Binding of α1-acid glycoprotein to membrane results in a unique structural change and ligand release

Biochemistry

Volumn 43, Issue 32, 2004, Pages 10513-10519

  Nishi, Koji ^a   Maruyama, Toru ^a   Halsall, H Brian ^b   Handa, Tetsuro ^c   Otagiri, Masaki ^a  

^a KUMAMOTO UNIVERSITY   (Japan)

^b UNIVERSITY OF CINCINNATI   (United States)

^c KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; DRUG PRODUCTS; ELECTROSTATICS; HORMONES; LIPIDS; PROTEINS;

ANIONIC LIPIDS; HELICAL CONFORMATION;

BIOCHEMISTRY;

AMINO ACID; ANION; CARBOHYDRATE; LIGAND; LIPID; LIPOSOME; OROSOMUCOID; PROGESTERONE; SODIUM CHLORIDE; STEROID HORMONE; ACID;

ACIDITY; ALPHA HELIX; ARTICLE; CHEMICAL INTERACTION; ELECTRICITY; LIGAND BINDING; MEMBRANE BINDING; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; BINDING SITE; CELL MEMBRANE; CHEMISTRY; CIRCULAR DICHROISM; LIPID METABOLISM; METABOLISM;

ACIDS; BINDING SITES; CELL MEMBRANE; CIRCULAR DICHROISM; ELECTROSTATICS; HYDROGEN-ION CONCENTRATION; LIGANDS; LIPID METABOLISM; LIPIDS; LIPOSOMES; OROSOMUCOID; PROGESTERONE; PROTEIN BINDING; PROTEIN CONFORMATION; SODIUM CHLORIDE;

EID: 4043117594     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0400204     Document Type: Article

References (46)

