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Effect of red seaweed sulfated galactans on initial steps of complement activation in vitro

The research described here presents data on the effect of galactans of red algae, carrageenans (λ/μ/ν-, κ-, κ/β-, and ι/κ-types), and agar on complement system activation in normal human serum. The experiments were based on well surfaces coated with triggering agents for binding initiating compleme...

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Detalles Bibliográficos
Autores principales: Sokolova, E.V., Kravchenko, A.O., Sergeeva, N.V., Kalinovsky, A.I., Glazunov, V.P., Bogdanovich, L.N., Yermak, I.M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Ltd. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7577181/
https://www.ncbi.nlm.nih.gov/pubmed/33357847
http://dx.doi.org/10.1016/j.carbpol.2020.117251
Descripción
Sumario:The research described here presents data on the effect of galactans of red algae, carrageenans (λ/μ/ν-, κ-, κ/β-, and ι/κ-types), and agar on complement system activation in normal human serum. The experiments were based on well surfaces coated with triggering agents for binding initiating complement components —C3 and C4. The sulfated galactans inhibited C3 binding to lipopolysaccharide with direct dependence on the sulfation degree of polysaccharides. Sulfation degree was also important in carrageenans’ capacity to reduce C4 binding to mannan. However, C4 binding to antibodies was considerably activated by carrageenans, especially with 3,6-anhydrogalactose. The gelling carrageenans were able to block antigen binding centers of total serum IgM and with more intensity than non-gelling. No structural characteristics mattered in ameliorating C5 cleavage by plasmin in extrinsic protease complement activation, but λ/μ/ν- and κ/β-carrageenans almost completely inhibited C5 cleavage. Thus, galactans participated in cell surface biology by imitating surface glycans in inhibition of C3 binding and mannose binding lectin, but as to the tthe heclassical pathway these substances stimulated complement, probably due to their structure based on carrabiose.