Identification of domains in apoA-I susceptible to proteolysis by mast cell chymase: Implications for HDL function

Journal of Lipid Research

Volumn 41, Issue 6, 2000, Pages 975-984

  Lee, Miriam ^a,b   Uboldi, Patrizia ^c   Giudice, Daniela ^c   Catapano, Alberico L ^c   Kovanen, Petri T ^a  

^a WIHURI RESEARCH INSTITUTE   (Finland)

^b UNIVERSITY OF HAVANA   (Cuba)

^c NONE

Author keywords

and pre migrating HDL; Cellular cholesterol efflux; LCAT; Monoclonal antibodies; Proteolysis of apoA 1

Indexed keywords

APOLIPOPROTEIN A1; CHOLESTEROL; CHYMASE; HIGH DENSITY LIPOPROTEIN; PHOSPHATIDYLCHOLINE STEROL ACYLTRANSFERASE;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BINDING AFFINITY; CHOLESTEROL TRANSPORT; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME MECHANISM; FEMALE; MALE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; RAT;

ANIMALS; ANTIBODIES, MONOCLONAL; APOLIPOPROTEIN A-I; CHOLESTEROL; CHYMASES; ENZYME ACTIVATION; ENZYME-LINKED IMMUNOSORBENT ASSAY; FEMALE; FOAM CELLS; HYDROLYSIS; LIPOPROTEINS, HDL; MALE; MAST CELLS; MICE; PHOSPHATIDYLCHOLINE-STEROL O-ACYLTRANSFERASE; RATS; RATS, WISTAR; SERINE ENDOPEPTIDASES;

EID: 0033920542     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (48)