1. Halsall, H. B., Austin, R. C., Dage, J. L., Sun, H., and Schlueter, K. T. (2000) Structural aspects of alpha1-acid glycoprotein and its interaction, in Proceedings of the international symposium on serum albumin and alpha1-acid glycoprotein (Otagiri, M., Sugiyama, Y., Testa, B., and Tillement, J. P., Eds.) pp 45-54, Tokyo Print, Kumamoto, Japan.
2. Kremer, J. M., Wilting, J., and Janssen, L. H. (1988) Drug binding to human alphal-acid glycoprotein in health and disease, Pharmacol. Rev. 40, 1-47.
3. Treuheit, M. J., Costello, C. E., and Halsall, H. B. (1992) Analysis of the five glycosylation sites of human alpha1-acid glycoprotein, Biochem. J. 283, 105-112.
4. Clark, A. J., Clissold, P. M., Al Shawi, R., Beattie, P., and Bishop, J. (1984) Structure of mouse major urinary protein genes: different splicing configurations in the 3′-non-coding region, EMBO J. 3, 1045-1052.
5. Baumann, P., Muller, W. E., Eap, C. B., and Tillement, J. P. (1989) Alpha1-acid glycoprotein. Genetics, biochemistry, physiological junctions and pharmacology, Alan R. Liss, New York.
6. Aubert, J. P., and Loucheux-Lefebvre, M. H. (1976) Carbohydrate-peptide linkage in glycoproteins, Arch. Biochem. Biophys. 175, 400-409.
7. Rojo-Dominguez, A., and Hernandez-Arana, A. (1993) Three-dimensional modeling of the protein moiety of human alpha1-acid glycoprotein, a lipocalin-family member, Protein Sequences Data Anal. 5, 349-355.
8. Lin, T. H., Sawada, Y., Sugiyama, Y., Iga, T., and Hanano, M. (1987) Effects of albumin and alpha1-acid glycoprotein on the transport of imipramine and desipramine through the blood-brain barrier in rats, Chem. Pharm. Bull. 35, 294-301.
9. Weisiger, R., Gollan, J., and Ockner, R. (1981) Receptor for albumin on the liver cell surface may mediate uptake of fatty acids and other albumin-bound substances, Science 211, 1048-1051.
10. Forker, E. L., and Luxon, B. A. (1981) Albumin helps mediate removal of taurocholate by rat liver, J. Clin. Invest. 67, 1517-1522.
11. Forker, E. L., and Luxon, B. A. (1983) Albumin-mediated transport of rose bengal by perfused rat liver. Kinetics of the reaction at the cell surface, J. Clin. Invest. 72, 1764-1771.
12. Horie, T., Mizuma, T., Kasai, S., and Awazu, S. (1988) Conformational change in plasma albumin due to interaction with isolated rat hepatocyte, Am. J. Physiol. 254, G465-G470.
13. Predescu, D., Predescu, S., McQuistan, T., and Palade, G. E. (1998) Transcytosis of alpha1-acidic glycoprotein in the continuous microvascular endothelium, Proc. Natl. Acad. Sci. U.S.A. 95, 6175-6180.
14. Andersen, M. M. (1983) Leucocyte-associated plasma proteins. Association of prealbumin, albumin, orosomucoid, alpha1-antitrypsin, transferrin and haptoglobin with human lymphocytes, monocytes, granulocytes and a promyelocytic leukaemic cell line (HL-60), Scand. J. Clin. Lab. Invest. 43, 49-59.
15. Andersen, M. M. (1984) Leucocyte-associated plasma proteins in leucocytes during disease states, and in leukaemic cells, Scand. J. Clin. Lab. Invest. 44, 257-265.
16. Cheresh, D. A., Haynes, D. H., and Distasio, J. A. (1984) Interaction of an acute phase reactant, alpha1-acid glycoprotein (orosomucoid), with the lymphoid cell surface: a model for non-specific immune suppression, Immunology 51, 541-548.
17. Neitchev, V. Z., and Bideaud, F. A. (1988) Temperature-dependent osmotic permeability in glycoprotein containing liposomes, Mol. Biol. Rep. 13, 85-88.
18. Drickamer, K. (1987) Membrane receptors that mediate glycoprotein endocytosis: structure and biosynthesis, Kidney Int., Suppl. 23, 167-183.
19. Nishi, K., Sakai, N., Komine, Y., Maruyama, T., Halsall, H. B., and Otagiri, M. (2002) Structural and drug-binding properties of alphal-acid glycoprotein in reverse micelles, Biochim. Biophys. Acta 1601, 185-191.
20. van der Goot, F. G., Gonzalez-Manas, J. M., Lakey, J. H., and Pattus, F. (1991) A "molten-globule" membrane-insertion intermediate of the pore-forming domain of colicin A, Nature 354, 408-410.
21. Jeffrey, P. D., Bewley, M. C., MacGillivray, R. T., Mason, A. B., Woodworth, R. C., and Baker, E. N. (1998) Ligand-induced conformational change in transferrins: crystal structure of the open form of the N-terminal half-molecule of human transferrin, Biochemistry 37, 13978-13986.
22. Suren, A. T., and Lukas, K. T. (1996) Reversible pH-dependent conformational change of reconstituted influenza hemagglutinin, J. Mol. Biol. 260, 312-316.
