RESUMEN
OBJECTIVES: To study and characterize the in vivo effect of the lectin from Luetzelburgia auriculata seed on acute inflammation models. METHODS: The lectin was purified from the crude saline extract by affinity chromatography on a guar-gum matrix. Native, heat-treated, and digested lectin was evaluated for anti-inflammatory activity by using peritonitis and paw edema models. The anti-inflammatory activity was characterized by intravital microscopy, nitric oxide production, and myeloperoxidase activity. RESULTS: The lectin exhibited anti-inflammatory activity (2 mg/kg) on both models, reducing local myeloperoxidase activity. Galactose or heat treatment (100 degrees C, 10 min) reduced anti-inflammatory action. Anti-inflammation involves the inhibition of adhesion and rolling of leukocytes along with augmentation of nitric oxide in serum. The lectin inhibited the edematogenic effect of histamine and prostaglandins (PGE2) but did not alter the chemoattractant effect of IL-8. CONCLUSIONS: The results indicate that this lectin is a potent anti-inflammatory molecule. Its effects engage diverse modulatory events.
Asunto(s)
Antiinflamatorios no Esteroideos/farmacología , Adhesión Celular/efectos de los fármacos , Dinoprostona/antagonistas & inhibidores , Fabaceae/química , Antagonistas de los Receptores Histamínicos , Inflamación/tratamiento farmacológico , Rodamiento de Leucocito/efectos de los fármacos , Leucocitos/efectos de los fármacos , Lectinas de Plantas/farmacología , Animales , Antiinflamatorios no Esteroideos/química , Carragenina , Quimiotaxis de Leucocito/efectos de los fármacos , Dinoprostona/farmacología , Edema/inducido químicamente , Edema/prevención & control , Electroforesis en Gel de Poliacrilamida , Galactosa/metabolismo , Indicadores y Reactivos , Inflamación/enzimología , Inflamación/patología , Neutrófilos/efectos de los fármacos , Óxido Nítrico/metabolismo , Peritonitis/inducido químicamente , Peritonitis/tratamiento farmacológico , Peroxidasa/metabolismo , Lectinas de Plantas/química , Ratas , Ratas Wistar , Semillas/químicaRESUMEN
A glucose/mannose-binding lectin was isolated from seeds of Parkia discolor (Mimosoideae) using affinity chromatography on Sephadex G-100 gel. The protein presented a unique component in SDS-PAGE corresponding to a molecular mass of 58,000 Da, which is very similar to that of a closely related lectin from Parkia platycephala. Among the simple sugars tested, mannose was the best inhibitor, but biantennary glycans, containing the trimannoside core, present in N-glycoproteins, also seem to be powerful inhibitors of the haemagglutinating activity induced by the purified lectin. The protein was characterised by high content of glycine and proline and absence of cysteine. Rabbit antibodies, anti-P. platycephala seed lectin, recognised the P. discolor lectin. However, no cross-reaction was observed when a set of other legume lectins from sub-family Papilionoideae and others from families Moraceae and Euphorbiaceae were assayed with the Parkia lectins. This suggests that Parkia lectins comprise a new group of legume lectins exhibiting distinct characteristics.