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1.
Plant Physiol ; 187(1): 116-132, 2021 09 04.
Artículo en Inglés | MEDLINE | ID: mdl-34618148

RESUMEN

Arabidopsis (Arabidopsis thaliana) defenses against herbivores are regulated by the jasmonate (JA) hormonal signaling pathway, which leads to the production of a plethora of defense compounds. Arabidopsis defense compounds include tryptophan-derived metabolites, which limit Arabidopsis infestation by the generalist herbivore two-spotted spider mite, Tetranychus urticae. However, the phytochemicals responsible for Arabidopsis protection against T. urticae are unknown. Here, we used Arabidopsis mutants disrupted in the synthesis of tryptophan-derived secondary metabolites to identify phytochemicals involved in the defense against T. urticae. We show that of the three tryptophan-dependent pathways found in Arabidopsis, the indole glucosinolate (IG) pathway is necessary and sufficient to assure tryptophan-mediated defense against T. urticae. We demonstrate that all three IGs can limit T. urticae herbivory, but that they must be processed by myrosinases to hinder T. urticae oviposition. Putative IG breakdown products were detected in mite-infested leaves, suggesting in planta processing by myrosinases. Finally, we demonstrate that besides IGs, there are additional JA-regulated defenses that control T. urticae herbivory. Together, our results reveal the complexity of Arabidopsis defenses against T. urticae that rely on multiple IGs, specific myrosinases, and additional JA-dependent defenses.


Asunto(s)
Arabidopsis/fisiología , Glucosinolatos/metabolismo , Glicósido Hidrolasas/metabolismo , Herbivoria , Indoles/metabolismo , Defensa de la Planta contra la Herbivoria , Proteínas de Plantas/metabolismo , Animales , Arabidopsis/enzimología , Tetranychidae/fisiología
2.
Asian Pac J Trop Biomed ; 4(Suppl 1): S516-20, 2014 May.
Artículo en Inglés | MEDLINE | ID: mdl-25183142

RESUMEN

OBJECTIVE: To identify the possible functional molecules for therapeutic uses by screening the crude aqueous and methanolic extracts derived from sesame seeds (Sesamum indicum) in vitro. METHODS: High performance liquid chromatography was used to scan the functional molecules present in the extracts. RESULTS: The crude aqueous extracts showed the possibilities to present caffeine and cetirizine or its derivatives like molecules. On the other hand, the crude methanolic extract may contain Loratadine or its derivatives like molecules. Both type of extracts showed hemagglutination inhibition activities in all types of human blood samples tested. However, they showed stronger binding with AB+ blood group than those of A+ and B+ blood. CONCLUSIONS: Sesame seeds may be considered as a functional food.

3.
Asian Pac J Trop Biomed ; 2(9): 673-8, 2012 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-23569993

RESUMEN

OBJECTIVE: To investigate the bioactivities of crude n-hexane, ethyl acetate and methanol extracts of aerial part of Boerhavia diffusa Linn. (B. diffusa) and its phytochemical analysis. METHODS: The identification of phytoconstituents and assay of antioxidant, thrombolytic, cytotoxic, antimicrobial activities were conducted using specific standard in vitro procedures. RESULTS: The results showed that the plant extracts were a rich source of phytoconstituents. Methanol extract showed higher antioxidant, thrombolytic activity and less cytotoxic activity than those of n-hexane and ethyl acetate extracts of B. diffusa. Among the bioactivities, antioxidant activity was the most notable compared to the positive control and thus could be a potential rich source of natural antioxidant. In case of antimicrobial screening, crude extracts of the plant showed remarkable antibacterial activity against tested microorganisms. All the extracts showed significant inhibitory activity against Candida albicuns, at a concentration of 1000 µg/disc. CONCLUSIONS: The present findings suggest that, the plant widely available in Bangladesh, could be a prominent source of medicinally important natural compounds.


