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Dual regulation of glycogen synthase kinase-3beta by the alpha1A-adrenergic receptor

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Dual regulation of glycogen synthase kinase-3beta by the alpha1A-adrenergic receptor. / Ballou, L M; Tian, P Y; Lin, H Y; Jiang, Y P; Lin, R Z.

In: J BIOL CHEM, Vol. 276, No. 44, 02.11.2001, p. 40910-6.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Ballou, LM, Tian, PY, Lin, HY, Jiang, YP & Lin, RZ 2001, 'Dual regulation of glycogen synthase kinase-3beta by the alpha1A-adrenergic receptor', J BIOL CHEM, vol. 276, no. 44, pp. 40910-6. https://doi.org/10.1074/jbc.M103480200

APA

Ballou, L. M., Tian, P. Y., Lin, H. Y., Jiang, Y. P., & Lin, R. Z. (2001). Dual regulation of glycogen synthase kinase-3beta by the alpha1A-adrenergic receptor. J BIOL CHEM, 276(44), 40910-6. https://doi.org/10.1074/jbc.M103480200

Vancouver

Ballou LM, Tian PY, Lin HY, Jiang YP, Lin RZ. Dual regulation of glycogen synthase kinase-3beta by the alpha1A-adrenergic receptor. J BIOL CHEM. 2001 Nov 2;276(44):40910-6. https://doi.org/10.1074/jbc.M103480200

Bibtex

@article{24d22d9b7994440d80072e14555a03a9,
title = "Dual regulation of glycogen synthase kinase-3beta by the alpha1A-adrenergic receptor",
abstract = "Catecholamines, acting through adrenergic receptors, play an important role in modulating the effects of insulin on glucose metabolism. Insulin activation of glycogen synthesis is mediated in part by the inhibitory phosphorylation of glycogen synthase kinase-3 (GSK-3). In this study, catecholamine regulation of GSK-3beta was investigated in Rat-1 fibroblasts stably expressing the alpha1A-adrenergic receptor. Treatment of these cells with either insulin or phenylephrine (PE), an alpha1-adrenergic receptor agonist, induced Ser-9 phosphorylation of GSK-3beta and inhibited GSK-3beta activity. Insulin-induced GSK-3beta phosphorylation is mediated by the phosphatidylinositol 3-kinase/Akt signaling pathway. PE treatment does not activate phosphatidylinositol 3-kinase or Akt (Ballou, L. M., Cross, M. E., Huang, S., McReynolds, E. M., Zhang, B. X., and Lin, R. Z. (2000) J. Biol. Chem. 275, 4803-4809), but instead inhibits insulin-induced Akt activation and GSK-3beta phosphorylation. Experiments using protein kinase C (PKC) inhibitors suggest that phorbol ester-sensitive novel PKC and G{\"o} 6983-sensitive atypical PKC isoforms are involved in the PE-induced phosphorylation of GSK-3beta. Indeed, PE treatment of Rat-1 cells increased the activity of atypical PKCzeta, and expression of PKCzeta in COS-7 cells stimulated GSK-3beta Ser-9 phosphorylation. In addition, PE-induced GSK-3beta phosphorylation was reduced in Rat-1 cells treated with a cell-permeable PKCzeta pseudosubstrate peptide inhibitor. These results suggest that the alpha1A-adrenergic receptor regulates GSK-3beta through two signaling pathways. One pathway inhibits insulin-induced GSK-3beta phosphorylation by blocking insulin activation of Akt. The second pathway stimulates Ser-9 phosphorylation of GSK-3beta, probably via PKC.",
keywords = "Adrenergic alpha-Agonists, Animals, Base Sequence, Calcium-Calmodulin-Dependent Protein Kinases, Cell Line, DNA Primers, Enzyme Activation, Glycogen Synthase Kinase 3, Glycogen Synthase Kinases, Humans, Insulin, Phenylephrine, Phosphorylation, Protein Kinase C, Rats, Receptors, Adrenergic, alpha-1, Serine, Signal Transduction",
author = "Ballou, {L M} and Tian, {P Y} and Lin, {H Y} and Jiang, {Y P} and Lin, {R Z}",
year = "2001",
month = nov,
day = "2",
doi = "10.1074/jbc.M103480200",
language = "English",
volume = "276",
pages = "40910--6",
journal = "J BIOL CHEM",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "44",

}

RIS

TY - JOUR

T1 - Dual regulation of glycogen synthase kinase-3beta by the alpha1A-adrenergic receptor

