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Ethnopharmacological relevance Unravelling the anti-diabetic mechanism of action of L. leonurus at adipose, liver, muscle and pancreatic level. Aims To investigate the mechanism of action of an organic extract of L. leonurus and marrubiin at the gene level in adipose, liver and muscle tissues of an obese rat model and in a co-culture model. Materials and methods Obese Wistar rats were fed a cafeteria diet for eight weeks, treated with an extract of L. Leonurus, marrubiin, sulfonylurea and aspirin for two weeks and the level of gene expression of selected markers were investigated across different tissues. The effects mediated by the different treatments were investigated in co-culture cell models involving 3T3-L1 (fat), Chang (liver), C2C12 (muscle) and INS-1 (pancreatic) cells under both normal and hyperglycemic conditions. Results L. leonurus extract mediated a significant increase in PPAR gamma, glucokinase, FAS and UCP2 gene expression in adipose tissue, whilst the opposite was observed in the liver. At the muscle level, a significant increase in FAS gene expression was observed relative to the obese control rats. Furthermore, the extract as well as marrubiin, modulated improvements in the adipokine profile. The co-culture models showed that the effect mediated by the extract was dependent on, the tissue type as well as the glycemic conditions. Conclusions L. Leonurus extract as well as marrubiin exhibit anti-diabetic properties where the mechanism of action is mainly at the adipose tissue level. The increase in expression of the genes of interest mentioned above potentially play a protective role towards the liver and possibly towards the muscle tissues as well.

Nanostructured lipid carriers (NLCs) of Leonotis leonurus were successfully produced using high-pressure homogenisation (HPH) on a LAB 40 homogeniser. The particle size was determined for the formulation as well as short-term stability study. The formulation was exposed to Chang liver cells for a glucose uptake study and to INS-1 cells for a chronic insulin release study under normoglycaemic and hyperglycaemic conditions. The particle size of the extract NLC was 220 nm with a PdI of 0.08 after homogenisation at 800 bar. The formulation was stable at the tested temperatures. The extract NLC formulation at 1 µg/ml improved glucose uptake, relative to the control liver cells. Insulin release in INS-1 cells was also elevated under hyperglycaemic conditions when exposed to the NLCs, in comparison with the control untreated cells and the non-formulated extract. The plant extract encapsulated in NLC improved the uptake of glucose and enhanced the insulin sensitivity in vitro, compared to the extract.

Nanostructured lipid carriers (NLCs) of Leonotis leonurus were successfully produced using high-pressure homogenisation (HPH) on a LAB 40 homogeniser. The particle size was determined for the formulation as well as short-term stability study. The formulation was exposed to Chang liver cells for a glucose uptake study and to INS-1 cells for a chronic insulin release study under normoglycaemic and hyperglycaemic conditions. The particle size of the extract NLC was 220 nm with a PdI of 0.08 after homogenisation at 800 bar. The formulation was stable at the tested temperatures. The extract NLC formulation at 1 µg/ml improved glucose uptake, relative to the control liver cells. Insulin release in INS-1 cells was also elevated under hyperglycaemic conditions when exposed to the NLCs, in comparison with the control untreated cells and the non-formulated extract. The plant extract encapsulated in NLC improved the uptake of glucose and enhanced the insulin sensitivity in vitro, compared to the extract.

One of the many control mechanisms of serine proteinases is their specific inhibition by protein proteinase inhibitors. An extract of Acacia schweinfurthii was screened for potential serine proteinase inhibition. It was successfully purified to homogeneity by precipitating with 80% (v/v) acetone and sequential chromatographic steps, including ion-exchange, affinity purification and reversed-phase high performance liquid chromatography. Reducing sodium dodecyl sulphate polyacrylamide gel electrophoresis conditions revealed an inhibitor (ASTI) consisting of two polypeptide chains A and B of approximate molecular weights of 16 and 10 kDa, respectively, and under non-reducing conditions, 26 kDa was observed. The inhibitor was shown to inhibit bovine trypsin (Ki of 3.45 nM) at an approximate molar ratio of inhibitor:trypsin (1:1). The A- and B-chains revealed complete sequences of 140 and 40 amino acid residues, respectively. Sequence similarity (70%) was reported between ASTI A-chain and ACTI A-chain (Acacia confusa) using ClustalW. The B-chain produced a 76% sequence similarity between ASTI and Leucaena leucocephala trypsin inhibitor.