α-Glucosidase and α-amylase inhibitors from Myrcia spp.: a stronger alternative to acarbose?

Figueiredo-González, María; Grosso, Clara; Valentão, Patrı́cia; Andrade, Paula B.

doi:10.1016/j.jpba.2015.10.042

Cited by 71 publications

(34 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Most of the studied plant samples were potent inhibitors of α-glucosidase, showing higher acarbose equivalent values, compared to α-amylase inhibition. Indeed, mild α-amylase inhibition versus marked α-glucosidase inhibition was requested, since a pronounced activity of the former enzyme advocated the event of gastrointestinal problems [ 30 ]. Specifically, the roots of flowering AL collected in Novele showed high α-glucosidase inhibitory activity and low inhibition against α-amylase.…”

Section: Discussionmentioning

confidence: 99%

A Comparative Assessment of Biological Effects and Chemical Profile of Italian Asphodeline lutea Extracts

Melucci

Locatelli

et al. 2018

Molecules

View full text Add to dashboard Cite

The present study aims to highlight the therapeutic potential of Asphodeline lutea (AL), a wild edible plant of the Mediterranean diet. Roots, aerial parts, and flowers of AL at two different phenological stages were collected from three locations in Italy. The inhibitory activities of extracts on strategic enzymes linked to human diseases were assessed. The antioxidant properties were evaluated in vitro, using six standard bioassays. The phenolic and anthraquinone profiles were also established using HPLC-PDA. Zinc, cadmium, lead, and copper contents were also determined. All the samples inhibited acetylcholinesterase (from 1.51 to 2.20 mg GALAEs/g extract), tyrosinase (from 7.50 to 25.3 mg KAEs/g extract), and α-amylase (from 0.37 to 0.51 mmol ACAEs/g extract). Aloe-emodin and physcion were present in all parts, while rhein was not detected. The phenolic profile and the heavy metals composition of specimens gathered from three different regions of Italy were different. It can be argued that samples collected near the street can contain higher concentrations of heavy metals. The experimental data confirm that the A. lutea species could be considered as a potential source of bioactive metabolites, and its consumption could play a positive and safe role in human health maintenance.

show abstract

Section: Discussionmentioning

confidence: 99%

A Comparative Assessment of Biological Effects and Chemical Profile of Italian Asphodeline lutea Extracts

Melucci

Locatelli

et al. 2018

Molecules

View full text Add to dashboard Cite

show abstract

“…Trilobatin also exhibits anti-hyperglycemic properties by accelerating liver glycogen synthesis, decreasing oxidative stress, increasing the expression of glucokinase, and up-regulating the expression of insulin receptor substrate (IRS) on long-term double high-fat diet and streptozotocin (STZ) induced type 2 diabetic mice [13]. Similar to other dihydrochalcones, phlorizin (a dual SGLT1/SGLT2 inhibitor) [14], phloretin (a GLUT2 inhibitor) [15], and acarbose (an alpha-glucosidase inhibitor) [16,17], our previous works demonstrated that trilobatin could be bind with SGLT1/2 [18]. But up to now, the effect of trilobatin on insulin resistance is still needed to be identified.…”

Section: Introductionmentioning

confidence: 99%

Trilobatin ameliorates insulin resistance through IRS-AKT-GLUT4 signaling pathway in C2C12 myotubes and ob/ob mice

Liu

Wang

et al. 2020

Chin Med

View full text Add to dashboard Cite

Background Trilobatin, a natural compound, has been found to exhibit anti-diabetic properties in high-fat diet (HFD) and streptozotocin (STZ) induced type 2 diabetic mice. But up to now no research has been reported on the effect of trilobatin on insulin resistance in peripheral tissues. Herein, we determined the effects of trilobatin on insulin resistance in palmitate-treated C2C12 myotubes and ob/ob mice. Methods Male ob/ob mice (8-10 weeks) and same background C57BL/6 mice were used to evaluate the role of trilobatin on insulin resistance; protein expression and phosphorylation were measured by western blot; glucose uptake was determined a fluorescent test. Results Treatment with trilobatin prevented palmitate-induced insulin resistance by enhancing glucose uptake and the phosphorylation of insulin resistance substrate 1 (IRS1) and protein Kinase B, (PKB/AKT), recovered the translocation of GLUT4 from cytoplasm to membrane, but preincubation with LY294002, an inhibitor of PI3K, blocked the effects of trilobatin on glucose uptake and the distribution of GLUT4 in C2C12 myotubes. Furthermore, administration with trilobatin for 4 weeks significantly improved insulin resistance by decreasing fasting blood glucose and insulin in serum, enhancing the phosphorylation of IRS1 and AKT, and recovering the expression and translocation of GLUT4 in ob/ob mice. Conclusions IRS-AKT-GLUT4 signaling pathway might be involved in trilobatin ameliorating insulin resistance in skeletal muscle of obese animal models.

show abstract

“…[17] Therefore, a compound with dual inhibition may elicit its pharmacological effects while minimizing its side effects. [18] The results presented here indicate that compound 1 is a promising α-amylase and α-glucosidase inhibitor for Figure S1). Figure 3.…”

Section: Discussionmentioning

confidence: 69%

Molecular Insight and Mode of Inhibition of α‐Glucosidase and α‐Amylase by Pahangensin A from Alpinia pahangensisRidl.

Loo

Leong

Sivasothy

et al. 2019

Chemistry & Biodiversity

View full text Add to dashboard Cite

The inhibition of carbohydrate‐hydrolyzing enzymes in human digestive organs is crucial in controlling blood sugar levels, which is important in treating type 2 diabetes. In the current study, pahangensin A (1), a bis‐labdanic diterpene characterized previously in the rhizomes of Alpinia pahangensis Ridl., was identified as an active dual inhibitor for α‐amylase (IC50=114.80 μm) and α‐glucosidase (IC50=153.87 μm). This is the first report on the dual α‐amylase and α‐glucosidase inhibitory activities of a bis‐labdanic diterpene. The Lineweaver‐Burk plots of compound 1 indicate that it is a mixed‐type inhibitor with regard to both enzymes. Based on molecular docking studies, compound 1 docked in a non‐active site of both enzymes. The dual inhibitory activity of compound 1 makes it a suitable natural alternative in the treatment of type 2 diabetes.

show abstract

α-Glucosidase and α-amylase inhibitors from Myrcia spp.: a stronger alternative to acarbose?

Cited by 71 publications

References 18 publications

A Comparative Assessment of Biological Effects and Chemical Profile of Italian Asphodeline lutea Extracts

A Comparative Assessment of Biological Effects and Chemical Profile of Italian Asphodeline lutea Extracts

Trilobatin ameliorates insulin resistance through IRS-AKT-GLUT4 signaling pathway in C2C12 myotubes and ob/ob mice

Molecular Insight and Mode of Inhibition of α‐Glucosidase and α‐Amylase by Pahangensin A from Alpinia pahangensisRidl.

Contact Info

Product

Resources

About