Interaction of fucoidan with the proteins of the complement classical pathway

Tissot, Bérangère; Montdargent, Béatrice; Chevolot, Lionel; Varenne, Anne; Descroix, Stéphanie; Gareil, Pierre; Daniel, Régis

doi:10.1016/s1570-9639(03)00230-9

Cited by 66 publications

(50 citation statements)

References 48 publications

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“…This data is in accordance with the literature that correlates anti-inflammatory effects with sulfated fucans but not with sulfated galactans. [3][4][5] On the other hand, Cf-PLS potentiated the edema at some scheme of treatment (Table 2). Cf-PLS at 0.9 mg/kg increased the carrageenan-evoked edema from 0.48Ϯ0.04 to 0.82Ϯ0.06 ml (co-injected with carrageenan) and to 0.8Ϯ0.12 ml (injected 10 min prior carrageenan), 2 h after development.…”

Section: Resultsmentioning

confidence: 96%

“…4,5) It was demonstrated that a sulfatedpolysaccharide fraction extracted from the brown algae Porphyra haitanesis presents an in vivo antioxidant property, causing an increase in the spleen and thymus size, suggestive of an immunostimulant action. 6) Additionally, sulfated galactans of the red marine algae Bryothamnion seaforthii presented antinociceptive activity in mice 7) and of the red micro algae Pophyridium sp.…”

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Biological Effects of a Sulfated-Polysaccharide Isolated from the Marine Red Algae Champia feldmannii

Assreuy

Gomes

Silva

et al. 2008

Biological & Pharmaceutical Bulletin

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Sulfated-polysaccharides are complex macromolecular constituents of the extracellular matrix of marine algae that play an important role in mechanical, osmotic and ionic regulation.1) In Biomedicine the anticoagulant and antithrombotic properties have been most widely exploited and, at least for galactans, appear to be dependent on the sulfatation content and/or position of the sulfate groups.2) A natural sulfated polymer of L-fucose (fucoidan) showed a dose-dependent inhibition of leukocyte migration in the in vivo peritonitis model, 3) and sulfated fucans isolated from brown algae showed potent in vitro and in vivo inhibition of the human complement system. 4,5) It was demonstrated that a sulfatedpolysaccharide fraction extracted from the brown algae Porphyra haitanesis presents an in vivo antioxidant property, causing an increase in the spleen and thymus size, suggestive of an immunostimulant action. 6) Additionally, sulfated galactans of the red marine algae Bryothamnion seaforthii presented antinociceptive activity in mice 7) and of the red micro algae Pophyridium sp. anti-inflammatory action inhibiting eritema formation after topical use in humans.8) However, studies of sulfated galactans role in models of inflammation in vivo are rare in the literature. Here we isolated and investigated the effects of a sulfated galactan from the red marine algae Champia feldmannii, widely encountered along the South East and North East Brazilian sea coast, in experimental models of acute inflammation, coagulation and nociception. MATERIALS AND METHODS AnimalsMale Wistar rats (150-250 g) and Swiss mice (25-35 g) were maintained with a controlled 12/12 h light/dark cycle, at a temperature of 25°C with free access to food and water. The experimental protocols used in this study were approved by the Institutional Animal Care and Use Committee of the State University of Ceará (UECE), Fortaleza-CE, Brazil, in accordance with international guidelines (NIH publication No. 85-23, revised 1985).Algae Champia feldmannii belongs to the order Rhodymeniales, family Lomentariaceae and was collected in the Pacheco beach of Caucaia, Ceará, Brazil. Algae were classified by Wladimir R. L. Farias, Department of Fishery Engeneering of Federal University of Ceará-Brazil.Erythrocytes Human erythrocytes were obtained from healthy donors at the Hematology Center of the Federal University of Ceará-Brazil.Drugs and Reagents Dextran sulphate, L-carrageenan, Evans blue, zymosan, morphine, cethylpiridinium chloride, sodium acetate, calcium chloride, ketamine, sulphuric acid, papain, 1-9-di-metylene blue (DMB), ethylenodiaminotetracetic acid (EDTA), indomethacin, dexamethasone, pentoxifylline, L-N-nitro-arginine methyl ester (L-NAME), meclyzine and formamide, N-acetyl-N,N,N-trimethylammonium bromide, 1,3-diaminopropane, toluidine blue, agarose gel (Sigma Chemical Co., St. Louis, MO, U.S.A. or SigmaAldrich Chemie, Steinheim, Germany); absolute ethanol, sodium chloride, sodium dodecyl sulfate (SDS) and 2-mer- 907, 60.455-970, Fortaleza-Ceará-Brasil. R...

