The expression of galactose on IgA paraproteins from patients with multiple myeloma
Апстракт
IgA myeloma for patients is considered prognostically unfavourable. Also, certain IgA myeloma
difficulties are related to structural characteristic of monoclonal IgA. Myeloma IgA express O- and
N-linked glycans, but their glycans can be different from those expressed on IgA of healthy people.
It was reported that loss of Gal residue of the IgA hinge region results in IgA deposits and nephropathy.
The monoclonal IgA were detected by agarose gel electrophoresis and identified by immunoelectrophoresis.
To assess polymerization and galactose expression, IgA was isolated from myeloma
patients by affinity chromatography on Protein M agarose.
Isolated proteins were analysed by non-reducing SDS-PAGE and all isolates contained multiple
protein fractions with the most intensely coloured fractions representing IgA monomers and
dimers. Western blot was used to confirm the presence of IgA monomer and dimers, but also the
presence of incomplete IgA molecules (intermediary of IgA synthesis ...or degraded IgA molecules) in
all samples. Expression of galactose on IgA was assessed by lectin blot with a D-galactose-binding
lectin, Ricinus communis lectin I (RCA-I). The result showed that galactose was expressed on both
monomeric and dimeric IgA. In some isolates galactose is expressed only on monomeric form while
in other isolates galactose is strongly expressed on IgA dimer but its expression on monomeric form
was weak.
This heterogeneity underscores the structural diversity of IgA in myeloma. Understanding its
impact on disease progression necessitates correlating structural features with clinical data.
Извор:
Book of abstracts / VII Symposium of the Serbian Proteomics Association – SePA “Application of proteomics in biomedicine”, Belgrade, Serbia, June 6th, 2024, 2024, 13-13Издавач:
- Belgrade : University of Belgrade – Faculty of Chemistry
Финансирање / пројекти:
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200015 (Универзитет у Београду, Институт за медицинска истраживања) (RS-MESTD-inst-2020-200015)
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200287 (Иновациони центар Технолошко-металуршког факултета у Београду доо) (RS-MESTD-inst-2020-200287)
Институција/група
Institut za medicinska istraživanjaTY - CONF AU - Vukadinović, Marija AU - Kosanović, Dejana AU - Ristić, Biljana AU - Savić, Olivera AU - Ilić, Vesna PY - 2024 UR - http://rimi.imi.bg.ac.rs/handle/123456789/1525 AB - IgA myeloma for patients is considered prognostically unfavourable. Also, certain IgA myeloma difficulties are related to structural characteristic of monoclonal IgA. Myeloma IgA express O- and N-linked glycans, but their glycans can be different from those expressed on IgA of healthy people. It was reported that loss of Gal residue of the IgA hinge region results in IgA deposits and nephropathy. The monoclonal IgA were detected by agarose gel electrophoresis and identified by immunoelectrophoresis. To assess polymerization and galactose expression, IgA was isolated from myeloma patients by affinity chromatography on Protein M agarose. Isolated proteins were analysed by non-reducing SDS-PAGE and all isolates contained multiple protein fractions with the most intensely coloured fractions representing IgA monomers and dimers. Western blot was used to confirm the presence of IgA monomer and dimers, but also the presence of incomplete IgA molecules (intermediary of IgA synthesis or degraded IgA molecules) in all samples. Expression of galactose on IgA was assessed by lectin blot with a D-galactose-binding lectin, Ricinus communis lectin I (RCA-I). The result showed that galactose was expressed on both monomeric and dimeric IgA. In some isolates galactose is expressed only on monomeric form while in other isolates galactose is strongly expressed on IgA dimer but its expression on monomeric form was weak. This heterogeneity underscores the structural diversity of IgA in myeloma. Understanding its impact on disease progression necessitates correlating structural features with clinical data. PB - Belgrade : University of Belgrade – Faculty of Chemistry C3 - Book of abstracts / VII Symposium of the Serbian Proteomics Association – SePA “Application of proteomics in biomedicine”, Belgrade, Serbia, June 6th, 2024 T1 - The expression of galactose on IgA paraproteins from patients with multiple myeloma EP - 13 SP - 13 UR - https://hdl.handle.net/21.15107/rcub_rimi_1525 ER -
@conference{ author = "Vukadinović, Marija and Kosanović, Dejana and Ristić, Biljana and Savić, Olivera and Ilić, Vesna", year = "2024", abstract = "IgA myeloma for patients is considered prognostically unfavourable. Also, certain IgA myeloma difficulties are related to structural characteristic of monoclonal IgA. Myeloma IgA express O- and N-linked glycans, but their glycans can be different from those expressed on IgA of healthy people. It was reported that loss of Gal residue of the IgA hinge region results in IgA deposits and nephropathy. The monoclonal IgA were detected by agarose gel electrophoresis and identified by immunoelectrophoresis. To assess polymerization and galactose expression, IgA was isolated from myeloma patients by affinity chromatography on Protein M agarose. Isolated proteins were analysed by non-reducing SDS-PAGE and all isolates contained multiple protein fractions with the most intensely coloured fractions representing IgA monomers and dimers. Western blot was used to confirm the presence of IgA monomer and dimers, but also the presence of incomplete IgA molecules (intermediary of IgA synthesis or degraded IgA molecules) in all samples. Expression of galactose on IgA was assessed by lectin blot with a D-galactose-binding lectin, Ricinus communis lectin I (RCA-I). The result showed that galactose was expressed on both monomeric and dimeric IgA. In some isolates galactose is expressed only on monomeric form while in other isolates galactose is strongly expressed on IgA dimer but its expression on monomeric form was weak. This heterogeneity underscores the structural diversity of IgA in myeloma. Understanding its impact on disease progression necessitates correlating structural features with clinical data.", publisher = "Belgrade : University of Belgrade – Faculty of Chemistry", journal = "Book of abstracts / VII Symposium of the Serbian Proteomics Association – SePA “Application of proteomics in biomedicine”, Belgrade, Serbia, June 6th, 2024", title = "The expression of galactose on IgA paraproteins from patients with multiple myeloma", pages = "13-13", url = "https://hdl.handle.net/21.15107/rcub_rimi_1525" }
Vukadinović, M., Kosanović, D., Ristić, B., Savić, O.,& Ilić, V.. (2024). The expression of galactose on IgA paraproteins from patients with multiple myeloma. in Book of abstracts / VII Symposium of the Serbian Proteomics Association – SePA “Application of proteomics in biomedicine”, Belgrade, Serbia, June 6th, 2024 Belgrade : University of Belgrade – Faculty of Chemistry., 13-13. https://hdl.handle.net/21.15107/rcub_rimi_1525
Vukadinović M, Kosanović D, Ristić B, Savić O, Ilić V. The expression of galactose on IgA paraproteins from patients with multiple myeloma. in Book of abstracts / VII Symposium of the Serbian Proteomics Association – SePA “Application of proteomics in biomedicine”, Belgrade, Serbia, June 6th, 2024. 2024;:13-13. https://hdl.handle.net/21.15107/rcub_rimi_1525 .
Vukadinović, Marija, Kosanović, Dejana, Ristić, Biljana, Savić, Olivera, Ilić, Vesna, "The expression of galactose on IgA paraproteins from patients with multiple myeloma" in Book of abstracts / VII Symposium of the Serbian Proteomics Association – SePA “Application of proteomics in biomedicine”, Belgrade, Serbia, June 6th, 2024 (2024):13-13, https://hdl.handle.net/21.15107/rcub_rimi_1525 .