Antioxidant indices and amino acid composition of phenolic containing Lima beans (Phaseolus lunatus) after simulated human gastrointestinal digestion

The present investigation was designed to characterize the phenolic profile of Lima beans (Phaseolus Lunatus) and also to evaluate the antioxidant indices: total phenolic content (TPC), total flavonoid content (TFC), ferric reducing antioxidant power (FRAP), 2,2-Diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity and amino acid composition at different stages of simulated gastrointestinal digestion (oral, gastric, intestinal). High Performance Liquid Chromatography (HPLC-DAD) analysis revealed the presence of some phenolic compounds (gallic acid, catechin, caffeic acid, rutin, quercitrin, quercetin, kaempferol and apigenin), with a reduced amount (mg/g) after cooking; gallic acid (raw: 1.96 ± 0.02; cooked: 1.82 ± 0.01); catechin (raw: 0.83 ± 0.01; cooked: 0.73 ± 0.01); rutin (raw: 2.61 ± 0.03; cooked:1.74 ±0.03); quercitrin (raw: 5.73 ± 0.01; cooked: 5.68 ± 0.01); apigenin (raw: 2.09 ±0.01; cooked:1.79 ± 0.02),  with exception of quercetin (raw: 2.11 ±0.02; cooked: 5.73 ±  0.02) and caffeic acid (raw: 2.08 ±0.04; cooked: 2.95 ± 0.04). The results of antioxidant indices of in vitro enzyme digested lima beans revealed higher values for cooked Lima beans compared to the raw counterpart, with a stepwise increase at the different stages of in vitro digestion, with the exception of ferric reducing antioxidant power; TPC (oral digestion: 65.44 ± 0.96; gastric digestion:134.87± 0.46; intestinal digestion:517.72 ± 4.70; mg/g tannic acid equivalent), TFC (oral digestion: 199.30 ± 6.43; gastric digestion: 1065.97 ± 1.22; intestinal digestion: 3691.87 ± 4.2; mg/g quercetin equivalent), DPPH (oral digestion: 85800.00 ± 305.50; gastric digestion: 99066.66 ± 115.47; intestinal digestion: 211354.20 ± 360.84 µmol TE/g sample). The results also revealed a progressive increase in the antioxidant indices and amino acid composition (mg/kg) for both raw and processed lima beans at various stages of the in vitro digestion, with the intestinal phase of simulated digestion ranking higher. This implied that the Lima beans contained some essential amino acids and antioxidant molecules that would be readily available after passing through the gastrointestinal tract and could therefore be explored as functional food in the management of free radical mediated diseases

Cytosine-block telomeric type DNA-binding activity of hnRNP proteins from human cell lines.

8Following the observation of the presence in mammalian nuclear extracts of a DNA binding activity quite specific for the single-stranded C-rich telomeric motif, we have isolated from the K562 human cell line by affinity chromatography and identified by mass spectrometry a number of proteins able to bind to this sequence. All of them belong to different heterogeneous nuclear ribonucleoprotein subgroups (hnRNP). Whereas many of them, namely hnRNP K, two isoforms of hnRNP I, and the factor JKTBP, appear to bind to this sequence with limited specificity after isolation, an isoform of hnRNP D (alias AUF1) and particularly hnRNP E1 (alias PCBP-1) show a remarkable specificity for the (CCCTAA)n repeated motif. Both have been obtained also as recombinant proteins expressed in Escherichia coli and have been shown to retain their binding specificity toward the C-block repeated sequence. In the light of the current knowledge about these proteins, their possible involvement in telomere functioning is discussed.nonenoneBandiera A.; Tell G.; Marsich E.; Scaloni A.; Pocsfalvi G.; Akintunde Akindahunsi A.; Cesaratto. L; Manzini G.Bandiera, Antonella; Tell, Gianluca; Marsich, Eleonora; Scaloni, A.; Pocsfalvi, G.; Akintunde Akindahunsi, A.; Cesaratto, Laura; Manzini, Giorgi

\u201cCytosine-block telomeric type DNA-binding activity of hnRNP proteins from human cell lines\u201c

Following the observation of the presence in mammalian nuclear extracts of a DNA binding activity quite specific for the single-stranded C-rich telomeric motif, we have isolated from the K562 human cell line by affinity chromatography and identified by mass spectrometry a number of proteins able to bind to this sequence. All of them belong to different heterogeneous nuclear ribonucleoprotein subgroups (hnRNP). Whereas many of them, namely hnRNP K, two isoforms of hnRNP I, and the factor JKTBP, appear to bind to this sequence with limited specificity after isolation, an isoform of hnRNP D (alias AUF1) and particularly hnRNP E1 (alias PCBP-1) show a remarkable specificity for the (CCCTAA)n repeated motif. Both have been obtained also as recombinant proteins expressed in Escherichia coli and have been shown to retain their binding specificity toward the C-block repeated sequence. In the light of the current knowledge about these proteins, their possible involvement in telomere functioning is discussed

