The leaves of Mangifera indica were assessed for antidiabetic properties using normoglycaemic, glucose-induced hyperglycaemia and streptozotocin (STZ) induced diabetic mice. The aqueous extract produced a reduction of blood glucose level in normoglycaemic and glucose-induced hyperglycaemia, but did not have any effect on streptozotocin-induced diabetic mice. The hypoglycaemic effect of the aqueous extract was compared with that of an oral dose of chlorpropamide under the same conditions. The results of this study indicate that the aqueous extract of the leaves of Mangifera indica possess hypoglycaemic activity.

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The leaves of Mangifera indica are used as an antidiabetic agent in Nigerian folk medicine. To determine whether or not there is a scientific basis for this use, the effect of the aqueous extract of the leaves on blood glucose level was assessed in normoglycaemic, glucose - induced hyperglycaemic and streptozotocin (STZ)-induced diabetic rats. The aqueous extract given orally (1 g/kg) did not alter the blood glucose levels in either normoglycaemic or STZ-induced diabetic rats. In glucose - induced hyperglycaemia, however, antidiabetic activity was seen when the extract and glucose were administered simultaneously and also when the extract was given to the rats 60 min before the glucose. The hypoglycaemic effect of the aqueous extract was compared with that of an oral dose of chlorpropamide (200 mg/kg) under the same conditions. The results of this study indicate that the aqueous extract of the leaves of Mangifera indica possess hypoglycaemic activity. This action may be due to an intestinal reduction of the absorption of glucose. However, other different mechanisms of action cannot be excluded.

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Purpose: To investigate the in vitro anticholinesterase, α-glucosidase and antioxidant activities of α-spinasterol isolated from Acacia auriculiformis leaves.Methods: The powdered leaves of Acacia auriculiformis were extracted with 70 % ethanol and the dried hydroalcoholic extract was suspended in water and partitioned with ethyl acetate and n-butanol to give their soluble fractions. The in vitro inhibitory activities of α-spinasterol were determined against cholinesterase and, α-glucosidase enzymes, and free radical scavenging potentials using (1,1-diphenyl-2-picrylhydarzyl (DPPH) and 2,2-azino-bis (3-Ethylbenzothiazoline-6-sulphonic acid (ABTS) antioxidantassays.Results: The compound, α-spinasterol, exhibited moderate anticholinesterase activity (IC50 value of 44.19±2.59 μg/mL which was significantly  different at (p < 0.05) when compared to the standard galanthamine (IC50 value of 1.73 ± 1.10 μg/mL). It also displayed a good α-glucosidase  inhibitory activity with IC``` value of 8.65 ± 1.71μg/mL which was not significantly different when compared to the standard, acarbose with IC50 value of 2.79±0.81 μg/mL. This compound, however, exhibited weak free radical scavenging activities at 26.93 ± 0.00 and 35.16 ±.0.26 % inhibition of DPPH+ and ABTS+ radicals as compared to ascorbic acid and Trolox (73.88 ± 0.04 and 99.82 ± 0.00%) respectively.Conclusion: The results show that α-spinasterol isolated from Acacia auriculiformis exerts potent inhibitory effect against cholinesterase enzyme which might serve as a lead in the search for drugs against Alzheimer disease and diabetes mellitus. Keywords: Acacia auriculiformis, α-Spinasterol, Galanthamine, Acarbose, Trolox, Ascorbic acid

