The lifetime of insulin hexamers

Biophysical Journal

Volumn 77, Issue 3, 1999, Pages 1638-1654

  Hassiepen, Ulrich ^a   Federwisch, Matthias ^a   Mülders, Thomas ^a   Wollmer, Axel ^a,b  

^a RWTH AACHEN UNIVERSITY   (Germany)

^b NOVARTIS PHARMA AG   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

INSULIN; PIG INSULIN;

ARTICLE; ENERGY TRANSFER; FLUORESCENCE SPECTROSCOPY; INSULIN TREATMENT; KINETICS; NONHUMAN; SWINE; TEMPERATURE SENSITIVITY;

SUS SCROFA;

EID: 0032817514     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77012-8     Document Type: Article

References (47)

1. Anderson, S., and G. Weber. 1966. The reversible acid dissociation and hybridization of lactic dehydrogenase. Arch. Biochem. Biophys. 116: 207-223.
2. B29-insuIin: dissociation of a protein-ligand complex. Protein Sci. 5:2521-2531.
3. Baker, E. N., T. L. Blundell, J. F. Cutfield, S. M. Cutfield, E. J. Dodson, G. G. Dodson, D. M. Crowfoot Hodgkin, R. E. Hubbard, N. W. Isaacs, C. D. Reynolds, K. Sakabe, N. Sakabe, and N. M. Vijayan. 1988. The structure of 2Zn pig insulin crystals at 1.5 A resolution. Philos. Trans. R. Soc. Land. B. 319:369-456.
4. Bentley, G., E. J. Dodson, G. G. Dodson, D. Hodgkin, and D. A. Mercola. 1976. Structure of insulin in 4-zinc insulin. Nature. 261:166-168.
5. Bentley, G. A., G. G. Dodson, E. J. Dodson, D. C. Hodgkin, D. A. Mercola, and A. Wollmer. 1975. Structural rearrangements in insulin: a comparison of 2 and 4 zinc insulin structures. British Diabetes Association, Medical and Scientific Section, Spring Meeting 1975, Sheffield.
6. Blundell, T. L., G. G. Dodson, D. C. Hodgkin, and D. A. Mercola. 1972. Insulin: the structure in the crystal and its reflection in chemistry and biology. Adv. Protein Chem. 26:279-402.
7. Brange, J. 1994. Stability of Insulin. Kluwer Academic Publishers, Boston.
8. Coffman, F. D., and M. F. Dunn. 1988. Insulin-metal ion interactions: the binding of divalent cations to insulin hexamers and tetramers and the assembly of insulin hexamers. Biochemistry. 27:6179-6187.
9. De Graaf, R. A. G., A. Lewit-Bentley, and S. P. Tolley. 1981. Effects of destabilizing agents on the insulin hexamer structure. In Structural Studies on Molecules of Biological Interest. G. G. Dodson, J. P. Glusker, and D. Sayre, editors. Clarendon Press, Oxford. 547-556.
10. Derewenda, U., Z. Derewenda, E. J. Dodson, G. G. Dodson, R. D. Reynolds, G. D. Smith, C. Sparks, and D. Swenson. 1989. Phenol stabilizes more helix in a new symmetrical zinc insulin hexamer. Nature. 338: 594-596.
11. Dodson, G. G., and D. Steiner. 1998. The role of assembly in insulin's biosynthesis. Curr. Opin. Struct. Biol. 8:189-194.
12. Ducommun, Y., and A. E. Merbach. 1986. Solvent exchange reactions. In Inorganic High Pressure Chemistry. R. van Eldik, editor. Elsevier, Amsterdam. 69-113.
13. Eigen, M. 1963. Fast elementary steps in chemical reaction mechanisms. Pure Appl. Chem. 6:97-115.
14. Eisenstein, E., and H. K. Schachman. 1989. Determining the roles of subunits in protein function. In Protein Function - A Practical Approach. T. E. Creighton, editor. IRL Press, Oxford. 135-176.
15. Erijman, L., and G. Weber. 1991. Oligomeric protein associations: transition from stochastic to deterministic equilibrium. Biochemistry. 30: 1595-1599.
16. Erijman, L., and G. Weber. 1993. Use of sensitized fluorescence for the study of the exchange of subunits in protein aggregates. Pholochem. Photobiol. 57:411-415.
17. Förster, T. 1948. Zwischenmolekulare Energiewanderung und Fluoreszenz. Ann. Phys. 2:55-75.
18. Gross, L., and M. F. Dunn. 1992. Spectroscopic evidence for an intermediate in the T6 to R6 allosteric transition of the Co(II)-substituted insulin hexamer. Biochemistry. 31:1295-1301.
19. Hassiepen, U., M. Federwisch, T. Mülders, V. J. Lenz, H. G. Gattner, P. Krüger, and A. Wollmer. 1998. Analysis of protein self-association at constant concentration by fluorescence-energy transfer. Eur. J. Biochem. 255:580-587.
20. Hvidt, S. 1991. Insulin association in neutral solutions studied by light scattering. Biophys. Chem. 39:205-213.
21. 6 insulin hexamer. J. Mol. Biol. 258:136-157.
22. Jaenicke, R. 1987. Folding and association of proteins. Prog. Biophys. Mol. Biol. 49:117-237.