AU - Ballou, L M

AU - Tian, P Y

AU - Lin, H Y

AU - Jiang, Y P

AU - Lin, R Z

PY - 2001/11/2

Y1 - 2001/11/2

N2 - Catecholamines, acting through adrenergic receptors, play an important role in modulating the effects of insulin on glucose metabolism. Insulin activation of glycogen synthesis is mediated in part by the inhibitory phosphorylation of glycogen synthase kinase-3 (GSK-3). In this study, catecholamine regulation of GSK-3beta was investigated in Rat-1 fibroblasts stably expressing the alpha1A-adrenergic receptor. Treatment of these cells with either insulin or phenylephrine (PE), an alpha1-adrenergic receptor agonist, induced Ser-9 phosphorylation of GSK-3beta and inhibited GSK-3beta activity. Insulin-induced GSK-3beta phosphorylation is mediated by the phosphatidylinositol 3-kinase/Akt signaling pathway. PE treatment does not activate phosphatidylinositol 3-kinase or Akt (Ballou, L. M., Cross, M. E., Huang, S., McReynolds, E. M., Zhang, B. X., and Lin, R. Z. (2000) J. Biol. Chem. 275, 4803-4809), but instead inhibits insulin-induced Akt activation and GSK-3beta phosphorylation. Experiments using protein kinase C (PKC) inhibitors suggest that phorbol ester-sensitive novel PKC and Gö 6983-sensitive atypical PKC isoforms are involved in the PE-induced phosphorylation of GSK-3beta. Indeed, PE treatment of Rat-1 cells increased the activity of atypical PKCzeta, and expression of PKCzeta in COS-7 cells stimulated GSK-3beta Ser-9 phosphorylation. In addition, PE-induced GSK-3beta phosphorylation was reduced in Rat-1 cells treated with a cell-permeable PKCzeta pseudosubstrate peptide inhibitor. These results suggest that the alpha1A-adrenergic receptor regulates GSK-3beta through two signaling pathways. One pathway inhibits insulin-induced GSK-3beta phosphorylation by blocking insulin activation of Akt. The second pathway stimulates Ser-9 phosphorylation of GSK-3beta, probably via PKC.

AB - Catecholamines, acting through adrenergic receptors, play an important role in modulating the effects of insulin on glucose metabolism. Insulin activation of glycogen synthesis is mediated in part by the inhibitory phosphorylation of glycogen synthase kinase-3 (GSK-3). In this study, catecholamine regulation of GSK-3beta was investigated in Rat-1 fibroblasts stably expressing the alpha1A-adrenergic receptor. Treatment of these cells with either insulin or phenylephrine (PE), an alpha1-adrenergic receptor agonist, induced Ser-9 phosphorylation of GSK-3beta and inhibited GSK-3beta activity. Insulin-induced GSK-3beta phosphorylation is mediated by the phosphatidylinositol 3-kinase/Akt signaling pathway. PE treatment does not activate phosphatidylinositol 3-kinase or Akt (Ballou, L. M., Cross, M. E., Huang, S., McReynolds, E. M., Zhang, B. X., and Lin, R. Z. (2000) J. Biol. Chem. 275, 4803-4809), but instead inhibits insulin-induced Akt activation and GSK-3beta phosphorylation. Experiments using protein kinase C (PKC) inhibitors suggest that phorbol ester-sensitive novel PKC and Gö 6983-sensitive atypical PKC isoforms are involved in the PE-induced phosphorylation of GSK-3beta. Indeed, PE treatment of Rat-1 cells increased the activity of atypical PKCzeta, and expression of PKCzeta in COS-7 cells stimulated GSK-3beta Ser-9 phosphorylation. In addition, PE-induced GSK-3beta phosphorylation was reduced in Rat-1 cells treated with a cell-permeable PKCzeta pseudosubstrate peptide inhibitor. These results suggest that the alpha1A-adrenergic receptor regulates GSK-3beta through two signaling pathways. One pathway inhibits insulin-induced GSK-3beta phosphorylation by blocking insulin activation of Akt. The second pathway stimulates Ser-9 phosphorylation of GSK-3beta, probably via PKC.

KW - Adrenergic alpha-Agonists

KW - Animals

KW - Base Sequence

KW - Calcium-Calmodulin-Dependent Protein Kinases

KW - Cell Line

KW - DNA Primers

KW - Enzyme Activation

KW - Glycogen Synthase Kinase 3

KW - Glycogen Synthase Kinases

KW - Humans

KW - Insulin

KW - Phenylephrine

KW - Phosphorylation

KW - Protein Kinase C

KW - Rats

KW - Receptors, Adrenergic, alpha-1

KW - Serine

KW - Signal Transduction

U2 - 10.1074/jbc.M103480200

DO - 10.1074/jbc.M103480200

M3 - SCORING: Journal article

C2 - 11533051

VL - 276

SP - 40910

EP - 40916

JO - J BIOL CHEM

JF - J BIOL CHEM

SN - 0021-9258

IS - 44

ER -