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Section: Resultsmentioning

confidence: 96%

mentioning

confidence: 99%

Biological Effects of a Sulfated-Polysaccharide Isolated from the Marine Red Algae Champia feldmannii

Assreuy

Gomes

Silva

et al. 2008

Biological & Pharmaceutical Bulletin

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“…The C1q molecule classically recognizes Ab-Ag complexes, but it also reacts with structurally different self and nonself targets, including C-reactive protein, bacterial porins, apoptotic cells, extracellular matrix proteins (13), polysaccharides, and prion-protein b-amyloid fibrils (14)(15)(16). C1q has an associated Ca 2+ -dependent tetramer composed of the serine proteases (SPs) C1s-C1r-C1r-C1s (17).…”

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Identification of a Catalytic Exosite for Complement Component C4 on the Serine Protease Domain of C1s

Duncan

Mohlin

Taleski

et al. 2012

The Journal of Immunology

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The classical pathway of complement is crucial to the immune system, but it also contributes to inflammatory diseases when dysregulated. Binding of the C1 complex to ligands activates the pathway by inducing autoactivation of associated C1r, after which C1r activates C1s. C1s cleaves complement component C4 and then C2 to cause full activation of the system. The interaction between C1s and C4 involves active site and exosite-mediated events, but the molecular details are unknown. In this study, we identified four positively charged amino acids on the serine protease domain that appear to form a catalytic exosite that is required for efficient cleavage of C4. These residues are coincidentally involved in coordinating a sulfate ion in the crystal structure of the protease. Together with other evidence, this pointed to the involvement of sulfate ions in the interaction with the C4 substrate, and we showed that the protease interacts with a peptide from C4 containing three sulfotyrosine residues. We present a molecular model for the interaction between C1s and C4 that provides support for the above data and poses questions for future research into this aspect of complement activation.

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“…It has been proposed that both C1r/C1s CUB1-EGF-CUB2 heterodimers are located inside the C1q cone and mediate ionic interactions through acidic residues contributed by the C1r and C1s CUB modules. Such ionic interactions at the C1q/ C1s-C1r-C1r-C1s interface are expected to involve lysine residues of the collagen-like stems of C1q as suggested by the observation that chemical modification of C1q with lysinespecific reagents inhibits C1 assembly and C1q hemolytic activity (4,18).…”

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confidence: 99%

Analysis of Human C1q by Combined Bottom-up and Top-down Mass Spectrometry

Pflieger

Przybylski

Gonnet

et al. 2010

Molecular & Cellular Proteomics

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C1q is a subunit of the C1 complex, a key player in innate immunity that triggers activation of the classical complement pathway. Featuring a unique structural organization and comprising a collagen-like domain with a high level of post-translational modifications, C1q represents a challenging protein assembly for structural biology. We report for the first time a comprehensive proteomics study of C1q combining bottom-up and top-down analyses.

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Interaction of fucoidan with the proteins of the complement classical pathway

Cited by 66 publications

References 48 publications

Biological Effects of a Sulfated-Polysaccharide Isolated from the Marine Red Algae Champia feldmannii

Biological Effects of a Sulfated-Polysaccharide Isolated from the Marine Red Algae Champia feldmannii

Identification of a Catalytic Exosite for Complement Component C4 on the Serine Protease Domain of C1s

Analysis of Human C1q by Combined Bottom-up and Top-down Mass Spectrometry

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