Gq/11 is involved in insulin-stimulated inositol phosphoglycan putative mediator generation in rat liver membranes: Co-localization of Gq/11 with the insulin receptor in membrane vesicles

S. Sleight; B. A. Wilson; D. B. Heimark; J. Larner

doi:10.1016/S0006-291X(02)00701-5

G_q/11 is involved in insulin-stimulated inositol phosphoglycan putative mediator generation in rat liver membranes: Co-localization of G_q/11 with the insulin receptor in membrane vesicles

S. Sleight, B. A. Wilson, D. B. Heimark, J. Larner

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

Abstract

Insulin signaling to generate inositol phosphoglycans (IPGs) was demonstrated to occur via the participation of the heterotrimeric G-proteins G_q/11. IPGs were measured as two specific inositol markers, myo-inositol and chiro-inositol after strong acid hydrolysis. Insulin and Pasteurella multocida toxin (PMT) generated both myo-inositol and chiro-inositol IPGs in a dose-dependent manner. PMT has been shown to activate G_q specifically. Insulin action was abrogated by pre-treatment with anti _Gq/11 antibody. Western blotting demonstrated the enrichment of both insulin receptor β subunit and G_q/11 in the liver membrane vesicles. Vesicles also contained clathrin, caveolin PLC β1 and PLCΔ. Immunogold staining revealed the co-localization of both insulin receptor β subunit and G_q/11 in an approximate stochiometric ratio of 1:3. No vesicles were detected with either component alone. The present and considerable published data provide strong evidence for insulin signaling both via a tyrosine kinase cascade mechanism and via heterotrimeric G-protein interactions.

Original language	English (US)
Pages (from-to)	561-569
Number of pages	9
Journal	Biochemical and Biophysical Research Communications
Volume	295
Issue number	2
DOIs	https://doi.org/10.1016/S0006-291X(02)00701-5
State	Published - 2002

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/S0006-291X(02)00701-5

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G_q/11 is involved in insulin-stimulated inositol phosphoglycan putative mediator generation in rat liver membranes: Co-localization of G_q/11 with the insulin receptor in membrane vesicles. / Sleight, S.; Wilson, B. A.; Heimark, D. B. et al.
In: Biochemical and Biophysical Research Communications, Vol. 295, No. 2, 2002, p. 561-569.

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

Sleight, S, Wilson, BA, Heimark, DB & Larner, J 2002, 'G_q/11 is involved in insulin-stimulated inositol phosphoglycan putative mediator generation in rat liver membranes: Co-localization of G_q/11 with the insulin receptor in membrane vesicles', Biochemical and Biophysical Research Communications, vol. 295, no. 2, pp. 561-569. https://doi.org/10.1016/S0006-291X(02)00701-5

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abstract = "Insulin signaling to generate inositol phosphoglycans (IPGs) was demonstrated to occur via the participation of the heterotrimeric G-proteins Gq/11. IPGs were measured as two specific inositol markers, myo-inositol and chiro-inositol after strong acid hydrolysis. Insulin and Pasteurella multocida toxin (PMT) generated both myo-inositol and chiro-inositol IPGs in a dose-dependent manner. PMT has been shown to activate Gq specifically. Insulin action was abrogated by pre-treatment with anti Gq/11 antibody. Western blotting demonstrated the enrichment of both insulin receptor β subunit and Gq/11 in the liver membrane vesicles. Vesicles also contained clathrin, caveolin PLC β1 and PLCΔ. Immunogold staining revealed the co-localization of both insulin receptor β subunit and Gq/11 in an approximate stochiometric ratio of 1:3. No vesicles were detected with either component alone. The present and considerable published data provide strong evidence for insulin signaling both via a tyrosine kinase cascade mechanism and via heterotrimeric G-protein interactions.",

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N2 - Insulin signaling to generate inositol phosphoglycans (IPGs) was demonstrated to occur via the participation of the heterotrimeric G-proteins Gq/11. IPGs were measured as two specific inositol markers, myo-inositol and chiro-inositol after strong acid hydrolysis. Insulin and Pasteurella multocida toxin (PMT) generated both myo-inositol and chiro-inositol IPGs in a dose-dependent manner. PMT has been shown to activate Gq specifically. Insulin action was abrogated by pre-treatment with anti Gq/11 antibody. Western blotting demonstrated the enrichment of both insulin receptor β subunit and Gq/11 in the liver membrane vesicles. Vesicles also contained clathrin, caveolin PLC β1 and PLCΔ. Immunogold staining revealed the co-localization of both insulin receptor β subunit and Gq/11 in an approximate stochiometric ratio of 1:3. No vesicles were detected with either component alone. The present and considerable published data provide strong evidence for insulin signaling both via a tyrosine kinase cascade mechanism and via heterotrimeric G-protein interactions.

AB - Insulin signaling to generate inositol phosphoglycans (IPGs) was demonstrated to occur via the participation of the heterotrimeric G-proteins Gq/11. IPGs were measured as two specific inositol markers, myo-inositol and chiro-inositol after strong acid hydrolysis. Insulin and Pasteurella multocida toxin (PMT) generated both myo-inositol and chiro-inositol IPGs in a dose-dependent manner. PMT has been shown to activate Gq specifically. Insulin action was abrogated by pre-treatment with anti Gq/11 antibody. Western blotting demonstrated the enrichment of both insulin receptor β subunit and Gq/11 in the liver membrane vesicles. Vesicles also contained clathrin, caveolin PLC β1 and PLCΔ. Immunogold staining revealed the co-localization of both insulin receptor β subunit and Gq/11 in an approximate stochiometric ratio of 1:3. No vesicles were detected with either component alone. The present and considerable published data provide strong evidence for insulin signaling both via a tyrosine kinase cascade mechanism and via heterotrimeric G-protein interactions.

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