Human recombinant Alpha2-HS glycoprotein is produced in insect cells as a full length inhibitor of the insulin receptor tyrosine kinase

L. Kalabay, K. Chavin, J. P. Lebreton, K. A. Robinson, M. G. Buse, P. Arnaud

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

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 B-chain 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 single-chain protein and possesses a biological role similar to that of its homologue in rats, pp63, described by Auberger et al.

Original languageEnglish
Pages (from-to)1-6
Number of pages6
JournalHormone and Metabolic Research
Volume30
Issue number1
DOIs
Publication statusPublished - Jan 1 1998

Keywords

  • Alpha2-HS Glycoprotein
  • Fetuin
  • Insulin receptor
  • Pp63
  • Recombinant baculovirus
  • Tyrosine kinase

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Biochemistry
  • Endocrinology
  • Clinical Biochemistry
  • Biochemistry, medical

Fingerprint Dive into the research topics of 'Human recombinant Alpha2-HS glycoprotein is produced in insect cells as a full length inhibitor of the insulin receptor tyrosine kinase'. Together they form a unique fingerprint.

  • Cite this