Neuromodulatory effect of solvent fractions of Africa eggplant (Solanium dadyphyllum) against KCN-induced mitochondria damage, viz. NADH-succinate dehydrogenase, NADH- cytochrome c reductase, and succinate-cytochrome c reductase

Abstract Background In the past few years, there has been a tremendous increase in the number of plant-based health supplements with respect to their safety and efficacy in diseases treatment and prevention. Solanum dasyphyllum, also known as Africa eggplant is ethnomedicinally used as an antivenom, pain reliever and anticonvulsant in various part of Nigeria, however, there is no scientific data to support some of these claims. Methods This study evaluated the protective effect of solvent fractions of Solanum dasyphyllum, hexane fraction of S. dasyphyllum (HFSD), dichloromethane fraction of S. dasyphyllum (DFSD), ethylacetate fraction of S. dasyphyllum (EAFSD), methanolic fraction of S. dasyphyllum (MFSD) and crude fraction of S. dasyphyllum (CFSD) on cyanide-induced oxidative stress and neurotoxicity in vitro in the cerebral cortex. Neuroprotective activities were evaluated by assaying for markers of oxidative stress, neurotoxicity and electron transport system enzymes via evaluating lipid peroxidation (LPO), protein carbonyl (PC), reduced glutathione (GSH), acetylcholinesterase (AChE), NADH-succinate dehydrogenase (NSD), NADH-cytochrome c reductase (NCR), and succinate-cytochrome c reductase (SCR) in the homogenate of cerebral cortex. Results The results showed that all solvent fractions of S. dasyphyllum significantly ameliorated cyanide-induced oxidative stress (P < 0.05). It inhibited the activity of acetylcholinesterase-HFSD (68.42 ± 5.37%), DFSD (36.32 ± 5.45%), EFA (20 ± 0.69%), MFSD (33.16 ± 4.8%) and CFSD (35.79 ± 2.8%), increased the activity of NSD [HFSD (94.74 ± 7.3%), EAFSD (78.95 ± 5.4%) and CFSD (60.53 ± 4.6%)], while DFSD (− 5.26 ± 1.4%) and MFSD (− 7.9 ± 0.4%) had a negative effect, increased the activity of NCR [HFSD (91.89 ± 7.1%), DFSD (90.54 ± 8.2%), EAFSD (62.16 ± 4.7%); MFSD (306.76 ± 7.2%) and CFSD (154.0 ± 8.1%)]. All the solvent fractions also significantly increased the activity of SCR [HFSD (70.59 ± 3.8%), EAFSD (58.82 ± 6.4%), MFSD (88.24 ± 9.0%) CFSD (76.47 ± 8.2%)] apart from DFSD (− 5.88 ± 1.2%) in rat cerebral cortex. Conclusion This result shows that S. dasyphyllum has neuroprotective activities, however HFSD shows the most potent bioactivities in maintaining mitochondria integrity by preserving the electron transport system. Further work can be done on isolating and characterizing the bioactive compound in HFSD for novel natural product in the treatment of neurological disorders

Parkia biglobosa Improves Mitochondrial Functioning and Protects against Neurotoxic Agents in Rat Brain Hippocampal Slices

Objective. Methanolic leaf extracts of Parkia biglobosa, PBE, and one of its major polyphenolic constituents, catechin, were investigated for their protective effects against neurotoxicity induced by different agents on rat brain hippocampal slices and isolated mitochondria. Methods. Hippocampal slices were preincubated with PBE (25, 50, 100, or 200 µg/mL) or catechin (1, 5, or 10 µg/mL) for 30 min followed by further incubation with 300 µM H2O2, 300 µM SNP, or 200 µM PbCl2 for 1 h. Effects of PBE and catechin on SNP- or CaCl2-induced brain mitochondrial ROS formation and mitochondrial membrane potential (ΔΨm) were also determined. Results. PBE and catechin decreased basal ROS generation in slices and blunted the prooxidant effects of neurotoxicants on membrane lipid peroxidation and nonprotein thiol contents. PBE rescued hippocampal cellular viability from SNP damage and caused a significant boost in hippocampus Na+, K+-ATPase activity but with no effect on the acetylcholinesterase activity. Both PBE and catechin also mitigated SNP- or CaCl2-dependent mitochondrial ROS generation. Measurement by safranine fluorescence however showed that the mild depolarization of the ΔΨm by PBE was independent of catechin. Conclusion. The results suggest that the neuroprotective effect of PBE is dependent on its constituent antioxidants and mild mitochondrial depolarization propensity