1. Barter, P. J., and K-A. Rye. 1996. High density lipoproteins and coronary heart disease. Atherosclerosis. 121: 1-12.
2. Fielding, C. F., and P. E. Fielding. 1995. Molecular physiology of reverse cholesterol transport. J. Lipid. Res. 36: 211-228.
3. von Eckardstein, A., A. Y. Huang, and G. Assman. 1994. Physiological role and clinical relevance of high-density lipoprotein subclasses. Curr. Opin. Lipidol. 5: 404-416.
4. Castro, G. R., and C. J. Fielding. 1988. Early incorporation of cell-derived cholesterol into pre-β-migrating high density lipoprotein. Biochemistry. 27: 25-29.
5. Lee, M., L. Lindstedt, and P. T. Kovanen. 1992. Mast cell-mediated inhibition of reverse cholesterol transport. Arterioscl. Thromb. Vasc. Biol. 12: 1329-1335.
6. Lindstedt, L., M. Lee, G. R. Castro, J-C. Fruchart, and P. T. Kovanen. 1996. Chymase in exocylosed rat mast cell granules effectively proteolyzes apolipoprotein Al-containing lipoproteins, so reducing the cholesterol efflux-inducing ability of serum and aortic intimal fluid. J. Clin. Invest. 97: 2174-2182.
7. 1LpA-I and LpA-IV by mast cell chymase reduces the cholesterol efflux ability promoted by plasma. Arterioscler. Thromb. Vasc. Biol. 19: 1066-1074.
8. Brouillette, C. G., and G. M. Anantharamaiah. 1995. Structural models of apolipoprotein A-I. Biochim. Biophys. Acta. 1256: 103-129.
9. Palgunachari, M. N., V. K. Mishra, S. Lund-Katz, M. C. Phillips, S. O. Adeyeye, N. Alluri, G. M. Anantharamaiah, and J. P. Segrest, 1996. Only the two end helixes of eight tandem amphipathic helical domains of human apoA-I have significant lipid affinity. Implications for HDL assembly. Arterioscler. Thromb. Vasc. Biol. 16: 328-338.
10. Allan, C. M., N. H. Fidge, J. R. Morrison, and J. Kanellos. 1993. Monoclonal antibodies to human apolipoprotein AI: probing the putative receptor binding domain of apolipoprotein AI. Biochem. J. 290: 449-455.
11. Dalton, M. B., and J. B. Swaney. 1993. Structural domains of apolipoprotein A-I within high density lipoproteins. J. Biol. Chem. 268; 19274-19283.
12. Luchoomun, J., N. Theret, V. Clavey, P. Duchateau, M. Rosseneu, R. Brasseur, P. Denefle, J-C. Fruchart, and G. R. Castro. 1994. Structural domain of apolipoprotein A-I involved in its interaction with cells. Biochim. Biophys. Acta. 1212: 319-326.
13. Davidson, W. S., S. Lund-Katz, W. J. Johnson, G. M. Anantharamaiah, M. N. Palgunachari, J. P. Segrest, G. H. Rothblat, and M. C. Phillips. 1994. The influence of apolipoprotein structure on the efflux of cellular free cholesterol to high density lipoprotein. J. Biol. Chem. 269: 22975-22982.
14. Banka, C. L., A. S. Black, and L. K. Curtiss. 1994. Localization of an apolipoprotein A-I epitope critical for lipoprotein-mediated cholesterol efflux from monocytic cells. J. Biol. Chem. 269: 10288-10297.
15. Fielding, P. E., M. Kawano, A. L. Catapano, A. Zoppo, S. Marcovina, and C. J. Fielding. 1994. Unique epitope of apolipoprotein A-I expressed in pre-β-1 high density lipoprotein and its role in the catalyzed efflux of cellular cholesterol. Biochemistry. 33: 6981-6985.
16. Sviridov, D., L. Pyle, and N. Fidge. 1996. Identification of a sequence of apolipoprotein A-I associated with the efflux of intracellular cholesterol to human serum and apolipoprotein A-I containing particles. Biochemistry. 35: 189-196.
17. Banka, C. L., D. J. Bonnet, A. S. Black, R. S. Smith, and L. K. Curtiss. 1991. Localization of an apolipoprotein A-I epitope critical for activation of lecithin-cholesterol acyltransferase. J. Biol. Chem. 266: 23886-23892.
18. Wong, L., L. K. Curtiss, J. Huang, C. J. Mann, B. Maldonado, and P. S. Roheim. 1992. Altered epitope expression of human interstitial fluid apolipoprotein A-I reduces its ability to activate lecithin cholesterol acyl transferase. J. Clin. Invest. 90: 2370-2375.
19. Minnich, A., X. Collet, A. Roghani, C. Cladaras, R. L. Hamilton, C. J. Fielding, and V. I. Zannis. 1992. Site-directed mutagenesis and structure-function analysis of the human apolipoprotein A-I. J. Biol. Chem. 267: 16553-16560.
20. Meng, Q-H., L. Calabresi, J-C. Fruchart, and Y. L. Fruchart. 1993. Apolipoprotein A-I domains involved in the activation of lecithin:cholesterol acyltransferase. J. Biol. Chem. 268: 16966-16973.
21. Sorci-Thomas, M., M. W. Kearns, and J. P. Lee. 1993. Apolipoprotein A-I domains involved in lecithin-cholesterol acyltransferase activation. Structure:function relationships. J. Biol. Chem. 268; 21403-21409.
22. Uboldi, P., M. Spoladore, S. Fantappie, S. Marcovina, and A. L. Catapano. 1996. Localization of apolipoprotein A-I epitopes involved in the activation of lecithin:cholesterol acyltransferase. J. Lipid Res. 37: 2557-2568.
23. Lindstedt, K. A., J. O. Kokkonen, and P. T. Kovanen. 1992. Soluble heparin proteoglycans released from stimulated mast cells induce uptake of low density lipoproteins by macrophages via scavenger receptor-mediated phagocytosis. J Lipid Res. 33: 65-75.
