ArticlePloS one2022
Annona muricata L. peel extract inhibits carbohydrate metabolizing enzymes and reduces pancreatic β-cells, inflammation, and apoptosis via upregulation of PI3K/AKT genes.
Article in PloS one, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 21 citations in OpenAlex.
- Bioprospection of indigenous herbal formulations for diabetes care: in vitro, network pharmacology, and molecular dynamics studies.BMC complementary medicine and therapies · 2025Article
- Optimization of Controlled-Release Microspheres Containing Vitexin and Isovitexin Through Experimental Design and Evaluation of Their Hypoglycemic Effects.Pharmaceutics · 2025Article
- Leveraging Underutilized Sri Lankan Fruits in the Fight against Autoimmune Disorders.Anti-inflammatory & anti-allergy agents in medicinal chemistry · 2025Review
- Comprehensive review of opportunities and challenges of ethnomedicinal plants for managing type 2 diabetes.Heliyon · 2024Review
- Soursop (Foods (Basel, Switzerland) · 2023Review
- Review
- Role of ceramides in diabetic foot ulcers (Review).International journal of molecular medicine · 2023Review
- Onopordum acanthium L. extract attenuates pancreatic β-Cells and cardiac inflammation in streptozocin-induced diabetic rats.PloS one · 2023Article
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Authors and funding
9 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
BACKGROUND AND
objectiveAnnona muricata L. peel has been recognized for many ethnobotanical uses, including diabetes management. However, limited detailed scientific information about its mechanism of antidiabetic activity exists. The objective of this study was to evaluate the anti-diabetic properties of an aqueous extract of A. muricata peel (AEAMP) and its mechanism of action on alloxan-induced diabetic rats.
methodsIn vitro antidiabetic assays, such as α-amylase and α-glucosidase were analyzed on AEAMP. Alloxan monohydrate (150 mg/kg b.w) was used to induce diabetes in the rats. 150 mg/kg b.w positive control group doses of 6.67, 13.53, and 27.06 mg/kg were administered to 3 groups for twenty-one days. The positive control group was administered 30 mg/kg of metformin. The negative and normal control groups were administered distilled water. The fasting blood glucose, serum insulin, lipid profile, inflammatory cytokines, antioxidant markers, carbohydrate metabolizing enzymes, and liver glycogen were analyzed as well as PI3K/AKT and apoptotic markers PCNA and Bcl2 by RT-PCR.
resultsAEAMP inhibited α-amylase and α-glucosidase enzymes more effectively than acarbose. AEAMP reduced FBG levels, HOMA-IR, G6P, F-1,6-BP, MDA, TG, TC, AI, CRI, IL-6, TNF-α, and NF-κB in diabetic rats. Furthermore, in diabetic rats, AEAMP improved serum insulin levels, HOMA-β, hexokinase, CAT, GST, and HDL-c. Liver PI3K, liver PCNA and pancreas PCNA were not significantly different in untreated diabetic rats when compared to normal rats suggesting alloxan induction of diabetes did not downregulate the mRNA expression of these genes. AEAMP significantly up-regulated expression of AKT and Bcl2 in the liver and pancreatic tissue. It is interesting that luteolin and resorcinol were among the constituents of AEAMP.
conclusionsAEAMP can improve β-cell dysfunction by upregulating liver AKT and pancreatic PI3K and AKT genes, inhibiting carbohydrate metabolizing enzymes and preventing apoptosis by upregulating liver and pancreatic Bcl2. However, the potential limitation of this study is the unavailability of equipment and techniques for collecting more data for the study.
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