The nonclassical insulin binding of insulin receptors from rat liver is due to the presence of two interacting α-subunits in the receptor complex

Arno Deger, Helmut Krämer, Reinhard Rapp, Rüdiger Koch, Ulrich Weber

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

The binding characteristics of the insulin receptor tetramer (α2β2) and dimer (αβ) were examined. Unlabelled insulin enhanced the dilution-induced dissociation only of the receptor tetramer-bound 125I-insulin. Furthermore, when both the receptor forms had been preincubated with anti-receptor-antibodies (B9-antiserum), insulin binding only to the receptor tetramer but not to the dimer was inhibited. However, both oligomers are not immunologically distinct since more than 80% of the two forms were immunoprecipitated by the antiserum. These results suggest that both insulin and anti-receptor-antibodies induce cooperative interactions between the two linked α-subunits of the receptor tetramer leading to a decrease in insulin binding of this receptor form.

Original languageEnglish (US)
Pages (from-to)459-464
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume135
Issue number2
DOIs
StatePublished - Mar 13 1986

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Insulin Receptor
Liver
Rats
Insulin
Immune Sera
Anti-Idiotypic Antibodies
Dimers
Antibodies
Oligomers
Dilution

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

The nonclassical insulin binding of insulin receptors from rat liver is due to the presence of two interacting α-subunits in the receptor complex. / Deger, Arno; Krämer, Helmut; Rapp, Reinhard; Koch, Rüdiger; Weber, Ulrich.

In: Biochemical and Biophysical Research Communications, Vol. 135, No. 2, 13.03.1986, p. 459-464.

Research output: Contribution to journalArticle

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