Purification of a thermostable antinociceptive lectin isolated fromAndira anthelmia

Autor: Luiz André Cavalcante Brizeno, Ana Maria Sampaio Assreuy, Edson Lopes da Ponte, Camila Bezerra Nobre, Francisco Lucas Faustino do Nascimento, Kyria S. Nascimento, Benildo Sousa Cavada, Cleane Gomes Moreira, Mayara Torquato Lima Silva
Rok vydání: 2015
Předmět:
Zdroj: Journal of Molecular Recognition. 29:248-252
ISSN: 0952-3499
DOI: 10.1002/jmr.2523
Popis: Andira anthelmia (tribe Dalbergieae), a plant from Brazilian Amazon, possesses a seed lectin that was purified by affinity chromatography in sepharose-mannose. This novel Dalbergieae lectin, named AAL, agglutinated rabbit erythrocytes treated with trypsin. The hemagglutinating activity of AAL was maintained after incubation at a wide range of temperature (40 to 70 °C) and pH, was shown to be dependent on divalent cations, and was inhibited by d-mannose and d-sucrose. AAL showed an electrophoretic profile in sodium dodecyl sulfate-polyacrylamide gel electrophoresis similar to other lectins of the tribe Dalbergieae, presenting a double band of molecular weight with approximately 20 kDa and other minor bands of 17, 15, and 13 kDa, being the smaller fragment glycosylated. AAL injected by intravenous route in mice showed antinociceptive activity in two behavioral tests (writhing and formalin). In the writhing test induced by acetic acid, AAL showed inhibitory effect at 0.01 mg/kg (68%), 0.1 mg/kg (46%) and 1 mg/kg (74%). In the formalin test, AAL (0.1 mg/kg) inhibited by 48% the licking time in the inflammatory phase, an effect that was recovered by the lectin association with mannose. In conclusion, AAL presents analgesic effect involving the lectin domain via peripheral mechanisms of inflammatory nociception. This activity highlights the importance of lectins as tools to be used for understanding the interaction of protein-carbohydrate in processes associated to inflammatory pain. Copyright © 2015 John Wiley & Sons, Ltd.
Databáze: OpenAIRE
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