23. Jaenicke, R., R. Koberstein, and B. Teuscher. 1971. The enzymically active unit of lactic dehydrogenase. Molecular properties of lactic dehydrogenase at low-protein and high salt concentrations. Eur. J. Biochem. 23:150-159.
24. Jaenicke, R., and R. Rudolph. 1986. Refolding and association of oligomeric proteins. Methods Enzymol. 131:218-250.
25. Kaarsholm, N. C., H. C. Ko, and M. F. Dunn. 1989. Comparison of solution structural flexibility and zinc binding domains for insulin, proinsulin, and miniproinsulin. Biochemistry. 28:4427-4435.
26. Koren, R., and G. G. Hammes. 1976. A kinetic study of protein-protein interactions. Biochemistry. 15:1165-1171.
27. Krüger, P., G. Gilge, Y. Cabuk, and A. Wollmer. 1990. Cooperativity and intermediate states in the T → R-structural transformation of insulin. Biol. Chem. Hoppe-Seyler. 371:669-673.
28. Lenz, V. J., H. G. Gattner, M. Leithäuser, D. Brandenburg, A. Wollmer, and H. Höcker. 1994. Proteolyses of a fluorogenic insulin derivative and native insulin in reversed micelles monitored by fluorescence emission, reversed-phase high-performance liquid chromatography, and capillary zone electrophoresis. Anal. Biochem. 221:85-93.
29. Levine, I. N. 1995. Physical Chemistry. McGraw-Hill, New York.
30. Meighen, E. A., V. Pigiet, and H. K. Schachman. 1970. Hybridization of native and chemically modified enzymes. 3. The catalytic subunits of aspartate transcarbamylase. Proc. Natl. Acad. Sci. USA. 65:234-241.
31. Nicholls, A., K. A. Sharp, and B. Honig. 1991. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins. 11:281-296.
32. Osbome, H. H., and M. R. Hollaway. 1974. The hybridization of glyceraldehyde 3-phosphate dehydrogenases from rabbit muscle and yeast. Kinetics and thermodynamics of the reaction and isolation of the hybrid. Biochem. J. 143:651-662.
33. 2+ to the Glu(B13) site drives hexamer assembly and induces a conformation change. Biochemistry. 27:3387-3397.
34. Peterman, B. F. 1979. Measurement of the dead time of a fluorescence stopped-flow instrument. Anal. Biochem. 93:442-444.
35. Price, N. C. 1994. Assembly of multi-subunit structures. In Mechanisms of Protein Folding. R. H. Pain, editor. IRL Press, Oxford. 160-193.
36. Rahuel-Clermont, S., C. A. French, N. C. Kaarsholm, M. F. Dunn, and C. I. Chou. 1997. Mechanisms of stabilization of the insulin hexamer through allosteric ligand interactions. Biochemistry. 36:5837-5845.
37. 1H N.M.R. studies of insulin. Reversible transformation of 2-zinc to 4-zinc insulin hexamer. Int. J. Pept. Protein Res. 28:146-153.
38. Renscheidt, H., W. Strassburger, U. Glatter, A. Wollmer, G. G. Dodson, and D. A. Mercolá. 1984. A solution equivalent of the 2Zn → 4Zn transformation of insulin in the crystal. Eur. J. Biochem. 142:7-14.
39. Roy, M., M. L. Brader, R. W. Lee, N. C. Kaarsholm, J. F. Hansen, and M. F. Dunn. 1989. Spectroscopic signatures of the T to R conformational transition in the insulin hexamer. J. Bio Chem. 264:19081-19085.
40. Schlichtkrull, J. 1958. Insulin Crystals. Munksgard, Copenhagen.
41. Schulzki, H. D., B. Kramer, J. Fleischhauer, D. A. Mercola, and A. Wollmer. 1990. Calcium-dependent distance changes in binary and ternary complexes of troponin. Eur. J. Biochem. 189:683-692.
42. Smith, G. D., and G. G. Dodson. 1992. The structure of a rhombohedral R6 insulin hexamer that binds phenol. Biopolymers. 32:441-445.
43. Smith, G. D., W. L. Duax, E. J. Dodson, G. G. Dodson, R. A. G. de Graaf, and C. D. Reynolds. 1982. The structure of des-Phe B1 bovine insulin. Ada Crystallogr. B. 38:3028-3032.
44. Sundberg, R. J., and R. B. Martin. 1974. Interactions of histidine and other imidazole derivatives with transition metal ions in chemical and biological systems. Chem. Rev. 74:471-517.
45. Thomas, B., and A. Wollmer. 1989. Cobalt probing of structural alternatives for insulin in solution. Biol. Chem. Hoppe-Seyler. 370:1235-1244.
46. Wollmer, A., B. Rannefeld, B. R. Johansen, K. R. Hejnaes, P. Baischmidt, and F. B. Hansen. 1987. Phenol-promoted structural transformation of insulin in solution. Biol. Chem. Hoppe-Seyler. 368:903-911.
47. Yang, Y. R., and H. K. Schachman. 1987. Hybridization as a technique for studying interchain interactions in the catalytic trimers of aspartate transcarbamoylase. Anal. Biochem. 163:188-195.