The search for new compounds for controlling pain and inflammation, with minimal side effects has focused on marine algae. The aim of this work was to investigate the effect of the purified lectin from the green marine alga Caulerpa cupressoides (CcL) in classical models of nociception and inflammation. Male Swiss mice received i.v. CcL 30 min prior to receiving 0.8% acetic acid (10 ml/kg; i.p); 1% formalin (20 microl; s.c.) or were subjected to thermal stimuli. We observed that CcL (3, 9 or 27 mg/kg) significantly reduced the number of writhes induced by acetic acid by 37.2%; 53.5% and 86.0%, respectively. CcL (27 mg/kg) also reduced the second phase of the formalin test. However, CcL (27 mg/kg) did not present significant antinociceptive effects in the hot plate test, when compared to morphine, suggesting that its antinociceptive action occurs predominantly through a peripheral mechanism. The antinociceptive effects were abolished when CcL was pre-incubated with mucin (20mg/kg; i.v.). When CcL (9 mg/kg) was administered i.v. in Wistar rats 30 min before carrageenan administration, neutrophil counts were reduced by 65.9%. CcL also inhibited paw edema in all time intervals, especially at the third hour. Finally, CcL (9 mg/kg) administered i.v. in mice did not cause hepatic or renal alterations and did not affect body mass or macroscopy of the organs examined. In conclusion, CcL appears to have important antinociceptive and anti-inflammatory activities and could represent an important agent for future studies.
Researchers see algae as a promising tool to discover both efficient and safe agents for pain therapy. We evaluated the antinociceptive and anti-inflammatory activities of lectin from the marine alga Pterocladiella capillacea lectin (PcL). PcL was purified and tested in classical models of nociception and inflammation. Male Swiss mice received PcL 30 min prior to receiving 0.8% acetic acid (10 m ml/10 g, i.p.), 1% formalin (20 m ml/intraplantar) or the hot plate test, and were compared to untreated animals or animals pretreated with indomethacin or morphine. PcL (0.9, 8.1 or 72.9 mg/kg, i.v.) significantly reduced the number of writhes (30%, 39%, and 52%, respectively). PcL (72.9 mg/kg, i.v.) also reduced (pϽ Ͻ0.05) both the first and second phases of the formalin test by 58% and 87%, respectively. However, PcL (72.9 mg/kg) did not present significant antinociceptive effects in the hot plate test when compared to morphine, suggesting that its antinociceptive action occurs via peripheral rather than a central-acting mechanism. It was also observed that leukocyte migration was induced by carrageenan (500 m mg/cavity) in male Wistar rats and that PcL (8.1 mg/kg, i.v.) significantly reduced neutrophil migration by 84%, as compared to untreated animals, suggesting inhibition of inflammatory mediators. The data indicated that PcL has peripheral actions with both anti-inflammatory and antinociceptive properties.
-(Purification and characterisation of a lectin from the red marine alga Pterocladiella capillacea (S.G. Gmel.) Santel. & Hommers.). A lectin present in the marine red alga Pterocladiella capillacea was purified and characterised by extraction of soluble proteins (crude extract) in 20 mM Tris-HCl buffer, pH 7.5. Among the analysed erythrocytes (human blood group A, B and O and the animals ox, goat, chicken and rabbit) the lectin agglutinated specifically rabbit erythrocytes. The hemagglutinating activity assay showed that the lectin was not dependent on divalent cations and was shown to be inhibited by the glycoproteins avidin and mucin. The purification procedure was conduced by precipitation of the crude extract with 80% saturation ammonium sulfate (F0/80) followed by affinity chromatography on guar-gum column. The lectin of P. capillacea was purified 14.5 fold and had a recovery of 27.4% of the original total specific activity present in the crude extract. The absence of carbohydrate suggested that the lectin is not a glycoprotein. The molecular mass of P. capillacea lectin, determined by gel filtration, was 5.8 kDa. SDS-PAGE in the presence of β-mercaptoethanol gave one band, indicating that the native lectin is a monomeric protein. The activation energy of denaturation process (∆G') was calculated to be 106.87 kJ . mol -1 at 70 o C.RESUMO -(Purificação e caracterização de uma lectina da alga marinha vermelha Pterocladiella capillacea (S.G. Gmel.) Santel. & Hommers.). Uma lectina presente na alga marinha vermelha Pterocladiella capillacea foi purificada e caracterizada pela extração de proteínas solúveis (extrato bruto) em tampão Tris-HCl 20 mM, pH 7,5. Entre os eritrócitos testados (grupos sangüíneos humanos A, B e O e os animais boi, cabra, galinha e coelho) a lectina aglutinou especificamente eritrócitos de coelho. O ensaio de atividade hemaglutinante evidenciou que a lectina não era dependente de cátions divalentes e inibida pelas glicoproteínas avidina e mucina. O procedimento de purificação foi conduzido por precipitação protéica do extrato bruto com sulfato de amônio até 80% de saturação (F 0/80), seguido por cromatografia de afinidade em coluna de goma de Guar. A lectina de P. capillacea foi purificada 14,5 vezes e teve uma recuperação de 27,4% da atividade específica total original presente no extrato bruto. A ausência de carboidrato sugeriu que a lectina não é uma glicoproteína. A massa molecular da lectina de P. capillacea, determinada por filtração em gel, foi de 5,8 kDa. PAGE-SDS em presença de β-mercaptoetanol mostou uma única banda protéica, indicando que a lectina de P. capillacea é uma proteína monomérica. A energia de ativação do processo de desnaturação (∆G') foi calculada em 106,87 kJ . mol -1 a 70 o C.
A lectin was purified from the seaweed Gracilaria cornea by hydrophobic interaction chromatography on phenyl-Sepharose CL-4B followed by affinity chromatography on immobilized mucin. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of G. cornea lectin (GCL) revealed a single protein band of approximately 60 kDa, whereas by gel filtration on Sephadex G-100 its native molecular mass was 66 kDa. GCL exhibited a single isoeletric point of 4.3 and a 52.5% content of neutral sugars. Furthermore, the EDTA-treated lectin did not show any significant decrease in its ability to agglutinate trypsin-treated chicken erythrocytes. These data suggest that GCL is an acidic, monomeric glycoprotein that probably does not require divalent metal ions for its hemagglutinating activity. GCL hemagglutinating activity was not inhibited by any of the mono-, di-, and trisaccharides tested but was by the complex glycoproteins fetuin and porcine stomach mucin. Exposure of engorged females of the cattle tick (Boophilus microplus) to 0.1 mg mL(-1) GCL significantly (P < 0.05) reduced the female weight after the oviposition period, the egg mass weight, the hatching period, and the mean larvae survival time.
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