RESUMO
In this study, we investigated the hepatoprotective effects of ethanol extracts from Chlorella vulgaris (CH) on animals. We measured its effect on the quinone reductase (QR) activity in Hepa1c1c7 cells, finding that CH induced a significantly higher QR activity in these cells. We isolated the active fraction (CH F4-2) from CH using chromatography methods. CH F4-2 may activate cellular antioxidant enzymes through upregulation of the Nrf2 pathway in hepatocarcinoma cells with CH F4-2 (25.0-200 µg/mL) for 48 h. Furthermore, CH F4-2 increased the expression of NQO1 [ NAD(P)H: quinone oxidoreductase, also known as QR], heme oxygenase-1, and glutathione-S-transferase P. Moreover, we found that ethanol-induced hepatic pathological changes-elevations in glutamic oxaloacetic transaminase, glutamic pyruvic transaminase, γ-glutamyltransferase, and lactate dehydrogenase-were significantly decreased. The inhibitory effect of CH on alcohol-induced liver injury was associated with the suppression of alcohol-induced increases in intestinal permeability. The ethanol extract from CH was found to induce QR activation, making it a potentially good candidate for a hepatoprotection agent.
Assuntos
Doença Hepática Induzida por Substâncias e Drogas , Chlorella vulgaris , Etanol , Fator 2 Relacionado a NF-E2 , Fitoterapia , Extratos Vegetais , Animais , Masculino , Ratos , Alanina Transaminase/sangue , Aspartato Aminotransferases/sangue , Doença Hepática Induzida por Substâncias e Drogas/tratamento farmacológico , Doença Hepática Induzida por Substâncias e Drogas/enzimologia , Chlorella vulgaris/química , Etanol/toxicidade , gama-Glutamiltransferase/sangue , L-Lactato Desidrogenase/sangue , Fígado/citologia , Fígado/metabolismo , Fígado/patologia , Neoplasias Hepáticas Experimentais/tratamento farmacológico , Neoplasias Hepáticas Experimentais/metabolismo , NAD(P)H Desidrogenase (Quinona)/efeitos dos fármacos , NAD(P)H Desidrogenase (Quinona)/metabolismo , Fator 2 Relacionado a NF-E2/efeitos dos fármacos , Fator 2 Relacionado a NF-E2/metabolismo , Extratos Vegetais/farmacologia , Quinona Redutases/efeitos dos fármacos , Quinona Redutases/metabolismo , Ratos Sprague-Dawley , Regulação para Cima/efeitos dos fármacosRESUMO
Bioactive peptides as products of hydrolysis of diverse marine invertebrate (shellfish, crustacean, rotifer, etc.) proteins are the focus of current research. After much research on these muscles and by-products, some biologically active peptides were identified and applied to useful compounds for human utilization. This chapter reviews bioactive peptides from marine invertebrates in regarding to their bioactivities. Additionally, specific characteristics of antihypertensive, anti-Alzheimer, antioxidant, antimicrobial peptide enzymatic production, methods to evaluate bioactivity capacity, bioavailability, and safety concerns of peptides are reviewed.
Assuntos
Organismos Aquáticos/química , Suplementos Nutricionais , Promoção da Saúde , Invertebrados/química , Peptídeos/metabolismo , Animais , Anti-Infecciosos/química , Anti-Infecciosos/metabolismo , Anti-Infecciosos/uso terapêutico , Anti-Hipertensivos/química , Anti-Hipertensivos/metabolismo , Anti-Hipertensivos/uso terapêutico , Crustáceos/química , Suplementos Nutricionais/análise , Humanos , Moluscos/química , Nootrópicos/química , Nootrópicos/metabolismo , Nootrópicos/uso terapêutico , Peptídeos/química , Peptídeos/uso terapêutico , Zooplâncton/químicaRESUMO
In this study, hydrolysates obtained from the freshwater rotifer Brachionus calyciflonus were investigated for angiotensin I converting enzyme (ACE) inhibitory peptides. Freshwater rotifer protein was hydrolyzed using six separate enzymes in a batch reactor. The peptic hydrolysate had the highest ACE inhibitory activity compared to the other hydrolysates. The highest ACE inhibitory peptide was separated using Sephadex G-25 column chromatography and high-performance liquid chromatography on a C18 column. The 50% inhibitory concentration (IC(50)) value of purified ACE inhibitory peptide was 40.01 microg/mL. ACE inhibitory peptide was identified as being seven amino acid residues of Ala-Gln-Gly-Glu-Arg-His-Arg by N-terminal amino acid sequence analysis. The IC(50) value of purified ACE inhibitory peptide was 47.1 microM, and Lineweaver-Burk plots suggested that the peptide purified from rotifer protein acts as a competitive inhibitor against ACE. The results of this study suggest that peptides derived from freshwater rotifers may be beneficial as antihypertension compounds in functional foods or as pharmaceuticals.
Assuntos
Inibidores da Enzima Conversora de Angiotensina/farmacologia , Anti-Hipertensivos/farmacologia , Fatores Biológicos/farmacologia , Peptídeos/farmacologia , Proteínas/metabolismo , Zooplâncton/química , Sequência de Aminoácidos , Inibidores da Enzima Conversora de Angiotensina/isolamento & purificação , Animais , Anti-Hipertensivos/isolamento & purificação , Ligação Competitiva , Fatores Biológicos/isolamento & purificação , Cromatografia , Água Doce , Hidrólise , Concentração Inibidora 50 , Dados de Sequência Molecular , Peptídeos/isolamento & purificaçãoRESUMO
OBJECTIVE: GH controls the proliferation of cartilage, fibroblasts or the differentiation of adipose and muscle tissue. However, the effect of GH on neuronal cells remains unknown. The present study was conducted to determine the proliferative or differentiating effect of GH on the nervous system in vitro. DESIGN: Neuronal hybrid cells (VSC4.1) were cultured with GH. The concentration ranged from 0.134 microg/ml up to 1.34 mg/ml. A cell confluency and MTT assay, cell cycle phase analysis with flow cytometry, extracellular receptor kinase (ERK) phosphorylation and mitogen activated protein kinase (MAPK) inhibitor (PD98050) assays were all performed to determine the effect on proliferation. Differentiation was evaluated by neurite outgrowth and neurofilament expression. Terminally differentiated neurons were stained by Hoechst 33342 for apoptotic nuclear fragmentation by degeneration. Poly-adenosyl ribose polymerase (PARP) expression and its cleavage products were evaluated. RESULTS: Cells at concentrations between 0.134 microg/ml and 1.34 microg/ml of GH proliferated with ERK phosphorylation, which was attenuated by MAPK inhibitors. Proliferation decreased at concentrations higher than 13.4 microg/ml; however, neurite outgrowth was observed at these concentrations. Terminally differentiated cells underwent apoptosis and showed nuclear fragmentation by Hoechst 33342 staining. PARP expression was increased with caspase-3 dependent-cleaved fragment. CONCLUSIONS: Our in vitro data demonstrate that GH exerts dual effects; proliferation with a specific GH dose window, or differentiation in a dose-dependent manner in cultured neuronal hybrid cells.