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DiaMedBase ID
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DMPPl553 |
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Medicinal Plant
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Pueraria lobata |
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Plant part(s)
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Roots |
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Objective
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To study the effects of puerarin |
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Journal Source
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Planta Med. 2002;
68(11):999-1003 |
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Title
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Stimulatory effect of puerarin on
alpha1A-adrenoceptor to increase glucose uptake into cultured C2C12
cells of mice |
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Authors
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Hsu HH, Chang CK, Su HC, Liu IM, Cheng
JT |
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Address
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Department of Surgery, Mackay Memorial
Hospital, Taipei City, Taiwan, R.O.C |
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Abstract
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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 C 2 C 12 cells using glucose
uptake as indicator.Puerarin enhanced the uptake of radioactive
glucose into C 2 C 12 cells in a concentration-dependent manner, which
was abolished by prazosin pretreatment. Activation of alpha 1 -adrenoceptors
by puerarin was further indicated by the displacement of [ 3H]prazosin
binding in C 2 C 12 cells. The stimulatory action of puerarin on
glucose uptake was also reduced in C 2 C 12 cells pre-incubated with
the antagonists, both WB 4101 and RS 17 056, at concentrations
sufficient to block alpha 1A -adrenoceptor (alpha 1A -AR). An
activation of alpha 1A -AR seems responsible for the action of
puerarin in C 2 C 12 cells. Pharmacological inhibition of
phospholipase C (PLC) by U73312 resulted a concentration-dependent
decrease of puerarin-stimulated glucose uptake in C 2 C 12 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 alpha
1A -AR by puerarin in C 2 C 12 cells may increase the glucose uptake
via the PLC-PKC pathway. |
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Diseases |
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Disease Link |
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DiaMedBase ID |
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DMPPt554 |
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Medicinal Plant
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Pueraria thunbergiana |
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Plant part(s)
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Flower |
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Objective |
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To elucidate the
pharmacological actions of immunosuppressive saponin obtained from the
flower of Pueraria thunbergiana (Leguminosae) in the diabetic
rat |
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Journal Source
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Journal of Medicinal
Food,
2004; 7(1):31-37 |
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Title
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Effect of
Kaikasaponin III Obtained from Pueraria thunbergiana Flowers on
Serum and Hepatic Lipid Peroxides and Tissue Factor Activity in the
Streptozotocin-Induced Diabetic Rat |
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Authors
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Jongwon Choi1,
Myung-Hee Shin1, Kun-Young Park2,
Kyung-Tae Lee3, Hyun-Ju Jung3,
Myung-Sun Lee3, Hee-Juhn Park4 |
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Address
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1College
of Pharmacy, Kyungsung University; 2Department of
Food and Nutrition, Pusan National University, Busan; 3College
of Pharmacy, Kyung-Hee University, Seoul; 4Department
of Botanical Resources, Sangji University, Wonju, Korea |
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Abstract
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We investigated the effect of
kaikasaponin III (KS-III) on Phase I and II enzymes and tissue factor
(TF) activity to elucidate the pharmacological actions of this
immunosuppressive saponin in the diabetic rat. This compound was
obtained from the flower of Pueraria thunbergiana (Leguminosae)
by chromatographic isolation. This crude drug (Puerariae Flos) has
been used as a therapeutic agent for diabetes mellitus in traditional
Korean medicine. KS-III prolonged the bleeding time and plasma
clotting time in streptozotocin (STZ)-treated rats and increased the
TF activity, suggesting that this compound has anti-thrombosis
activity in STZ-induced rats. It also inhibited the formation of
malondialdehyde (MDA) and hydroxy radicals in serum and liver, but
promoted superoxide dismutase (SOD) activity. Low MDA concentrations
and low xanthine oxidase and aldehyde oxidase activities were observed
in the KS-III-treated rats, suggesting that such Phase I enzyme
activities are the major source of lipid peroxidation. However, KS-III
increased Phase II enzyme activities such as SOD, glutathione
peroxidase, and catalase, suggesting the activation of free
radical-scavenging enzymes. These results suggest that KS-III may
exhibit its hypoglycemic and hypolipidemic effects by up-regulating or
down-regulating antioxidant mechanisms via the changes in Phase
I and II enzyme activities. |
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Diseases |
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Disease Link |
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