Inhibitory effect of aqueous extract from the gall of Rhus chinensis on alpha-glucosidase activity and postprandial blood glucose

As a dimer of proanthocyanidin, proanthocyanidin B2 (PB2) was found to effectively attenuate postprandial blood glucose in mice after sucrose loading.

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ALPHA AMYLASE AND ALPHA GLUCOSIDASE INHIBITION ACTIVITY OF SELECTED EDIBLE SEAWEEDS FROM SOUTH COAST AREA OF INDIA

International Journal of Pharmacy and Pharmaceutical Sciences ◽

10.22159/ijpps.2017v9i6.17684 ◽

2017 ◽

Vol 9 (6) ◽

pp. 64 ◽

Cited By ~ 2

Author(s):

P. Reka ◽

Thahira Banu A. ◽

M. Seethalakshmi

Keyword(s):

Aqueous Extract ◽

Inhibitory Activity ◽

Alpha Amylase ◽

Postprandial Blood Glucose ◽

Inhibition Activity ◽

Gracilaria Edulis ◽

Edible Seaweeds ◽

Daily Diet ◽

Postprandial Blood Glucose Level ◽

Alpha Glucosidase

Objective: The present work was to investigate the alpha amylase and alpha-glucosidase inhibitory activity of the selected edible seaweeds.Methods: The seaweeds namely Acanthophora spicifera, Gracilaria corticata, Gracilaria edulis, Ulva lactuca and Ulva reticulata were selected for this study. Six and eight hours of ethanol and aqueous extract were used for the estimation of alpha amylase using DNS method and alpha-glucosidase inhibition activity.Results: The study reported that the solvent from ethanol and aqueous in eight hours of extraction showed a higher inhibitory activity than six hours of extraction. Maximum of 89.1±0.96 and 79.55±3.08 percent of alpha-amylase and alpha-glucosidase inhibition activity were detected in the eight hours of aqueous extract (0.5 ml) of Ulva reticulata and Gracilaria edulis respectively. All the selected edible seaweeds had significant differences (p<0.05) in alpha amylase and alpha glucosidase inhibition activity between the selected seaweeds with different extracts.Conclusion: It was concluded that all the selected edible seaweeds have the potential to act as a potent inhibitor of the carbohydrate hydrolyzing enzyme. Thus, it was clear from the study that seaweeds incorporated in small amounts in the dishes consumed in the daily diet can bring a control on postprandial blood glucose level.

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An inhibitory effect on the increase in the postprandial blood glucose by Banaba extract capsule enriched corosolic acid

Journal for the Integrated Study of Dietary Habits ◽

10.2740/jisdh.17.255 ◽

2006 ◽

Vol 17 (3) ◽

pp. 255-259 ◽

Cited By ~ 8

Author(s):

Satomi Tsuchibe ◽

Seigo Kataumi ◽

Masaki Mori ◽

Haruki Mori

Keyword(s):

Blood Glucose ◽

Inhibitory Effect ◽

Postprandial Blood Glucose ◽

Corosolic Acid

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Inhibitory Effect of the Stem Bark Extracts of Albizia chevalieri Harms on the Activity of Alpha-glucosidase Obtained from Aspergillus niger

European Journal of Medicinal Plants ◽

10.9734/ejmp/2019/v27i230107 ◽

2019 ◽

pp. 1-10

Author(s):

Abdulhafiz Damilola Oso ◽

Idris Bello ◽

Yusuf Sa’idu ◽

Onu Andrew

Keyword(s):

Ethyl Acetate ◽

Competitive Inhibition ◽

Stem Bark ◽

Inhibitory Effect ◽

Acetate Buffer ◽

Bark Extract ◽

Methanol Extracts ◽

Glucosidase Activity ◽

Alpha Glucosidase

The aim of the current study is to evaluate the inhibition of α-glucosidase activity by stem bark extract of Albizia chevalieri. The activity of alpha glucosidase was assayed in vitro using 50 mM acetate buffer pH 6.0 (prepared from acetic acid and sodium acetate) and various concentration of maltose (0.5 mM to 10 mM). Five test tubes, labeled TA – TE, each containing 1.5 ml of acetate buffer, 0.5 ml of alpha glucosidase and 0.5 ml of a known concentration of plant extract and control tubes (CA – CE) were assessed for Alpha glucosidase activity. The results showed that hexane, ethyl acetate and methanol extracts inhibited α-glucosidase activity. The results further indicated that the extracts act by competitive inhibition with inhibition constant of 232 mg/ml, 157 mg/ml and 67 mg/ml for hexane, ethyl acetate and methanol extracts, respectively. The value for the inhibition constants shows that there is a strong binding of the enzyme to the inhibitor as the polarity of solvent increases. The inhibitory activity of Albizia chevalieri may be due one or more of the phytochemicals present in the extracts.

