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 language | English (US) |
|---|---|
| Pages (from-to) | 459-464 |
| Number of pages | 6 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 135 |
| Issue number | 2 |
| DOIs | |
| State | Published - Mar 13 1986 |
Fingerprint
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 journal › Article
}
TY - JOUR
T1 - The nonclassical insulin binding of insulin receptors from rat liver is due to the presence of two interacting α-subunits in the receptor complex
AU - Deger, Arno
AU - Krämer, Helmut
AU - Rapp, Reinhard
AU - Koch, Rüdiger
AU - Weber, Ulrich
PY - 1986/3/13
Y1 - 1986/3/13
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0022441892&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0022441892&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(86)90016-1
DO - 10.1016/0006-291X(86)90016-1
M3 - Article
C2 - 3516142
AN - SCOPUS:0022441892
VL - 135
SP - 459
EP - 464
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -