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
Autor: | Rômulo Farias Carneiro, Maria H.C. Santos, Celso Shiniti Nagano, Renato R. Roma, Valdenice F. Santos, Claudener S. Teixeira, Gerlânia de Oliveira Leite, Alexandre Holanda Sampaio, Plínio Delatorre, Ana L.E. Santos, Raquel O. Pereira, Bruno A.M. Rocha, Rafael C. Silva, Adriana Rolim Campos |
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Rok vydání: | 2019 |
Předmět: |
0301 basic medicine
Male Biophysics TRPV1 Mannose TRPV Cation Channels Biochemistry Biophysical Phenomena Chromatography Affinity Protein Structure Secondary Acetylglucosamine 03 medical and health sciences chemistry.chemical_compound Glucosamine Facial Pain Tandem Mass Spectrometry Lectins parasitic diseases Animals Amino Acid Sequence Receptor Molecular Biology Zebrafish chemistry.chemical_classification 030102 biochemistry & molecular biology Molecular mass biology Chemistry Proteolytic enzymes Lectin Fabaceae 030104 developmental biology biology.protein lipids (amino acids peptides and proteins) Electrophoresis Polyacrylamide Gel Female Rabbits Glycoprotein |
Zdroj: | Archives of biochemistry and biophysics. 664 |
ISSN: | 1096-0384 |
Popis: | A new mannose/N-acetyl- d glucosamine-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 29 kDa (α-chain), 13 kDa (β-chain) and 8 kDa (γ-chain) with secondary structure composed of 3% α-helix, 44% β-sheet, 21% β-turn, and 32% coil. The orofacial antinociceptive activity of the lectin was also evaluated. MaL (0.03 mg 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. |
Databáze: | OpenAIRE |
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