Horm Metab Res 1998; 30(1): 1-6
DOI: 10.1055/s-2007-978822
Original Basic

© Georg Thieme Verlag Stuttgart · New York

Human Recombinant Alpha2-HS Glycoprotein is Produced in Insect Cells as a Full Length Inhibitor of the Insulin Receptor Tyrosine Kinase

L. Kalabay1 , K. Chavin2 , J.-P. Lebreton3 , K. A. Robinson2 , M. G. Buse2 , P. Arnaud2
  • 13rd Department of Medicine, Semmeiweis University Medical School, Budapest, Hungary
  • 2Departments of Microbiology and Immunology, Surgery and Medicine, Medical University of South Carolina, Charleston, USA
  • 3INSERM U. 78, Bois-Guillaume Cedex, France
Further Information

Publication History



Publication Date:
20 April 2007 (online)

Human Alpha2-HS glycoprotein (AHSG), a glycoprotein synthesized by hepatocytes, was expressed in insect cells using the recombinant baculovirus system. The protein was purified from the cell supernatant, and appeared as a single band at about 52 kDa. Western blot using a specific antibody to the Bchain of AHSG indicated that the connecting peptide was present in the protein. When incubated with solubilized insulin receptors, recombinant AHSG inhibited the tyrosine kinase activity of the receptors in a dose-dependent fashion at concentrations in the range of those of the circulating protein. AHSG did not interfere with the binding of insulin to its receptor. These results indicate that human AHSG represents a natural inhibitor of the insulin receptor tyrosine kinase, is active as a singlechain protein and possesses a biological role similar to that of its homologue in rats, pp63, described by Auberger et al. (1).