2014
DOI: 10.5114/reum.2014.47230
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Serum IgG galactosylation in psoriatic arthritis patients undergoing a biological treatment. A preliminary report

Abstract: S t r e s z c z e n i eCel pracy: Grupa pacjentów z łuszczycowym zapaleniem stawów (ŁZS, 11 osób) została poddana leczeniu. Od każdego pacjenta pobrano dwie próbki surowicy: przed leczeniem (próbka before) i po zakończeniu leczenia (próbka after). Wykonane badanie miało na celu uzyskanie informacji, czy leczenie pacjentów z ŁZS poprawia galaktozylację N-glikanów w IgG, co zostało uprzednio wykazane dla pacjentów z reumatoidalnym zapaleniem stawów (RZS). Materiał i metody: Immunoglobulinę G (IgG) izolowano z su… Show more

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(2 citation statements)
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“…It should also be mentioned that in lectin-ELISA method, glycan-lectin reaction reflect the reactions that occur in living organisms, including the availability of sugar residues for lectins, which additionally allows to deepen the knowledge about mechanisms of these interactions. The profile and degree of IgG sialylation and galactosylation/agalactosylation was determined using modified solid phase enzyme-linked immunosorbent assay, lectin-ELISA described by us earlier [31][32][33][34] . The method was based on the reactivity of IgG glycan moieties with specific biotinylated lectins: Maackia amurensis agglutinin (MAA, recognizing sialic acid α2,3-linked) and Sambucus nigra agglutinin (SNA, which recognize sialic acid α2,6-linked), Ricinus communis agglutinin I (RCA-I) which detect the terminal galactose; Griffonia simplicifolia lectin II (GSL-II) detecting the terminal GlcNAc (Vector Laboratories Inc., Burlingame, CA, USA).…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…It should also be mentioned that in lectin-ELISA method, glycan-lectin reaction reflect the reactions that occur in living organisms, including the availability of sugar residues for lectins, which additionally allows to deepen the knowledge about mechanisms of these interactions. The profile and degree of IgG sialylation and galactosylation/agalactosylation was determined using modified solid phase enzyme-linked immunosorbent assay, lectin-ELISA described by us earlier [31][32][33][34] . The method was based on the reactivity of IgG glycan moieties with specific biotinylated lectins: Maackia amurensis agglutinin (MAA, recognizing sialic acid α2,3-linked) and Sambucus nigra agglutinin (SNA, which recognize sialic acid α2,6-linked), Ricinus communis agglutinin I (RCA-I) which detect the terminal galactose; Griffonia simplicifolia lectin II (GSL-II) detecting the terminal GlcNAc (Vector Laboratories Inc., Burlingame, CA, USA).…”
Section: Discussionmentioning
confidence: 99%
“…Another important aspect was the comparison of native serum IgG glycosylation with glycosylation of IgG isolated from serum, and evaluation the potential diagnostic suitability of glycan analysis when glycoprotein is not isolated earlier from biological fluid. The degree of IgG sialylation and galactosylation/agalactosylation was analysed using a modified solid phase enzyme-linked immunosorbent assay, lectin-ELISA [31][32][33][34] .…”
mentioning
confidence: 99%