A2; Phospholipid

Indexed keywords

HIGH DENSITY LIPOPROTEIN; LOW DENSITY LIPOPROTEIN; MUTANT PROTEIN; PHOSPHATIDYLCHOLINE STEROL ACYLTRANSFERASE; PHOSPHOLIPASE A2;

ALPHA HELIX; ARTICLE; ENZYME ACTIVITY; HYDROPHILICITY; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN LIPID INTERACTION; SITE DIRECTED MUTAGENESIS; STRUCTURE ACTIVITY RELATION;

ANIMALS; CORNEAL OPACITY; COS CELLS; ENZYME ACTIVATION; ESTERASES; HUMANS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PHENOTYPE; PHOSPHATIDYLCHOLINE-STEROL O-ACYLTRANSFERASE; PHOSPHOLIPASES A; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS;

EID: 0034122723     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (39)

1. McLean, J., C. Fielding, D. Drayna, H. Dieplinger, B. Baer, W. Kohr, W. Henzel, and R. Lawn. 1986. Cloning and expression of human lecithin-cholesterol acyltransferase cDNA. Proc. Natl. Acad. Sci. USA. 83: 2335-2339.
2. Glomset, J. A. 1968. The plasma lecithin:cholesterol acyltransferase reaction. J. Lipid Res. 9: 155-167.
3. Jonas, A. 1998. Regulation of lecithin:cholesterol acyltransferase activity. Prog. Lipid Res. 37: 209-234.
4. Peelman, F., N. Vinaimont, A. Verhee, B. Vanloo, J. L. Verschelde, C. Labeur, M. S. Seguret, N. Duverger, G. Hutchinson, J. Vandekerckhove, J. Tavernier, and M. Rosseneu. 1998. A proposed architecture for lecithin cholesterol acyl transferase (LCAT): identification of the catalytic triad and molecular modeling. Protein Sci. 7: 587-599.
5. Francone, O. L., and C. J. Fielding. 1991. Structure-function relationships in human lecithin:cholesterol acyltransferase. Site-directed mutagenesis at serine residues 181 and 216. Biochemistry. 30: 10074-10077.
6. Adimoolam, S., Y. P. Lee, and A. Jonas. 1998. Mutagenesis of highly conserved histidines in lecithin cholesterol acyltransferase: identification of an essential histidine (His 377). Biochem. Biophys. Res. Commun. 243: 337-341.
7. Peelman, F., B. Vanloo, O. Perez-Mendez, A. Decout, J. L. Verschelde, C. Labeur, N. Vinaimont, A. Verhee, N. Duverger, R. Brasseur, J. Vandekerckhove, J. Tavernier, and M. Rosseneu. 1999. Characterization of functional residues in the interfacial recognition domain of lecithin cholesterol acyltransferase (LCAT). Protein Eng. 12: 71-78.
8. Adimoolam, S., and A. Jonas. 1997. Identification of a domain of lecithin-cholesterol acyltransferase that is involved in interfacial recognition. Biochem. Biophys. Res. Commun. 232: 783-787.
9. Kuivenhoven, J. A., H. Pritchard, J. Hill, J. Frohlich, G. Assmann, and J. Kastelein. 1997. The molecular pathology of lecithin:cholesterol acyltransferase (LCAT) deficiency syndromes. J. Lipid Res. 38: 191-205.
10. Carlson, L. A. 1979. A further case of fish-eye disease. Lancet. 2: 1376-1377.
11. Carlson, L. A., and L. Holmquist. 1985. Evidence for the presence in human plasma of lecithin:cholesterol acyltransferase activity (beta-LCAT) specifically esterifying free cholesterol of combined pre-beta- and beta-lipoproteins. Studies of fish eye disease patients and control subjects. Acta Med. Scand. 218: 197-205.
12. Bonelli, F. S., and A. Jonas. 1992. Continuous fluorescence assay for lecithin:cholesterol acyltransferase using a water-soluble phosphatidylcholine. J. Lipid Res. 33: 1863-1869.
13. Yamazaki, S., T. Mitsunaga, Y. Furukawa, and T. Nishida. 1983. Interaction of lecithin-cholesterol acyltransferase with human plasma lipoproteins and with lecithin-cholesterol vesicles. J. Biol. Chem. 258: 5847-5853.
14. Jonas, A. 1986. Synthetic substrates of lecithin:cholesterol acyltransferase. J. Lipid Res. 27: 689-698.
15. Bonelli, F. S., K. E. Kezdy, and A. Jonas. 1987. A continuous fluorescence assay for lecithin cholesterol acyltransferase. Anal. Biochem. 166: 204-207.
16. Sparks, D. L., and P. H. Pritchard. 1989. The neutral lipid composition and size of recombinant high density lipoproteins regulates lecithin:cholesterol acyltransferase activity. Biochem. Cell Biol. 67: 358-364.
17. Pownall, H. J., Q. Pao, and J. B. Massey. 1985. Acyl chain and head-group specificity of human plasma lecithin:cholesterol acyltransferase. Separation of matrix and molecular specificities. J. Biol. Chem. 260: 2146-2152.
18. Vanloo, B., J. Morrison, N. Fidge, G. Lorent, L. Lins, R. Brasseur, J. M. Ruysschaert, J. Baert, and M. Rosseneu. 1991. Characterization of the discoidal complexes formed between apoA-I-CNBr fragments and phosphatidylcholine. J. Lipid Res. 32: 1253-1264.
