scholarly journals Inhibitory Effect of the Leaf of Psidium guajava Grown in Vietnam on α-Glucosidase and Protein Tyrosine Phosphatase 1B in vitro

2019 ◽  
Vol 35 (1) ◽  
Author(s):  
Dang Kim Thu ◽  
Le Thi Thu Huong ◽  
Tran Trong Nghia ◽  
Bui Thanh Tung
Keyword(s):  
Type 2 Diabetes ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Psidium Guajava ◽  
Inhibitory Effect ◽  
Diabetic Rats ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine

Type 2 diabetes is a fairly common chronic disease. α-glucosidase and protein tyrosine phosphatase, as enzymes, play an important role in type 2 diabetes. This study evaluates the inhibitory effect of the two enzymes in vitro of ethanol extract and fractions of Vietnam Psidium guajava’s leaves. The leaves were collected, dried and extracted with 96% ethanol and successively fractionated with n-hexane, ethyl acetate and butanol solvents. The results show that the EtOH extract, n-nexan, EtOAc and BuOH fractions had high α-glucosidase inhibitory effect with IC50 values ​​of 2.20; 2.53; 2.24 and 2.16 µg/mL, respectively. In addition, EtOAc and BuOH fractions also show strong inhibitory PTP1B effect with IC50 at 120.22 mg/mL and 97.72 mg/mL, respectively. The study results show that Psidium guajava leaves are a potential source of material to inhibit α-glucosidase and PTP1B in the treatment of diabetes. Keywords Psidium guajava, α-glucosidase, protein tyrosine phosphatase 1B, diabetes, extraction. References [1] A. Chaudhury, C. Duvoor, R. Dendi, V. Sena, S. Kraleti, A. Chada, et al. Clinical review of antidiabetic drugs: Implications for type 2 diabetes mellitus management, Frontiers in endocrinology. 8 (2017) 6.[2] F.A. Van de Laar, P.L. Lucassen, R.P. Akkermans, E. H. Van de Lisdonk, G.E. Rutten,C. Van, Alpha - glucosidase inhibitors for type 2 diabetes mellitus. The Cochrane Library (2005).[3] J. Montalibet, B.P. Kennedy. Therapeutic strategies for targeting PTP1B in diabetes. Drug Discovery Today: Therapeutic Strategies 2(2) (2005) 129.[4] S.M. Barbalho, Farinazzi-Machado, R. De Alvares Goulart, A.C.S. Brunnati, A. Otoboni, B. Ottoboni. Psidium guajava (Guava): A plant of multipurpose medicinal applications, Med Aromat Plants. 1(104) (2012) 2167.[5] R.M.P. Gutiérrez, S. Mitchell, Solis R. V. Psidium guajava: a review of its traditional uses, phytochemistry and pharmacology. Journal of ethnopharmacology 117(1) (2008) 1.[6] B. T. Tùng, Đ.K. Thu, P.T. Hải, N.T. Hải. Đánh giá tác dụng ức chế enzym α-glucosidase của các phân đoạn dịch chiết quả Lựu (Punica granatum Linn), Tạp chí Y Dược cổ truyền Việt Nam. 5(18) (2018) 59.[7] P.H. Nguyen, J.L. Yang, M.N. Uddin, S.L. Park, S.I. Lim, D.W. Jung, et al. Protein tyrosine phosphatase 1B (PTP1B) inhibitors from Morinda citrifolia (Noni) and their insulin mimetic activity, Journal of natural products. 76(11) (2013) 2080.[8] H.B.H. Khan, D. Rajendran, M.R. Bai, Sorimuthu S. Protective effect of Psidium guajava leaf extract on altered carbohydrate metabolism in streptozotocin-induced diabetic rats, Journal of dietary supplements. 10(4) (2013) 335.[9] H. Mukhtar, S. Ansari, M. Ali, T. Naved, Z. Bhat Effect of water extract of Psidium guajava leaves on alloxan-induced diabetic rats. Die Pharmazie-An International Journal of Pharmaceutical Sciences. 59(9) (2004) 734.[10] W. K. Oh, C. H. Lee, M. S. Lee, E. Y. Bae, C. B. Sohn, H. Oh, et al. Antidiabetic effects of extracts from Psidium guajava, Journal of ethnopharmacology. 96(3) (2005) 411.[11] B. Wang, H. Liu, J. Hong, H. Li, C. Huang, Effect of Psidium guajava leaf extract on alpha-glucosidase activity in small intestine of diabetic mouse. Sichuan da xue xue bao Yi xue ban, Journal of Sichuan University Medical science edition. 38(2) (2007) 298.[12] S. C. Shen, F. C. Cheng, N. J. Wu. Effect of guava (Psidium guajava Linn.) leaf soluble solids on glucose metabolism in type 2 diabetic rats, Phytotherapy Research. 22(11) (2008) 1458.      