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Inhibitory Effect of Tangeretin and Cardamonin on Human Intestinal SGLT1 Activity In Vitro and Blood Glucose Levels in Mice In Vivo

Nutrients ◽

10.3390/nu13103382 ◽

2021 ◽

Vol 13 (10) ◽

pp. 3382

Author(s):

Hideo Satsu ◽

Ryosuke Shibata ◽

Hiroto Suzuki ◽

Shimon Kimura ◽

Makoto Shimizu

Keyword(s):

Blood Glucose ◽

Inhibitory Effect ◽

Postprandial Blood Glucose ◽

Oral Glucose ◽

Glucose Levels ◽

Blood Glucose Levels ◽

Blood Glucose Elevation ◽

Lifestyle Related Diseases

Rapid postprandial blood glucose elevation can cause lifestyle-related diseases, such as type II diabetes. The absorption of food-derived glucose is primarily mediated by sodium/glucose cotransporter 1 (SGLT1). Moderate SGLT1 inhibition can help attenuate postprandial blood glucose elevation and prevent lifestyle-related diseases. In this study, we established a CHO cell line stably expressing human SGLT1 and examined the effects of phytochemicals on SGLT1 activity. Among the 50 phytochemicals assessed, tangeretin and cardamonin inhibited SGLT1 activity. Tangeretin and cardamonin did not affect the uptake of L-leucine, L-glutamate, and glycyl-sarcosine. Tangeretin, but not cardamonin, inhibited fructose uptake, suggesting that the inhibitory effect of tangeretin was specific to the monosaccharide transporter, whereas that of cardamonin was specific to SGLT1. Kinetic analysis suggested that the suppression of SGLT1 activity by tangeretin was associated with a reduction in Vmax and an increase in Km, whereas suppression by cardamonin was associated with a reduction in Vmax and no change in Km. Oral glucose tolerance tests in mice showed that tangeretin and cardamonin significantly suppressed the rapid increase in blood glucose levels. In conclusion, tangeretin and cardamonin were shown to inhibit SGLT1 activity in vitro and lower blood glucose level in vivo.

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Nitric oxide, islet acid glucan-1,4-alpha-glucosidase activity and nutrient-stimulated insulin secretion

Journal of Endocrinology ◽

10.1677/joe.0.1650293 ◽

2000 ◽

Vol 165 (2) ◽

pp. 293-300 ◽

Cited By ~ 3

Author(s):

H Mosen ◽

A Salehi ◽

I Lundquist

Keyword(s):

Nitric Oxide ◽

Insulin Secretion ◽

Insulin Release ◽

Lysosomal Enzymes ◽

Inhibitory Effect ◽

Isolated Islets ◽

No Production ◽

No Donor ◽

Glucosidase Activity ◽

Alpha Glucosidase

The mechanism of nutrient-evoked insulin release is clearly complex. One part of that mechanism is postulated to be the activation of the glycogenolytic enzyme acid glucan-1,4-alpha-glucosidase. As nitric oxide (NO) has been found to be a potent inhibitor of glucose-stimulated insulin secretion, we have now investigated a possible influence of exogenous NO and inhibition of endogenous NO production on islet acid glucan-1,4-alpha-glucosidase activity in relation to insulin release stimulated by glucose and l-arginine. In isolated islets, NO derived from the intracellular NO donor hydroxylamine inhibited the activation of acid glucan-1, 4-alpha-glucosidase and its isoform acid alpha-glucosidase in parallel with inhibition of glucose-stimulated insulin release. In comparison, other lysosomal enzymes were largely unaffected. Similarly, the spontaneous NO donor sodium nitroprusside, as well as NO gas, when added to islet homogenates, suppressed the activities of these acid alpha-glucosidehydrolases and, to a lesser extent, the activities of other lysosomal enzymes. Finally, in the presence of the NO synthase inhibitor N(G)-nitro-l-arginine methyl ester, insulin release from isolated islets stimulated by glucose or l-arginine was markedly potentiated in parallel with an accompanying increase in the activities of acid glucan-1,4-alpha-glucosidase and acid alpha-glucosidase. Other lysosomal enzymes and neutral alpha-glucosidase were not influenced. We propose that an important inhibitory effect of NO on the insulin secretory processes stimulated by glucose and l-arginine is exerted via inactivation of islet acid glucan-1,4-alpha-glucosidase, a putative key enzyme in nutrient-stimulated insulin release.

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