Stimulatory effect of puerarin on α1A-adrenoceptor to increase glucose uptake into cultured C2C12 cells of mice

Hsi Hsien Hsu, Cheng Kuei Chang, Hui Chen Su, I. Min Liu, Juei Tang Cheng

研究成果: 雜誌貢獻文章

18 引文 (Scopus)

摘要

Effects of puerarin, an active principle contained in the roots of Pueraria lobata (Leguminosae), on the regulation of glucose metabolism in an insulin deficient state were investigated in cultured myoblast C2C12 cells using glucose uptake as indicator. Puerarin enhanced the uptake of radioactive glucose into C2C12 cells in a concentration-dependent manner, which was abolished by prazosin pretreatment. Activation of α1-adrenoceptors by puerarin was further indicated by the displacement of [3H]prazosin binding in C2C12 cells. The stimulatory action of puerarin on glucose uptake was also reduced in C2C12 cells pre-incubated with the antagonists, both WB 4101 and RS 17056, at concentrations sufficient to block α1A-adrenoceptor (α1A-AR). An activation of α1A-AR seems responsible for the action of puerarin in C2C12 cells. Pharmacological inhibition of phospholipase C (PLC) by U73312 resulted a concentration-dependent decrease of puerarin-stimulated glucose uptake in C2C12 cells. This inhibition of glucose uptake by U73122 was specific because the inactive congener, U73343, failed to block puerarin-stimulated glucose uptake. Moreover, both chelerythrine and GF 109203X diminished the action of puerarin at concentration sufficient to inhibit protein kinase C (PKC). The obtained data suggest that an activation of α1A-AR by puerarin in C2C12 cells may increase the glucose uptake via the PLC-PKC pathway.
原文英語
頁(從 - 到)999-1003
頁數5
期刊Planta Medica
68
發行號11
DOIs
出版狀態已發佈 - 十一月 1 2002
對外發佈Yes

指紋

adrenergic receptors
Adrenergic Receptors
cultured cells
Cultured Cells
Cells
uptake mechanisms
Glucose
glucose
mice
phospholipase C
protein kinase C
cells
Prazosin
Chemical activation
Type C Phospholipases
Protein Kinase C
Pueraria montana var. lobata
Pueraria
myoblasts
puerarin

ASJC Scopus subject areas

  • Plant Science
  • Drug Discovery
  • Organic Chemistry
  • Pharmacology

引用此文

Stimulatory effect of puerarin on α1A-adrenoceptor to increase glucose uptake into cultured C2C12 cells of mice. / Hsu, Hsi Hsien; Chang, Cheng Kuei; Su, Hui Chen; Liu, I. Min; Cheng, Juei Tang.

於: Planta Medica, 卷 68, 編號 11, 01.11.2002, p. 999-1003.

研究成果: 雜誌貢獻文章

Hsu, Hsi Hsien ; Chang, Cheng Kuei ; Su, Hui Chen ; Liu, I. Min ; Cheng, Juei Tang. / Stimulatory effect of puerarin on α1A-adrenoceptor to increase glucose uptake into cultured C2C12 cells of mice. 於: Planta Medica. 2002 ; 卷 68, 編號 11. 頁 999-1003.
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abstract = "Effects of puerarin, an active principle contained in the roots of Pueraria lobata (Leguminosae), on the regulation of glucose metabolism in an insulin deficient state were investigated in cultured myoblast C2C12 cells using glucose uptake as indicator. Puerarin enhanced the uptake of radioactive glucose into C2C12 cells in a concentration-dependent manner, which was abolished by prazosin pretreatment. Activation of α1-adrenoceptors by puerarin was further indicated by the displacement of [3H]prazosin binding in C2C12 cells. The stimulatory action of puerarin on glucose uptake was also reduced in C2C12 cells pre-incubated with the antagonists, both WB 4101 and RS 17056, at concentrations sufficient to block α1A-adrenoceptor (α1A-AR). An activation of α1A-AR seems responsible for the action of puerarin in C2C12 cells. Pharmacological inhibition of phospholipase C (PLC) by U73312 resulted a concentration-dependent decrease of puerarin-stimulated glucose uptake in C2C12 cells. This inhibition of glucose uptake by U73122 was specific because the inactive congener, U73343, failed to block puerarin-stimulated glucose uptake. Moreover, both chelerythrine and GF 109203X diminished the action of puerarin at concentration sufficient to inhibit protein kinase C (PKC). The obtained data suggest that an activation of α1A-AR by puerarin in C2C12 cells may increase the glucose uptake via the PLC-PKC pathway.",
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AU - Hsu, Hsi Hsien

AU - Chang, Cheng Kuei

AU - Su, Hui Chen

AU - Liu, I. Min

AU - Cheng, Juei Tang

PY - 2002/11/1

Y1 - 2002/11/1

N2 - Effects of puerarin, an active principle contained in the roots of Pueraria lobata (Leguminosae), on the regulation of glucose metabolism in an insulin deficient state were investigated in cultured myoblast C2C12 cells using glucose uptake as indicator. Puerarin enhanced the uptake of radioactive glucose into C2C12 cells in a concentration-dependent manner, which was abolished by prazosin pretreatment. Activation of α1-adrenoceptors by puerarin was further indicated by the displacement of [3H]prazosin binding in C2C12 cells. The stimulatory action of puerarin on glucose uptake was also reduced in C2C12 cells pre-incubated with the antagonists, both WB 4101 and RS 17056, at concentrations sufficient to block α1A-adrenoceptor (α1A-AR). An activation of α1A-AR seems responsible for the action of puerarin in C2C12 cells. Pharmacological inhibition of phospholipase C (PLC) by U73312 resulted a concentration-dependent decrease of puerarin-stimulated glucose uptake in C2C12 cells. This inhibition of glucose uptake by U73122 was specific because the inactive congener, U73343, failed to block puerarin-stimulated glucose uptake. Moreover, both chelerythrine and GF 109203X diminished the action of puerarin at concentration sufficient to inhibit protein kinase C (PKC). The obtained data suggest that an activation of α1A-AR by puerarin in C2C12 cells may increase the glucose uptake via the PLC-PKC pathway.

AB - Effects of puerarin, an active principle contained in the roots of Pueraria lobata (Leguminosae), on the regulation of glucose metabolism in an insulin deficient state were investigated in cultured myoblast C2C12 cells using glucose uptake as indicator. Puerarin enhanced the uptake of radioactive glucose into C2C12 cells in a concentration-dependent manner, which was abolished by prazosin pretreatment. Activation of α1-adrenoceptors by puerarin was further indicated by the displacement of [3H]prazosin binding in C2C12 cells. The stimulatory action of puerarin on glucose uptake was also reduced in C2C12 cells pre-incubated with the antagonists, both WB 4101 and RS 17056, at concentrations sufficient to block α1A-adrenoceptor (α1A-AR). An activation of α1A-AR seems responsible for the action of puerarin in C2C12 cells. Pharmacological inhibition of phospholipase C (PLC) by U73312 resulted a concentration-dependent decrease of puerarin-stimulated glucose uptake in C2C12 cells. This inhibition of glucose uptake by U73122 was specific because the inactive congener, U73343, failed to block puerarin-stimulated glucose uptake. Moreover, both chelerythrine and GF 109203X diminished the action of puerarin at concentration sufficient to inhibit protein kinase C (PKC). The obtained data suggest that an activation of α1A-AR by puerarin in C2C12 cells may increase the glucose uptake via the PLC-PKC pathway.

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KW - CC cells

KW - Leguminosae

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KW - Protein kinase C

KW - Pueraria lobata

KW - Puerarin

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