Agglutinins in Marine Algae for Human Erythrocytes

Boyd, William C.; Almodóvar, Luis; Boyd, Lyle G.

doi:10.1111/j.1537-2995.1966.tb04699.x

Cited by 104 publications

(68 citation statements)

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“…Lectins are present in a wide range of organisms from bacteria to animals, being present in all classes and families, although not in all the kinds and species (Lis & Sharon 1981). The first report on the occurrence of lectins in marine algae is relatively recent (Boyd et al 1966). Although several studies on lectins from marine algae have been reported, the number of these proteins purified and characterised is still considered small.…”

Section: Introductionmentioning

confidence: 99%

Purification and characterisation of a lectin from the red marine alga Pterocladiella capillacea (S.G. Gmel.) Santel. & Hommers.

Oliveira¹,

Nascimento²,

Lima³

et al. 2002

Rev. bras. Bot.

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-(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.

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Section: Introductionmentioning

confidence: 99%

Purification and characterisation of a lectin from the red marine alga Pterocladiella capillacea (S.G. Gmel.) Santel. & Hommers.

Oliveira¹,

Nascimento²,

Lima³

et al. 2002

Rev. bras. Bot.

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“…The proteins present in algae which are capable of binding to and agglutinating cells were first identified by Boyd et al (5) and designated as marine algal hemagglutinins. However, algal lectins were recently termed phycolectins (6,7) and represent a group of proteins which preferentially bind glycoproteins and share some other characteristics such as relatively low molecular weights, no metal requirement for hemagglutination, and occurrence in monomeric forms.…”

Section: Introductionmentioning

confidence: 99%

Antinociceptive activity of sulfated carbohydrates from the red algae Bryothamnion seaforthii (Turner) Kütz. and B. triquetrum (S.G. Gmel.) M. Howe

Viana

Freitas

Lima

et al. 2002

Braz J Med Biol Res

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We report the antinociceptive activity, determined by the writhing, formalin and hot-plate tests in mice, of crude (F0/60), lectin and carbohydrate fractions isolated by ammonium sulfate precipitation (0 to 60%) from Bryothamnion seaforthii and B. triquetrum, species of red algae. Not only fraction F0/60 but also lectins from both species significantly inhibited acetic acid-induced abdominal contractions after intraperitoneal or oral administrations. In the formalin test, lectins (1 and 5 mg/kg, ip, and 5 to 20 mg/kg, po) inhibited the 1st and 2nd phases (5 and 20 min, respectively), but the effect occurred predominantly on the 2nd phase. The effects of the lectins were totally or partially reversed by naloxone (2 mg/kg, sc) in the 1st and 2nd phases, respectively. Experiments performed with lectins in the absence and presence of avidin (1 mg/kg, ip) and D-mannose (1 mg/kg, ip) showed that avidin did not interfere with the effect of B. seaforthii lectin but partially reversed the effect of B. triquetrum lectin. DMannose completely reversed the effects of both species. F0/60 fractions from both algae significantly increased the latency time in response to thermal stimuli, and naloxone reversed antinociception, indicating the involvement of the opioid system in both the peripheral and central effects of the fractions. In the writhing test, the carbohydrate fractions were the most active, inhibiting the contractions by 71 and 79% (B. triquetrum) and by 46 and 69% (B. seaforthii) at doses of 1 and 5 mg/kg, ip, respectively. Sulfated carbohydrate fractions of B. seaforthii and B. triquetrum, containing only about 5% protein as contaminants, are probably responsible for the antinociceptive effects of these red algae.

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“…4) As a consequence of these properties, they are involved in many biological processes, including host-pathogen interactions, cell-cell communication and induction of apoptosis, cancer metastasis and differentiation, targeting of cells, and recognizing and binding carbohydrates. 5) Lectins have been studied in almost all living organisms, especially in land plants, 6) although the first report on the occurrence of lectins from marine algae was related by Boyd et al 7) In general, algal lectins have a lower molecular mass than higher plant lectins and have no affinity for simple sugars, being more specific for complex oligosaccharides, often glycoproteins. 8) Some algal lectins have been detected and isolated from algae, such as Solieria filiformis, 9) Enantiocladia duperreyi, 10) Pterocladiella capillacea, 11) Vidalia obtusiloba, 12) Gracilaria cornea, 13) and Gracilaria ornate.…”

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confidence: 99%

Antinociceptive and Anti-inflammatory Activities of Lectin from Marine Red Alga Pterocladiella capillacea

Silva

Lima

Araújo

et al. 2010

Biological & Pharmaceutical Bulletin

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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.

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Agglutinins in Marine Algae for Human Erythrocytes

Cited by 104 publications

References 2 publications

Purification and characterisation of a lectin from the red marine alga Pterocladiella capillacea (S.G. Gmel.) Santel. & Hommers.

Purification and characterisation of a lectin from the red marine alga Pterocladiella capillacea (S.G. Gmel.) Santel. & Hommers.

Antinociceptive activity of sulfated carbohydrates from the red algae Bryothamnion seaforthii (Turner) Kütz. and B. triquetrum (S.G. Gmel.) M. Howe

Antinociceptive and Anti-inflammatory Activities of Lectin from Marine Red Alga Pterocladiella capillacea

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