Pharmacognosy Magazine

ORIGINAL ARTICLE
Year
: 2017  |  Volume : 13  |  Issue : 51  |  Page : 676--683

Inhibition of glycation-induced cytotoxicity, protein glycation, and activity of proteolytic enzymes by extract from Perovskia atriplicifolia Roots


Mehran Miroliaei1, Akram Aminjafari1, Sylwester Ślusarczyk2, Izabela Nawrot-Hadzik3, Mehdi Rahimmalek4, Adam Matkowski3 
1 Department of Biology, Division of Biochemistry, Cell and Molecular Biology, University of Isfahan, Isfahan, Iran
2 Department of Pharmaceutical Biology and Botanical Garden of Medicinal Plants, Wroclaw Medical University, Wrocław; Department of Crop Biochemistry, Institute of Soil Science and Plant Cultivation (IUNG), Pulawy, Poland
3 Department of Pharmaceutical Biology and Botanical Garden of Medicinal Plants, Wroclaw Medical University, Wrocław, Poland
4 Department of Agronomy and Plant Breeding, College of Agriculture, Isfahan University of Technology, Isfahan, Iran

Correspondence Address:
Adam Matkowski
Department of Pharmaceutical Biology and Botanical Garden of Medicinal Plants, Wroclaw Medical University, Wrocław
Poland

Background: Protein glycation and glycotoxicity belong to the main oxidative-stress related complications in diabetes. Perovskia species are used in Asian folk medicine as antidiabetic herbs. Objective: The aim of this study was to verify the ability of the methanolic extract from Perovskia atriplicifolia Benth. roots to diminish glycation of albumin and to prevent cell damage in vitro. Furthermore, we tested the extract for in vitro antioxidant activity and inhibition of elastase and collagenase. Material and Methods: The aqueous methanol extract was analyzed by UHPLC-MS for the content of polyphenols and terpenoids. The prevention of glycated albumin-induced cell damage was tested in four mammalian cell lines (peripheral blood mononuclear cells, human embryonic kidney cells – HEK293, normal human fibroblasts, and Chinese hamster ovary cells) with the 5-(3-carboxymethoxyphenyl)-2-(4,5-dimethylthiazoly)-3-(4-sulfophenyl) tetrazolium assay. Results: Glycated albumin is significantly more toxic than native human serum albumin (LC50from 35.00 to 48.34 μ g/mL vs. 5.47–9.10 μ g/mL, respectively). The extract, rich in rosmarinic acid (344.27 mg/g dry mass), mitigated the glycated albumin toxicity, and increased glycated albumin-treated cell survival by more than 50%. The inhibition of advanced glycation endproduct formation was confirmed by monitoring conformational changes. The free radical scavenging activity was higher than Trolox and metal reducing power was one-third to half that of ascorbic acid. The activity of elastase and collagenase was inhibited by 54.75% ± 6.87% and 60.03% ± 7.22%, respectively. Conclusions: The results confirm antiglycative and antiglycotoxic potential of Perovskia root and its traditional antidiabetic use. The high activity can be attributed to rosmarinic acid abundance. Abbreviations used: AGE: advanced glycation end-products; DPPH: 2,2-diphenyl-1-picrylhydrazyl; HSA: human serum albumin.


How to cite this article:
Miroliaei M, Aminjafari A, Ślusarczyk S, Nawrot-Hadzik I, Rahimmalek M, Matkowski A. Inhibition of glycation-induced cytotoxicity, protein glycation, and activity of proteolytic enzymes by extract from Perovskia atriplicifolia Roots.Phcog Mag 2017;13:676-683


How to cite this URL:
Miroliaei M, Aminjafari A, Ślusarczyk S, Nawrot-Hadzik I, Rahimmalek M, Matkowski A. Inhibition of glycation-induced cytotoxicity, protein glycation, and activity of proteolytic enzymes by extract from Perovskia atriplicifolia Roots. Phcog Mag [serial online] 2017 [cited 2022 Dec 8 ];13:676-683
Available from: http://www.phcog.com/article.asp?issn=0973-1296;year=2017;volume=13;issue=51;spage=676;epage=683;aulast=Miroliaei;type=0