19. Peelman, F., J. L. Verschelde, B. Vanloo, C. Ampe, C. Labeur, J. Tavernier, J. Vandekerckhove, and M. Rosseneu. 1999. Effects of natural mutations in lecithin:cholesterol acyltransferase on the enzyme structure and activity. J. Lipid Res. 40: 59-69.
20. 2 with pyrene-labeled lecithin as a substrate. Anal. Biochem. 116: 553-558.
21. Egloff, M. P., F. Marguet, G. Buono, R. Verger, C. Cambillau, and H. van Tilbeurgh. 1995. The 2.46 A resolution structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate. Biochemistry. 34: 2751-2762.
22. Seguret, M. S., M. M. Latta, G. Castro, G. Luc, J. C. Fruchart, E. Rubin, P. Denefle, and N. Duverger. 1996. Potential gene therapy for lecithin-cholesterol acyltransferase (LCAT)-deficient and hypoalphalipoproteinemic patients with adenovirus-mediated transfer of human LCAT gene. Circulation. 94: 2177-2184.
23. Matz, C. E., and A. Jonas. 1982. Micellar complexes of human apolipoprotein A-I with phosphatidylcholines and cholesterol prepared from cholate-lipid dispersions. J. Biol. Chem. 257: 4535-4540.
24. Vanloo, B., J. Taveirne, J. Baert, G. Lorent, L. Lins, J. M. Ruyschaert, and M. Rosseneu. 1992. LCAT activation properties of apo A-I CNBr fragments and conversion of discoidal complexes into spherical particles. Biochim. Biophys. Acta. 1128: 258-266.
25. 2 activities. Methods Mol. Biol. 109: 123-131.
26. Corijn, J., R. Deleys, C. Labeur, B. Vanloo, L. Lins, R. Brasseur, J. Baert, J. M. Ruysschaert, and M. Rosseneu. 1993. Synthetic model peptides for apolipoproteins. II. Characterization of the discoidal complexes generated between phospholipids and synthetic model peptides for apolipoproteins. Biochem. Biophys. Acta. 1170: 8-16.
27. Matz, C. F., and A. Jonas. 1982. Reaction of human lecithin cholesterol acyltransferase with synthetic micellar complexes of apolipoprotein A-I, phosphatidylcholine, and cholesterol. J. Biol. Chem. 257: 4541-4546.
28. 2 and acyltransferase activities characteristic of high density lipoprotein lecithin:cholesterol acyltransferase in fish eye disease. Acta Med. Scand. 222: 23-26.
29. Klein, H. G., N. Duverger, J. J. Albers, S. Marcovina, H. B. Brewer, Jr., and S. Santamarina-Fojo. 1995. In vitro expression of structural defects in the lecithin-cholesterol acyltransferase gene. J. Biol. Chem. 270: 9443-9447.
30. Adimoolam, S., L. Jin, E. Grabbe, J. J. Shieh, and A. Jonas. 1998. Structural and functional properties of two mutants of lecithin-cholesterol acyltransferase (T123I and N228K). J. Biol. Chem. 273: 32561-32567.
31. Czarnecka, H., and S. Yokoyama. 1993. Regulation of lecithin-cholesterol acyltransferase reaction by acyl acceptors and demonstration of its "idling" reaction. J. Biol. Chem. 268: 19334-19340.
32. Funke, H., A. von Eckardstein, P. H. Pritchard, J. J. Albers, J. J. Kastelein, C. Droste, and G. Assmann. 1991. A molecular defect causing fish eye disease: an amino acid exchange in lecithin-cholesterol acyltransferase (LCAT) leads to the selective loss of alpha-LCAT activity. Proc. Natl. Acad. Sci. USA. 88: 4855-4859.
33. Kuivenhoven, J. A., E. van-Voorst-tot-Voorst, H. Wiebusch, S. M. Marcovina, H. Funke, G. Assmann, P. H. Pritchard, and J. J. Kastelein. 1995. A unique genetic and biochemical presentation of fish-eye disease. J. Clin. Invest. 96: 2783-2791.
34. Hill, J. 1994. The molecular pathology of lecithin:cholesterol acyltransferase deficiency. Ph.D Thesis.
35. 2-like activity by sn-2-difluoroketone phosphatidylcholine analogues. J. Biol. Chem. 264: 1963-1967.
36. Zhou, G. Y., M. Jauhiainen, K. Stevenson, and P. J. Dolphin. 1991. Human plasma lecithin:cholesterol acyltransferase. Preparation and use of immobilized p-aminophenylarsenoxide as a catalytic site-directed covalent ligand in enzyme purification. J. Chromatogr. 568: 69-83.
37. Wang, X., C. S. Wang, J. Tang, F. Dyda, and X. C. Zhang. 1997. The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism. Structure. 5: 1209-1218.
38. Dhoest, A., Z. Zhao, B. De Geest, E. Deridder, A. Sillen, Y. Engelborghs, D. Collen, and P. Holvoet. 1997. Role of the Arg123-Tyr166 paired helix of apolipoprotein A-I in lecithin:cholesterol acyltransferase activation. J. Biol. Chem. 272: 15967-15972.
39. Sorci-Thomas, M. G., L. Curtiss, J. S. Parks, M. J. Thomas, M. W. Kearns, and M. Landrum. 1998. The hydrophobic face orientation of apolipoprotein A-I amphipathic helix domain 143-164 regulates lecithin:cholesterol acyltransferase activation. J. Biol. Chem. 273: 11776-11782.