Insulin-induced tyrosine-phosphorylation in intact rat adipocytes

Kaoru Momomura; Kazuyuki Tobe; Yousuke Seyama; Fumimaro Takaku; Masato Kasuga

doi:10.1016/S0006-291X(88)81264-6

Insulin-induced tyrosine-phosphorylation in intact rat adipocytes

Kaoru Momomura^*, Kazuyuki Tobe, Yousuke Seyama, Fumimaro Takaku, Masato Kasuga

^*Corresponding author for this work

Internal Medicine （1）

Research output: Contribution to journal › Article › peer-review

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Abstract

Insulin-induced tyrosine-phosphorylation in intact isolated rat adipocytes was studied using immunoblotting method with anti-phosphotyrosine antibodies. Insulin-stimulated adipocytes were solubilized with Triton X-100. The lysate was incubated with wheat germ agglutinin, then with hydroxylapatite. Insulin stimulated tyrosinephosphorylation of a 95 KDa protein which adsorbs to wheat germ agglutinin and appears to be the β-subunit of the insulin receptor. Among the proteins adsorbed to hydroxylapatite, tyrosine-phosphorylation of 170 KDa and 60 KDa proteins was stimulated. 170 KDa was also stimulated by polyclonal anti-insulin receptor antibodies B-10 Ig G, IGF-I and H₂O₂ . The detection of these proteins in rat adipocytes may lead to the elucidation of a common signal transduction pathway in insulin-responsive cells.

Original language	English
Pages (from-to)	1181-1186
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	155
Issue number	3
DOIs	https://doi.org/10.1016/S0006-291X(88)81264-6
State	Published - 1988/09/30

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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title = "Insulin-induced tyrosine-phosphorylation in intact rat adipocytes",

abstract = "Insulin-induced tyrosine-phosphorylation in intact isolated rat adipocytes was studied using immunoblotting method with anti-phosphotyrosine antibodies. Insulin-stimulated adipocytes were solubilized with Triton X-100. The lysate was incubated with wheat germ agglutinin, then with hydroxylapatite. Insulin stimulated tyrosinephosphorylation of a 95 KDa protein which adsorbs to wheat germ agglutinin and appears to be the β-subunit of the insulin receptor. Among the proteins adsorbed to hydroxylapatite, tyrosine-phosphorylation of 170 KDa and 60 KDa proteins was stimulated. 170 KDa was also stimulated by polyclonal anti-insulin receptor antibodies B-10 Ig G, IGF-I and H2O2 . The detection of these proteins in rat adipocytes may lead to the elucidation of a common signal transduction pathway in insulin-responsive cells.",

author = "Kaoru Momomura and Kazuyuki Tobe and Yousuke Seyama and Fumimaro Takaku and Masato Kasuga",

note = "Funding Information: This work was supported by a Grant-in=Aid for Development of Scientific Research from the Ministry of Edcation, Science and Culture of Japan.",

year = "1988",

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doi = "10.1016/S0006-291X(88)81264-6",

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T1 - Insulin-induced tyrosine-phosphorylation in intact rat adipocytes

AU - Momomura, Kaoru

AU - Tobe, Kazuyuki

AU - Seyama, Yousuke

AU - Takaku, Fumimaro

AU - Kasuga, Masato

N1 - Funding Information: This work was supported by a Grant-in=Aid for Development of Scientific Research from the Ministry of Edcation, Science and Culture of Japan.

PY - 1988/9/30

Y1 - 1988/9/30

N2 - Insulin-induced tyrosine-phosphorylation in intact isolated rat adipocytes was studied using immunoblotting method with anti-phosphotyrosine antibodies. Insulin-stimulated adipocytes were solubilized with Triton X-100. The lysate was incubated with wheat germ agglutinin, then with hydroxylapatite. Insulin stimulated tyrosinephosphorylation of a 95 KDa protein which adsorbs to wheat germ agglutinin and appears to be the β-subunit of the insulin receptor. Among the proteins adsorbed to hydroxylapatite, tyrosine-phosphorylation of 170 KDa and 60 KDa proteins was stimulated. 170 KDa was also stimulated by polyclonal anti-insulin receptor antibodies B-10 Ig G, IGF-I and H2O2 . The detection of these proteins in rat adipocytes may lead to the elucidation of a common signal transduction pathway in insulin-responsive cells.

AB - Insulin-induced tyrosine-phosphorylation in intact isolated rat adipocytes was studied using immunoblotting method with anti-phosphotyrosine antibodies. Insulin-stimulated adipocytes were solubilized with Triton X-100. The lysate was incubated with wheat germ agglutinin, then with hydroxylapatite. Insulin stimulated tyrosinephosphorylation of a 95 KDa protein which adsorbs to wheat germ agglutinin and appears to be the β-subunit of the insulin receptor. Among the proteins adsorbed to hydroxylapatite, tyrosine-phosphorylation of 170 KDa and 60 KDa proteins was stimulated. 170 KDa was also stimulated by polyclonal anti-insulin receptor antibodies B-10 Ig G, IGF-I and H2O2 . The detection of these proteins in rat adipocytes may lead to the elucidation of a common signal transduction pathway in insulin-responsive cells.

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JF - Biochemical and Biophysical Research Communications

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Insulin-induced tyrosine-phosphorylation in intact rat adipocytes

Abstract

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