Abstract
Insulin-like growth factor (IGF) -I and -II mediate mitogenesis, differentiation and insulin-like metabolic effects.1 Their amino acid sequence is divided into 4 domains designated B-C-A-D beginning from the amino terminus. The B-and A-domains of IGF-I and IGF-II share substantial homology with each other and with the B-and A-chains of insulin.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
M. M. Rechter and S. P. Nisstey, Peptide Growth Factors and Their Receptors I. Insulin-like Growth Factors, in: “Handbook Exp. Pharm., Vol. 95,” M. B. Sporn and A. B. Roberts, eds., Springer-Verlag, Berlin (1990), p 263.
M. M. Rechter, Insulin-like growth factor binding proteins, Vitamins &Hormones 47:1 (1993).
K. Sakano, T. Enjoh, F. Numata, H. Fujiwara, Y. Marumoto, N. Higashihashi, Y. Sato, J. F. Perdue, and Y. Fujita-Yamaguchi, The design, expression, and characterization of human insulin-like growth factor II (IGF-II) mutants specific for either the IGF-II/cation-independent mannose 6-phosphate receptor or IGF-I receptor, J. Biol. Chem. 266:20626 (1991).
L. A. Bach, N. R. Thotakura, and M. M. Rechler, Human insulin-like growth factor binding protein-6 is Oglycosylated, Biochem. Biophys. Res. Commun. 186:301 (1992).
L. A. Bach, S. Hsieh, K. Sakano, H. Fujiwara, J. F. Perdue, and M. M. Rechler, Binding of mutants of human insulin-like growth factor II (IGF-II) to insulin-like growth factor binding proteins 1-6, J. Biol. Chem. (1993). In press.
T. L. Blundell, S. Bedarkar, and R. E. Humbel, Tertiary structures, receptor binding, and antigenicity of insulinlike growth factors, Federation Proc. 42:2592 (1983).
B. Forbes, L. Szabo, R. C. Baxter, F. J. Ballard, and J. C. Wallace, Classification of the insulin-like growth factor binding proteins into three distinct categories according to their binding specificities, Biochem. Biophys. Res. Commun. 157:196 (1988).
D. R. Clemmons, M. L. DeHoff, W. H. Busby, M. L. Bayne, and M. A. Cascieri, Competition for binding to insulin-like growth factor (IGF) binding protein-2,3,4, and 5 by the IGFs and IGF analogs, Endocrinology 131:890 (1992).
C. Lüthi, B. V. Roth, and R. E. Humbel, Mutants of human insulin-like growth factor II (IGF II)-Expression and characterization of truncated IGF II and of two naturally occurring variants, Eur. J. Biochem. 205:483 (1992).
S. E. Shoelson, Z. -X. Lu, L. Parlautan, C. S. Lynch, and M. A. Weiss, Mutations at the dimer, hexamer, and receptor-binding surfaces of insulin independently affect insulin-insulin and insulin-receptor interactions, Biochemistry 31:1757 (1992).
Q. X. Hua, S. E. Shoelson, K. Inouye, and M. A. Weiss, Paradoxical structure and function in a mutant human insulin associated with diabetes mellitus, Proc. Natl. Acad. Sci. USA 90:582 (1993).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1994 Springer Science+Business Media New York
About this chapter
Cite this chapter
Bach, L.A., Hsieh, S., Sakano, Ki., Fujiwara, H., Perdue, J.F., Rechler, M.M. (1994). Towards Identification of a Binding Site on Insulin-Like Growth Factor-II for IGF-Binding Proteins. In: Le Roith, D., Raizada, M.K. (eds) Current Directions in Insulin-Like Growth Factor Research. Advances in Experimental Medicine and Biology, vol 343. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2988-0_6
Download citation
DOI: https://doi.org/10.1007/978-1-4615-2988-0_6
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-6301-9
Online ISBN: 978-1-4615-2988-0
eBook Packages: Springer Book Archive