scholarly journals Inhibitory Effects of Secondary Metabolites from the Lichen Stereocaulon evolutum on Protein Tyrosine Phosphatase 1B

Planta Medica ◽  
2021 ◽  
Author(s):  
Birgit Waltenberger ◽  
Françoise Lohézic-Le Dévéhat ◽  
Thi Huyen Vu ◽  
Olivier Delalande ◽  
Claudia Lalli ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Inhibitory Activity ◽  
Tyrosine Phosphatase ◽  
Inhibitory Effect ◽  
Positive Control ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine ◽  
Ic50 Values ◽  
A Cell

AbstractProtein tyrosine phosphatase 1B plays a significant role in type 2 diabetes mellitus and other diseases and is therefore considered a new drug target. Within this study, an acetone extract from the lichen Stereocaulon evolutum was identified to possess strong protein tyrosine phosphatase 1B inhibition in a cell-free assay (IC50 of 11.8 µg/mL). Fractionation of this bioactive extract led to the isolation of seven known molecules belonging to the depsidones and the related diphenylethers and one new natural product, i.e., 3-butyl-3,7-dihydroxy-5-methoxy-1(3H)-isobenzofurane. The isolated compounds were evaluated for their inhibition of protein tyrosine phosphatase 1B. Two depsidones, lobaric acid and norlobaric acid, and the diphenylether anhydrosakisacaulon A potently inhibited protein tyrosine phosphatase 1B with IC50 values of 12.9, 15.1, and 16.1 µM, respectively, which is in the range of the protein tyrosine phosphatase 1B inhibitory activity of the positive control ursolic acid (IC50 of 14.4 µM). Molecular simulations performed on the eight compounds showed that i) a contact between the molecule and the four main regions of the protein is required for inhibitory activity, ii) the relative rigidity of the depsidones lobaric acid and norlobaric acid and the reactivity related to hydrogen bond donors or acceptors, which interact with protein tyrosine phosphatase 1B key amino acids, are involved in the bioactivity on protein tyrosine phosphatase 1B, iii) the cycle opening observed for diphenylethers decreased the inhibition, except for anhydrosakisacaulon A where its double bond on C-8 offsets this loss of activity, iv) the function present at C-8 is a determinant for the inhibitory effect on protein tyrosine phosphatase 1B, and v) the more hydrogen bonds with Arg221 there are, the more anchorage is favored.

scholarly journals Association of Protein Tyrosine Phosphatase 1B Gene Polymorphisms With Type 2 Diabetes

Diabetes ◽  
2004 ◽  
Vol 53 (11) ◽  
pp. 3007-3012 ◽  
Author(s):  
J. L. Bento ◽  
N. D. Palmer ◽  
J. C. Mychaleckyj ◽  
L. A. Lange ◽  
C. D. Langefeld ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Protein Tyrosine Phosphatase ◽  
Gene Polymorphisms ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine

scholarly journals Association Testing of the Protein Tyrosine Phosphatase 1B Gene (PTPN1) With Type 2 Diabetes in 7,883 People

Diabetes ◽  
2005 ◽  
Vol 54 (6) ◽  
pp. 1884-1891 ◽  
Author(s):  
J. C. Florez ◽  
C. M. Agapakis ◽  
N. P. Burtt ◽  
M. Sun ◽  
P. Almgren ◽  
...  
Keyword(s):  
Type 2 Diabetes ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine ◽  
Association Testing

scholarly journals PROTEIN TYROSINE PHOSPHATASE 1B (PTP1B) IN OBESITY AND TYPE 2 DIABETES

2009 ◽  
Vol 38 (1) ◽  
pp. 2-7 ◽  
Author(s):  
Mirela Delibegovic ◽  
Nimesh Mody
Keyword(s):  
Type 2 Diabetes ◽  
Insulin Sensitivity ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Developed Countries ◽  
Protein Tyrosine Phosphatase 1B ◽  
Protein Tyrosine ◽  
The Developed Countries

Increased incidence in obesity is reaching epidemic proportions and is placing a major burden on the healthcare systems in the developed countries. Obesity is a major risk factor for the development of type 2 diabetes, metabolic syndrome, cardiovascular disease and cancer. Thus, the search for molecules that regulate the development of obesity and its associated pathologies is ongoing. Protein tyrosine phosphatase 1B (PTP1B) has been found to be a major regulator of body fat stores, energy balance, and insulin sensitivity in vivo. Increased expression of PTP1B is associated with insulin resistance in rodents and humans and deletion of PTP1B leads to leanness and insulin sensitivity in rodents, suggesting that PTP1B may be a very attractive molecular target for anti-obesity, anti-diabetic agents.

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