23. Bychkova, V. E., Berni, R., Rossi, G. L., Kutyshenko, V. P., and Ptitsyn, O. B. (1992) Retinol-binding protein is in the molten globule state at low pH, Biochemistry 31, 7566-7571.
24. Gasymov, O. K., Abduragimov, A. R., Yusifov, T. N., and Glasgow, B. J. (1998) Structural changes in human tear lipocalins associated with lipid binding, Biochim. Biophys. Acta 1386, 145-156.
25. Essassi, D., Zini, R., and Tillement, J. P. (1990) Use of 1-anilino-8-naphthalene sulfonate as a fluorescent probe in the investigation of drug interactions with human alpha 1-acid glycoprotein and serum albumin, J. Pharm. Sci. 79, 9-13.
26. Bruser, C. A., Signal, C. T., Resh, M. D., and McLaughlin, S. (1994) Membrane binding of myristylated peptides corresponding to the NH2 terminus of Src, Biochemistry 33, 13093-13101.
27. Muzammil, S., Kumar, Y., and Tayyab, S. (1999) Molten globule-like state of human serum albumin at low pH, Eur. J. Biochem. 266, 26-32.
28. Matthews, J. M., Norton, R. S., Hammacher, A., and Simpson, R. J. (2000) The single mutation Phe173→Ala induces a molten globule-like state in murine interleukin-6, Biochemistry 39, 1942-1950.
29. McLaughlin, S. (1989) The electrostatic properties of membranes, Annu. Rev. Biophys. Biophys. Chem. 18, 113-136.
30. Friedman, M. L., Wermeling, J. R., and Halsall, H. B. (1986) The influence of N-acetylneuraminic acid on the properties of human orosomucoid, Biochem. J. 236, 149-153.
31. Halsall, H. B., Villalobos, A. P., Ivancic, J. S., Bencosme, A. I., and Chung, P. (1989) Monoclonal antibodies against human orosomucoid: tools for the exploration of structure, function and interactions, Prog. Clin. Biol. Res. 300, 67-84.
32. Schlueter, K. T. (1992) Photoaffinity labelling the basic binding site of orosomucoid, Ph.D. Dissertation, University of Cincinnati.
33. Kemmink, J., and Creighton, T. E. (1993) Local conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor and their roles in folding, J. Mol. Biol. 234, 861-878.
34. Ptitsyn, O. B. (1995) Molten globule and protein folding, Adv. Protein Chem. 47, 83-229.
35. London, E. (1992) Diphtheria toxin: membrane interaction and membrane translocation, Biochim. Biophys. Acta 1113, 25-51.
36. Gray, R. A., Vander Velde, D. G., Burke, C. J., Manning, M. C., Middaugh, C. R., and Borchardt, R. T. (1994) Delta-sleep-inducing peptide: solution conformational studies of a membrane-permeable peptide, Biochemistry 33, 1323-1331.
37. Jongh, H. H., Killian, J. A., and Kruijff, B. (1992) A water-lipid interface induces a highly dynamic folded state in apocytochrome c and cytochrome c, which may represent a common folding intermediate, Biochemistry 31, 1636-1643.
38. Banuelos, S., and Muga, A. (1995) Binding of molten globule-like conformations to lipid bilayers. Structure of native and partially folded alpha-lactalbumin bound to model membranes, J. Biol. Chem. 270, 29910-29915.
39. Hamada, D., Segawa, S., and Goto, Y. (1996) Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein, Nat. Struct. Biol. 3, 868-873.
40. Mottonen, J., Strand, A., Symersky, J., Sweet, R. M., Danley, D. E., Geoghegan, K. F., Gerard, R. D., and Goldsmith, E. J. (1992) Structural basis of latency in plasminogen activator inhibitor-1, Nature 355, 270-273.
41. Berkenpas, M. B., Lawrence, D. A., and Ginsburg, D. (1995) Molecular evolution of plasminogen activator inhibitor-1 functional stability, EMBO J. 14, 2969-2977.
42. Boncela, J., Papiewska, I., Fijalkowska, I., Walkowiak, B., and Cierniewski, C. S. (2001) Acute phase protein alpha1-acid glycoprotein interacts with plasminogen activator inhibitor type 1 and stabilizes its inhibitory activity, J. Biol. Chem. 276, 35305-35311.
43. Prusiner, S. B. (1989) Scrapie prions, Annu. Rev. Microbiol. 43, 345-374.
44. Morillas, M., Swietnicki, W., Gambetti, P., and Surewicz, W. K. (1999) Membrane environment alters the conformational structure of the recombinant human prion protein, J. Biol. Chem. 274, 36859-36865.
45. Turk, B. E., Jiang, H., and Liu, J. O. (1996) Binding of thalidomide to alpha1-acid glycoprotein may be involved in its inhibition of tumor necrosis factor alpha production, Proc. Natl. Acad. Sci. U.S.A. 93, 7552-7556.
46. Bennett, M., and Schmid, K. (1980) Immunosuppression by human plasma alpha1-acid glycoprotein: importance of the carbohydrate moiety, Proc. Natl. Acad. Sci. U.S.A. 77, 6109-6113.