Asunto(s)
Nyctaginaceae/química , Fitoquímicos/química , Componentes Aéreos de las Plantas/química , Extractos Vegetales/química , Extractos Vegetales/farmacología , Animales , Antiinfecciosos/química , Antiinfecciosos/farmacología , Antioxidantes/química , Artemia/efectos de los fármacos , Bacterias/efectos de los fármacos , Compuestos de Bifenilo/antagonistas & inhibidores , Dosificación Letal Mediana , Pruebas de Sensibilidad Microbiana , Óxido Nítrico/antagonistas & inhibidores , Fenoles/química , Picratos/antagonistas & inhibidores , Extractos Vegetales/toxicidad
5.
Antiviral Res ; 88(1): 10-8, 2010 Oct.
Artículo en Inglés | MEDLINE | ID: mdl-20615432

RESUMEN

Strictinin, which is a member of the ellagitanin family of hydrolyzable tannins, prevented replication of human, duck and swine influenza A viruses (IAVs) in vitro at non-toxic concentrations. The addition of strictinin at the same time as IAV inoculation to MDCK cells inhibited viral replication in a dose-dependent manner. Strictinin showed 50% inhibitory concentrations for IAVs from 0.09±0.021 to 0.28±0.037µM (mean±S.E.M.) by the focus-forming assay. Treatment of MDCK cells with strictinin before and after viral inoculation resulted in no significant antiviral activity. Further studies showed that strictinin inhibited IAV-induced hemifusion. However, strictinin exhibited no inhibitory effect against receptor binding, sialidase activity. Strictinin also showed an antiviral effect on influenza B virus and human parainfluenza virus type-1 in vitro. The results indicate that strictinin is a useful antiviral agent.


Asunto(s)
Antivirales/farmacología , Virus de la Influenza A/efectos de los fármacos , Virus de la Influenza B/efectos de los fármacos , Virus de la Parainfluenza 1 Humana/efectos de los fármacos , Fenoles/farmacología , Animales , Línea Celular , Relación Dosis-Respuesta a Droga , Humanos , Virus de la Influenza A/fisiología , Virus de la Influenza B/fisiología , Neuraminidasa/antagonistas & inhibidores , Virus de la Parainfluenza 1 Humana/fisiología , Taninos/farmacología , Acoplamiento Viral/efectos de los fármacos , Replicación Viral/efectos de los fármacos
6.
Biol Pharm Bull ; 32(7): 1188-92, 2009 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-19571383

RESUMEN

Hesperidin, a flavonoid obtained from citrus fruits, is known to have multiple biological activities and antimicrobial activities for human viruses; however, hesperidin has very low solubility in water and the target molecule of hesperidin for influenza virus remains unknown. A water-soluble derivative of hesperidin, glucosyl hesperidin (GH), which was synthesized by regioselective transglycosylation with cyclodextrin glucanotransferase, has been reported to have biological activities that are as or stronger than those of hesperidin. To determine the inhibitory effect of GH on influenza A virus (IAV) infection, Madin-Darby canine kidney (MDCK) cells were treated with GH before, at the same time as, and after IAV inoculation. GH treatment before IAV inoculation had no effect on virus replication, whereas, treatment with GH at the same time as or after IAV inoculation induced distinct reduction in IAV replication. Inhibition analysis of GH against two surface glycoprotein spikes of IAV revealed that GH prevents IAV replication by inhibition of viral sialidase activity that is involved in the entry and release stages on IAV infection but not by receptor binding inhibition. GH had no cytotoxic effects on MDCK cells in a dose range of 0-25 mM. Our results provide useful information for the development of novel sialidase inhibitors for influenza prevention.


Asunto(s)
Antivirales/farmacología , Glucósidos/farmacología , Hesperidina/análogos & derivados , Virus de la Influenza A/efectos de los fármacos , Neuraminidasa/antagonistas & inhibidores , Replicación Viral/efectos de los fármacos , Animales , Antivirales/química , Línea Celular , Efecto Citopatogénico Viral , Perros , Relación Dosis-Respuesta a Droga , Glucósidos/química , Pruebas de Inhibición de Hemaglutinación , Hesperidina/química , Hesperidina/farmacología , Humanos , Virus de la Influenza A/enzimología , Virus de la Influenza A/fisiología , Estructura Molecular , Factores de Tiempo , alfa-Fetoproteínas/farmacología
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