Characterization of a lectin from the craysfish Cherax quadricarinatus hemolymph and its effect on hemocytes.

Autor: Sánchez-Salgado JL; Departamento de Bioquimica, Laboratorio de Inmunologia, Facultad de Medicina UNAM, 04510, Mexico; Posgrado de Ciencias del Mar y Limnologia, UNAM, 04510, Mexico., Pereyra MA; Departamento de Bioquimica, Laboratorio de Inmunologia, Facultad de Medicina UNAM, 04510, Mexico., Vivanco-Rojas O; Departamento de Bioquimica, Laboratorio de Inmunologia, Facultad de Medicina UNAM, 04510, Mexico., Sierra-Castillo C; Centro de Investigaciones Biologicas, Universidad Autonoma del Estado de Morelos, Cuernavaca 62209, Mexico., Alpuche-Osorno JJ; Departamento de Bioquimica, Laboratorio de Inmunologia, Facultad de Medicina UNAM, 04510, Mexico; Instituto Tecnologico de Oaxaca, Oaxaca 68030, Mexico., Zenteno E; Departamento de Bioquimica, Laboratorio de Inmunologia, Facultad de Medicina UNAM, 04510, Mexico; Centro de Investigaciones UNAM-UABJO, Oaxaca 68020, Mexico., Agundis C; Departamento de Bioquimica, Laboratorio de Inmunologia, Facultad de Medicina UNAM, 04510, Mexico. Electronic address: agundis@bq.unam.mx.
Jazyk: angličtina
Zdroj: Fish & shellfish immunology [Fish Shellfish Immunol] 2014 Aug; Vol. 39 (2), pp. 450-7. Date of Electronic Publication: 2014 Jun 11.
DOI: 10.1016/j.fsi.2014.05.039
Abstrakt: Lectins participate in the immune mechanisms of crustaceans. They have been considered as humoral receptors for pathogen-associated molecular patterns; however, some reports suggest that lectins could regulate crustacean cellular functions. In the present study, we purified and characterized a serum lectin (CqL) from the hemolymph of Cherax quadricarinatus by affinity chromatography and determined its participation in the regulation of hemocytes' oxidative burst. CqL is a 290-kDa lectin in native form, constituted by 108, 80, and 29-kDa subunits. It is mainly composed of glycine, alanine, and a minor proportion of methionine and histidine. It showed no carbohydrates in its structure. CqL is composed of several isoforms, as determined by 2D-electrophoresis, and shows no homology with any crustacean protein as determined by Lc/Ms mass spectrometry. CqL agglutinated mainly rat and rabbit erythrocytes and showed a broad specificity for monosaccharides such as galactose, glucose, and sialic acid, as well as for glycoproteins, such as porcine stomach and bovine submaxillary mucin and fetuin. It is a Mn(2+)-dependent lectin. CqL recognized 8% of crayfish granular hemocytes and increased 4.2-fold the production of hemocytes' superoxide anion in vitro assays when compared with non-treated hemocytes. This effect showed the same specificity for carbohydrates as hemagglutination; moreover, superoxide dismutase and diphenyleneiodonium chloride were effective inhibitors of CqL oxidative-activation. The CqL homoreceptor is a 120-kDa glycoprotein identified in the hemocytes lysate. Our results suggest that CqL participates actively in the regulation of the generation of superoxide anions in hemocytes using NADPH-dependent mechanisms.
(Copyright © 2014 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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