Purification and biophysical characterization of a mannose/N-acetyl-d-glucosamine-specific lectin from Machaerium acutifolium and its effect on inhibition of orofacial pain via TRPV1 receptor.
Arch Biochem Biophys
; 664: 149-156, 2019 03 30.
Article
em En
| MEDLINE
| ID: mdl-30772259
ABSTRACT
A new mannose/N-acetyl-dglucosamine-specific lectin, named MaL, was purified from seeds of Machaerium acutifolium by precipitation with ammonium sulfate, followed by affinity and ion-exchange chromatography. MaL haemagglutinates either native rabbit erythrocytes or those treated with proteolytic enzymes. MaL is highly stable by the ability to maintain its haemagglutinating activity after exposure to temperatures up to 50⯰C. The lectin haemagglutinating activity was optimum between pH 6.0 and 7.0 and inhibited after incubation with d-mannose and N-acetyl-d-glucosamine and α-methyl-d-mannopyranoside. MaL is a glycoprotein with relative molecular mass of 29â¯kDa (α-chain), 13â¯kDa (ß-chain) and 8â¯kDa (γ-chain) with secondary structure composed of 3% α-helix, 44% ß-sheet, 21% ß-turn, and 32% coil. The orofacial antinociceptive activity of the lectin was also evaluated. MaL (0.03â¯mgâ¯mL-1) reduced orofacial nociception induced by capsaicin, an effect that occurred via carbohydrate recognition domain interaction, suggesting an interaction of MaL with the transient receptor potential cation channel subfamily V member 1 (TRPV1) receptor. Our results confirm the potential pharmacological relevance of MaL as an inhibitor of acute orofacial mediated by TRPV1.
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Base de dados:
MEDLINE
Assunto principal:
Acetilglucosamina
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Dor Facial
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Canais de Cátion TRPV
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Lectinas
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Fabaceae
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Manose
Limite:
Animals
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article