Keyword search (3,448 papers available)


Flavanone glycosides inhibit β-site amyloid precursor protein cleaving enzyme 1 and cholinesterase and reduce Aβ aggregation in the amyloidogenic pathway.

Author(s): Ali MY, Jannat S, Edraki N, Das S, Chang WK, Kim HC, Park SK, Chang MS

Chem Biol Interact. 2019 Jun 10;: Authors: Ali MY, Jannat S, Edraki N, Das S, Chang WK, Kim HC, Park SK, Chang MS

Article GUID: 31194956
Kinetics and molecular docking of dihydroxanthyletin-type coumarins from Angelica decursiva that inhibit cholinesterase and BACE1.

Author(s): Ali MY, Seong SH, Jung HA, Jannat S, Choi JS

Arch Pharm Res. 2018 Jul;41(7):753-764 Authors: Ali MY, Seong SH, Jung HA, Jannat S, Choi JS

Article GUID: 30047040
Inhibition of β-site amyloid precursor protein cleaving enzyme 1 and cholinesterases by pterosins via a specific structure-activity relationship with a strong BBB permeability.

Author(s): Jannat S, Balupuri A, Ali MY, Hong SS, Choi CW, Choi YH, Ku JM, Kim WJ, Leem JY, Kim JE, Shrestha AC, Ham HN, Lee KH, Kim DM, Kang NS, Park GH

Exp Mol Med. 2019 02 12;51(2):12 Authors: Jannat S, Balupuri A, Ali MY, Hong SS, Choi CW, Choi YH, Ku JM, Kim WJ, Leem JY, Kim JE, Shrestha AC, Ham HN, Lee KH, Kim DM, Kang NS, Park GH

Article GUID: 30755593
Didymin, a dietary citrus flavonoid exhibits anti-diabetic complications and promotes glucose uptake through the activation of PI3K/Akt signaling pathway in insulin-resistant HepG2 cells.

Author(s): Ali MY, Zaib S, Rahman MM, Jannat S, Iqbal J, Park SK, Chang MS

Chem Biol Interact. 2019 May 25;305:180-194 Authors: Ali MY, Zaib S, Rahman MM, Jannat S, Iqbal J, Park SK, Chang MS

Article GUID: 30928401
Title:Didymin, a dietary citrus flavonoid exhibits anti-diabetic complications and promotes glucose uptake through the activation of PI3K/Akt signaling pathway in insulin-resistant HepG2 cells.
Authors:Ali MY,  Zaib S,  Rahman MM,  Jannat S,  Iqbal J,  Park SK,  Chang MS
Link:https://www.ncbi.nlm.nih.gov/pubmed/30928401?dopt=Abstract
Category:Chem Biol Interact
PMID:30928401
Dept Affiliation: CHEMBIOCHEM
1 Department of Chemistry and Biochemistry, Faculty of Arts and Science, Concordia University, 7141 Sherbrooke St. W., Montreal, Quebec, Canada; Department of Biology, Faculty of Arts and Science, Concordia University, 7141 Sherbrooke St. W., Montreal, Quebec, Canada; Centre for Structural and Functional Genomic, Dept. of Biology, Faculty of Arts and Science, Concordia University, 7141 Sherbrooke St. W., Montreal, QC, Canada; Department of Prescriptionology, College of Korean Medicine, Kyung Hee University, 26, Kyunghee Dae-ro, Dongdaemun-gu, Seoul, 02447, Republic of Korea. Electronic address: mdyousof.ali@concordia.ca.
2 Centre for Advanced Drug Research, COMSATS University Islamabad, Abbottabad Campus, Abbottabad, 22060, Pakistan.
3 Department of Biotechnology and Genetic Engineering, Islamic University, Kushtia, 7003, Bangladesh.
4 Department of Biochemistry and Molecular Biology, College of Medicine, Korea Molecular Medicine and Nutrition Research Institute, Korea University, Seoul, 02841, Republic of Korea.
5 Department of Prescriptionology, College of Korean Medicine, Kyung Hee University, 26, Kyunghee Dae-ro, Dongdaemun-gu, Seoul, 02447, Republic of Korea.

Description:

Didymin, a dietary citrus flavonoid exhibits anti-diabetic complications and promotes glucose uptake through the activation of PI3K/Akt signaling pathway in insulin-resistant HepG2 cells.

Chem Biol Interact. 2019 May 25;305:180-194

Authors: Ali MY, Zaib S, Rahman MM, Jannat S, Iqbal J, Park SK, Chang MS

Abstract

Didymin is a naturally occurring orally active flavonoid glycoside (isosakuranetin 7-O-rutinoside) found in various citrus fruits, which has been previously reported to possess a wide variety of pharmacological activities including anticancer, antioxidant, antinociceptive, neuroprotective, hepatoprotective, inflammatory, and cardiovascular. However, there have not been any reports concerning its anti-diabetic potential until now. Therefore, we evaluated the anti-diabetic potential of didymin via inhibition of a-glucosidase, protein tyrosine phosphatase 1B (PTP1B), rat lens aldose reductase (RLAR), human recombinant AR (HRAR), and advanced glycation end-product (AGE) formation inhibitory assays. Didymin strongly inhibited PTP1B, a-glucosidase, HRAR, RLAR, and AGE in the corresponding assays. Kinetic study revealed that didymin exhibited a mixed type inhibition against a-glucosidase and HRAR, while it competitively inhibited PTP1B and RLAR. Docking simulations of didymin demonstrated negative binding energies and close proximity to residues in the binding pocket of HRAR, RLAR, PTP1B and a-glucosidase, indicating that didymin have high affinity and tight binding capacity towards the active site of these enzymes. Furthermore, we also examined the molecular mechanisms underlying the anti-diabetic effects of didymin in insulin-resistant HepG2 cells which significantly increased glucose uptake and decreased the expression of PTP1B in insulin-resistant HepG2 cells. In addition, didymin activated insulin receptor substrate (IRS)-1 by increasing phosphorylation at tyrosine 895 and enhanced the phosphorylations of phosphoinositide 3-kinase (PI3K), Akt, and glycogen synthasekinase-3(GSK-3). Interestingly, didymin reduced the expression of phosphoenolpyruvate carboxykinase and glucose 6-phosphatase, two key enzymes involved in the gluconeogenesis and leading to a diminished glucose production. The results of the present study clearly demonstrated that didymin will be useful for developing multiple target-oriented therapeutic modalities for treatment of diabetes, and diabetes-associated complications.

PMID: 30928401 [PubMed - indexed for MEDLINE]