24. Lowry, O. H., N. J. Rosebrough, A. L. Farr, and R. J. Randall. 1951. Protein measurement with Folin phenol reagent. J. Biol. Chem. 193: 265-275.
25. Woodbury, R. G., M. T. Everitt, and H. Neurath. 1981. Mast cell proteases. Methods Enzymol. 80: 588-609.
26. Kokkonen, J. O., M. Vartiainen, and P. T. Kovanen. 1986. Low density lipoprotein degradation by secretory granules of rat mast cells. J. Biol. Chem. 261: 16067-16072.
27. Havel, R. J., H. A. Eder, and J. H. Bragdon. 1955. The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum. J. Clin. Invest. 34: 1345-1353.
28. Lindstedt, L., J. Saarinen, N. Kalkkinen, H. Welgus, and P. T. Kovanen. 1999. Matrix metalloproteinases -3, -7, and -12, but not -9, reduce high density lipoprotein-induced cholesterol efflux from human macrophage foam cells by truncation of the carboxyl terminus of apolipoprotein AI. J. Biol. Chem. 274: 22627-22634.
29. Basu, S. K., Goldstein J. L., Anderson R. G. W., and Brown M. S. 1976. Degradation of cationized low density lipoprotein and regulation of cholesterol metabolism in homozygous familial hypercholesterolemia fibroblasts. Proc. Natl. Acad. Sci. USA. 73: 3178-3182.
30. Brown, M. S., S. E. Dana, and J. L. Goldstein. 1975. Receptor-dependent hydrolysis of cholesteryl esters contained in plasma low density lipoprotein. Proc. Natl. Acad. Sci. USA. 72: 2925-2929.
31. McFarlane, A. S. 1958. Efficient trace-labeling of proteins with iodine. Nature (London) 182: 53-57.
32. Bilheimer, D. W., S. Eisenberg, and R. I. Levy. 1972. The metabolism of very low density lipoproteins. I. Preliminary in vitro and in vivo observations. Biochim. Biophys. Acta. 260: 212-221.
33. Weber, K., and M. Osborn. 1969. The reliability of molecular weight determination by dodecyl sulfate polyacrylamide gel electrophoresis. J. Biol. Chem. 244: 4406-4412.
34. Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76: 4350-4354.
35. Chen, C-H., and J. J. Alcers. 1985. A rapid large-scale procedure for purification of lecithin-cholesterol acyltransferase from human and animal plasma. Biochim. Biophys. Acta. 834: 188-195.
36. Albers, J. J., C-H. Chen, and A. G. Lacko. 1986. Isolation, characterization, and assay of lecithin cholesterol acyltransferase. Methods Enzymol. 129: 763-783.
37. Clay, M. A., and P. J. Barter. 1996. Formation of new HDL particles from lipid-free apolipoprotein A-I. J. Lipid. Res. 37: 1722-1732.
38. Ji, Y., and A. Jonas, 1995. Properties of an N-terminal proteolytic fragment of apolipoprotein AI in solution and in reconstituted high density lipoproteins. J. Biol. Chem. 270: 11290-11297.
39. Roberts, L. M., M. J. Ray, T-W. Shih, E. Hayden, M. M. Reader, and C. G. Brouillette. 1997. Structural analysis of apolipoprotein A-I: Limited proteolysis of methionine-reduced and -oxidized lipid-free and lipid-bound human apoA-I. Biochemistry. 36: 7615-7624.
40. Kunitake, S. T., G. Ch. Chen, S-F. Kung, J. W. Schilling, D. A. Hardman, and J. P. Kane. 1989. Pro-beta high density lipoprotein. Unique disposition of apolipoprotein A-I increases susceptibility to proteolysis. Arteriosclerosis. 10: 25-30.
41. Fantappie, S., A. Corsini, A. Sidoli, S. Marcovina, P. Uboldi, A. Granala, B. Da Ros, P. Rossi, R. Fumagalli, and A. L. Catapano. 1992. Monoclonal antibodies to human low density lipoprotein identify distinct areas on apolipoprotein B-100 relevant to the LDL-receptor interaction. J. Lipid Res. 33: 1111-1121.
42. Bolin, D. J., and A. Jonas. 1996. Sphingomyclin inhibits the lecithin-cholesterol acyltransferase reaction with reconstituted high density lipoproteins by decreasing enzyme binding. 1996. J. Biol. Chem. 271: 19152-19158.
43. Jonas, A. 1998. Regulation of lecithin cholesterol acyltransferase activity. Prog. Lipid Res. 37: 209-234.
44. Wilson, J. E. 1991. The use of monoclonal antibodies and limited proteolysis in elucidation of structure-function relationships in proteins. Methods Biochem. Anal. 35: 207-250.
45. Vanloo, B., J. Taveirne, J. Baert, G. Lorent, L. Lins, J. M. Ruyschaert, and M. Rosseneu. 1992. LCAT activation properties of apoA-I CNBr fragments and conversion of discoidal complexes into spherical particles. Biochim. Biophys. Acta. 1128: 258-266.
46. Wang, J., J. A. Delozie, A. K. Gevre, P. J. Dolpin, and J. S. Parks. 1998. Role of glutamic acid residues 154, 155, and 165 of lecithinicholesterol acyl transferase in cholesterol esterification and phospholipase A2 activities. J. Lipid Res. 39: 51-58.
47. McCall, M. R., J. J. M. van den Berg, F. A. Kuypers, D. L. Tribble, R. M. Krauss, L. J. Knoff, and T. M. Forte. 1994. Modification of LCAT activity and HDL structure. New links between cigarette smoke and coronary heart disease risk. Arterioscler. Thromb. Vasc. Biol. 14: 248-253.
48. Kaartinen, M., A. Penttilä, and P. T. Kovanen. 1995. Extracellular mast cell granules carry apolipoprotein B-100-containing lipoproteins into phagocytes in human arterial intima. Functional coupling of exocytosis and phagocytosis in neighboring cells. Arterioscler. Thromb. Vasc. Biol. 15: 2047-2054.