Fate of insulin analogs in intact and nephrectomized rats determined by their receptor binding constants

American Journal of Physiology - Endocrinology and Metabolism

Volumn 272, Issue 6 35-6, 1997, Pages

  Kruse, Viggo ^a   Jensen, Ivan ^a   Permin, Lise ^a   Heding, Anders ^b  

^a NOVO NORDISK A S   (Denmark)

^b HAGEDORN RESEARCH INSTITUTE   (Denmark)

Author keywords

125I labeled analogs; Association and dissociation rate constants; Insulin fragments; Protein bound insulin; Q Sepharose chromatography

Indexed keywords

HUMAN INSULIN; INSULIN DERIVATIVE;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; BIOSENSOR; CHROMATOGRAPHY; CONTROLLED STUDY; DISSOCIATION CONSTANT; HORMONE RECEPTOR INTERACTION; INSULIN METABOLISM; MALE; NEPHRECTOMY; NONHUMAN; PRIORITY JOURNAL; RAT;

EID: 0030845447     PISSN: 01931849     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpendo.1997.272.6.e1089     Document Type: Article

References (21)

1. 51Cr-labeled erythrocytes from the blood of volume-expanded rats. Am. J. Physiol. 234 (Renal Fluid Electrolyte Physiol. 3): F386-F392, 1978.
2. Autoniades, H. N. Metabolism of single-component and high-molecular-weight radioactive insulin in rats. Endocrinology 99: 481-489, 1976.
3. Benzi, L., P. Cecchetti, A. Ciccarone, A. Pilo, G. di Cianni, and R. Navalesi. Insulin degradation in vitro and in vivo: a comparative study in men. Evidence that immunoprecipitable, partially rebindable degradation products are released from cells and circulate in blood. Diabetes 43: 297-304, 1994.
4. Berman, M., W. F. Beltz, P. C. Grief, R. Chabay, and R. C. Boston. CONSAM User's Guide. Washington D. C., US Govt. Printing Office, 1984. (DHSS publ. no. 1983-421-132: 3279)
5. Berman, M., E. A. McGuire, J. Roth, and A. J. Zeleznik. Kinetic modeling of insulin binding to receptors and degradation in vivo in the rabbit. Diabetes 29: 50-59, 1980.
6. Brange, J. Stability of Insulin. Studies on the Physical and Chemical Stability of Insulin in Pharmaceutical Formulation. Lancaster, UK: Kluwer Academic Publishers, 1994, p. 23-36.
7. Brange, J., U. Ribel, J. F. Hansen, G. Dodson, M. T. Hansen, S. Havelund, S. G. Melberg, F. Norris, K. Norris, L. Snel, A. R. Sørensen, and H. O. Voigt. Monomeric insulins obtained by protein engineering and their medical implications. Nature 333: 679-682, 1988.
8. Carpentier, J. L. Insulin receptor internalization: molecular mechanisms and physiopathological implications. Diabetologia 37, Suppl. 2: S117-S124, 1994.
9. Drejer, K., V. Kruse, U. D. Larsen, P. Hougaard, S. Bjørn, and S. Gammeltoft. Receptor binding and tyrosine kinase activation by insulin analogues with extreme affinities studied in hepatoma HepG2 cells. Diabetes 40: 1488-1495, 1991.
10. Duckworth, W. C., F. G. Hamel, J. Liepnieks, D. Peavy, B. Frank, and R. Rabkin. Insulin degradation products from perfused rat kidney. Am. J. Physiol. 256 (Endocrinol. Metab. 19): E208-E214, 1989.
11. Duckworth, W. C., F. G. Hamel, D. E. Peavy, J. J. Liepnieks, M. P. Ryan, M. A. Hermodson, and B. H. Frank. Degradation products of insulin generated by hepatocytes and by insulin protease. J. Biol. Chem. 263: 1826-1833, 1988.
12. Hansen, B. F., G. Danielsen, K. Drejer, A. R. Sørensen, F. C. Wiberg, H. H. Klein, and A. G. Lundemose. Sustained signalling from the insulin receptor after stimulation with insulin analogues exhibiting increased mitogenic potency. Biochem. J. 315: 271-279, 1996.
13. Heding, A., R. Gill, Y. Ogawa, P. De Meyts, and R. M. Shymko. Biosensor measurement of the binding of insulin-like growth factors I and II and their analogues to insulin-like growth factor-binding protein-3. J. Biol. Chem. 271: 13948-13952, 1996.
14. Hua, Q. X., S. E. Shoelson, M. Kochoyan, and M. A. Weiss. Receptor binding redefined by a structural switch in a mutant human insulin. Nature 354: 238-241, 1991.
15. Jensen, I., V. Kruse, and U. D. Larsen. Scintigraphic studies in rats. Kinetics of insulin analogues covering wide range of affinities. Diabetes 40: 628-632, 1991.
16. Lee, H. B., and M. D. Blaufox. Blood volume in the rat. J. Nucl. Med. 25: 72-76, 1985.
17. Morishima, T., S. Pye, C. Bradshaw, and J. Radziuk. Posthepatic rate of appearance of insulin: measurement and validation in the nonsteady state. Am. J. Physiol. 263 (Endocrinol. Metab. 26): E772-E779, 1992.
18. Pezzino, V., V. Papa, A. Costantino, L. Frittitta, P. Russo, I. D. Goldfine, and R. Vigneri. Identification and initial characterization of insulin receptor-like immunoreactivity in human plasma. J. Clin. Endocrinol. Metab. 74: 1116-1121, 1992.
19. 123I-insulin and scintillation scanning. In: Insulin Receptors. Clinical Assessment, Biological Responses, and Comparison to the IGF-I Receptor. Part B, edited by C. R. Kahn and L. C. Harrison. New York: Liss, 1988, p. 135-151.
20. 125I-insulin: kinetics of interaction with its receptors and rate of degradation in vivo. Am. J. Physiol. 239 (Endocrinol. Metab. 2): E3-E11, 1980.
21. Yonezawa, K., K. Yokono, K. Shii, J. Hari, S. Yaso, T. Sakamoto, Y. Kawase, H. Akiyama, S. Taketomi, and S. Baba. Biological properties of an initial degradation product of insulin by insulin-degrading enzyme. Endocrinology 124: 496-504, 1989.