Background: The decoctions of the bark of Acacia auriculiformis are used in folkloric medicine to relieve pain and inflammation and as remedy for cancer. Objective: The aim of this work is to screen the extract and fractions of Acacia auriculiformis for protein kinase inhibitory activity and also to isolate and characterize chemical entities from this plant and evaluate their protein kinase inhibitory activity. Materials and Methods: Kinase inhibitory activity were assayed in appropriate buffer, with either protein or peptide as substrate in the presence of 15µM (33-P) ATP (3,000Ci/mmol; 10mCi/ml) in a final volume of 30µL. Controls were performed with appropriate dilutions of dimethyl sulphoxide. A portion of the Chloroform extract, ethylacetate and n-butanol soluble fractions of the stem bark of Acacia auriculiformis were screened against a panel of disease-related protein kinases and the active fractions was tested over a wide range of concentrations from 0.016 to 50µg/ml and the IC 50 values were determined from the dose response curve. The most active fraction was subjected to chromatographic separation using Silica gel G column chromatography and sephadex LH-20 to give compound I. The structure of the isolated compound was elucidated using NMR and LC-MS. Results: The Primary screening of the extract and fractions showed that the chloroform extract was inactive against all the protein kinases investigated, while the ethylacetate and n-butanol soluble fractions inhibited all the protein kinases tested. Compound I also inhibited all the kinases tested. The IC 50 of the active fractions and compound were also evaluated. Ethylacetate fraction inhibited all the kinases tested with the highest activity against Haspine kinase with IC 50 of 1.0 µg/ml, while n-butanol also gave the highest activity against Haspine kinase with 1C 50 of 1.3 µg/ml. From the active ethylacetate fractions 3, 4', 7, 8-tetrahydroxy flavone was isolated. The Compound exhibited the maximal activity against DYRK1A kinase with an IC 50 of 2.05 µg/ml followed by CDK9 with an IC 50 of 2.28 µg/ml. Conclusion: 3, 4',7, 8-tetrahydroxy flavone was isolated was found to be a DYRK1A and CDK9 inhibitor which might justify the anticancer potential of this plant.

The purpose of this work is to investigate the protein kinase inhibitory activity of constituents from Acacia auriculiformis stem bark. Column chromatography and NMR spectroscopy were used to purify and characterize betulin from an ethyl acetate soluble fraction of acacia bark. Betulin, a known inducer of apoptosis, was screened against a panel of 16 disease-related protein kinases. Betulin was shown to inhibit Abelson murine leukemia viral oncogene homolog 1 (ABL1) kinase, casein kinase 1ε (CK1ε), glycogen synthase kinase 3α/β (GSK-3 α/β), Janus kinase 3 (JAK3), NIMA Related Kinase 6 (NEK6), and vascular endothelial growth factor receptor 2 kinase (VEGFR2) with activities in the micromolar range for each. The effect of betulin on the cell viability of doxorubicin-resistant K562R chronic myelogenous leukemia cells was then verified to investigate its putative use as an anti-cancer compound. Betulin was shown to modulate the mitogen-activated protein (MAP) kinase pathway, with activity similar to that of imatinib mesylate, a known ABL1 kinase inhibitor. The interaction of betulin and ABL1 was studied by molecular docking, revealing an interaction of the inhibitor with the ABL1 ATP binding pocket. Together, these data demonstrate that betulin is a multi-target inhibitor of protein kinases, an activity that can contribute to the anticancer properties of the natural compound and to potential treatments for leukemia.

The purpose of this work is to investigate the protein kinase inhibitory activity of constituents from ethyl acetate soluble fraction of Acacia auriculiformis stem bark. Column chromatography, gel filtration and NMR spectroscopy were used to purified and characterized betulin from the extract. Betulin which is a known inducer of apoptosis was screened against a panel of 16 disease-related protein kinases. Betulin was shown to inhibit Abelson murine leukemia viral oncogene homolog 1 (ABL1) kinase, casein kinase 1epsilon (CK1epsilon), glycogen synthase kinase 3alpha/&beta; (GSK-3alpha/&beta;), Janus kinase 3 (JAK3), NIMA Related Kinase 6 (NEK6) and vascular endothelial growth factor receptor 2 kinase (VEGFR2) and with activity in &micro;M range. The effect of betulin on the cell viability of doxorubicin-resistant K562R chronic myelogenous leukemia cells was then verified to underline its putative use as anti-cancer compound. Betulin was shown to modulate the mitogen-activated protein (MAP) kinase pathway similarly to imatinib mesylate, a well-known inhibitor of ABL1 kinase. The interaction of betulin and ABL1 was studied by molecular docking showing an interaction of the inhibitor with the ATP binding pocket. Altogether, these data demonstrate that betulin is a multi-target inhibitor of protein kinases, an activity that can contribute to the anticancer properties of the natural compound and notably for treatment of leukemia.