Glycosylation of IgG B cell receptor (IgG BCR) in multiple myeloma: relationship between sialylation and the signal activity of IgG BCR
Samo za registrovane korisnike
2008
Autori
Ilić, Vesna![](/themes/MirageRIMI/images/orcid.png)
Milošević-Jovčić, Nadežda
Petrović, Sonja
![](/themes/MirageRIMI/images/orcid.png)
Marković, Dragana
![](/themes/MirageRIMI/images/orcid.png)
Stefanović, Gordana
Ristić, Tatjana
Članak u časopisu (Objavljena verzija)
![](/themes/MirageRIMI//images/creativecommons/arr.png)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
Little is known about the glycosylation of the isotype switched B cell receptor (BCR) in multiple myeloma, and the way it might affect receptor function. In this work IgG BCRs isolated from the individual lysates of peripheral blood lymphocytes (PBL) of 32 patients with IgG multiple myeloma and healthy controls were investigated for the expression of sialic acid (SA), galactose (Gal) and N-acetylglucosamine (GlcNAc), the sugars known to specify the glycoforms of human serum IgG. The degree of glycosylation and signaling status of all 32 isolated myeloma IgG BCRs were correlated and compared with the glycosylation of the IgG paraproteins isolated from sera of the same patients. It was shown that BCR IgG in myeloma is more heavily sialylated when compared with normal controls, that the increased sialylation of IgG BCR is associated with higher levels of tyrosine phosphorylation (signaling activity) of the IgG BCR supramolecular complex and that BCR IgG and serum IgG paraprotein from the ...same patient differed in all cases in the levels of terminal sugar expression. The results suggest that the development of the malignant clone in MM from post-switch B cells expressing IgG BCR at their surfaces to plasma cells secreting IgG paraprotein may be followed by permanent glycosylation changes in the IgG molecules.
Ključne reči:
multiple myeloma / IgG BCR / signaling activity / glycosylationIzvor:
Glycoconjugate Journal, 2008, 25, 4, 383-392Izdavač:
- Springer, Dordrecht
DOI: 10.1007/s10719-007-9101-9
ISSN: 0282-0080
PubMed: 18188696
WoS: 000254302800009
Scopus: 2-s2.0-41149114122
Institucija/grupa
Institut za medicinska istraživanjaTY - JOUR AU - Ilić, Vesna AU - Milošević-Jovčić, Nadežda AU - Petrović, Sonja AU - Marković, Dragana AU - Stefanović, Gordana AU - Ristić, Tatjana PY - 2008 UR - http://rimi.imi.bg.ac.rs/handle/123456789/201 AB - Little is known about the glycosylation of the isotype switched B cell receptor (BCR) in multiple myeloma, and the way it might affect receptor function. In this work IgG BCRs isolated from the individual lysates of peripheral blood lymphocytes (PBL) of 32 patients with IgG multiple myeloma and healthy controls were investigated for the expression of sialic acid (SA), galactose (Gal) and N-acetylglucosamine (GlcNAc), the sugars known to specify the glycoforms of human serum IgG. The degree of glycosylation and signaling status of all 32 isolated myeloma IgG BCRs were correlated and compared with the glycosylation of the IgG paraproteins isolated from sera of the same patients. It was shown that BCR IgG in myeloma is more heavily sialylated when compared with normal controls, that the increased sialylation of IgG BCR is associated with higher levels of tyrosine phosphorylation (signaling activity) of the IgG BCR supramolecular complex and that BCR IgG and serum IgG paraprotein from the same patient differed in all cases in the levels of terminal sugar expression. The results suggest that the development of the malignant clone in MM from post-switch B cells expressing IgG BCR at their surfaces to plasma cells secreting IgG paraprotein may be followed by permanent glycosylation changes in the IgG molecules. PB - Springer, Dordrecht T2 - Glycoconjugate Journal T1 - Glycosylation of IgG B cell receptor (IgG BCR) in multiple myeloma: relationship between sialylation and the signal activity of IgG BCR EP - 392 IS - 4 SP - 383 VL - 25 DO - 10.1007/s10719-007-9101-9 ER -
@article{ author = "Ilić, Vesna and Milošević-Jovčić, Nadežda and Petrović, Sonja and Marković, Dragana and Stefanović, Gordana and Ristić, Tatjana", year = "2008", abstract = "Little is known about the glycosylation of the isotype switched B cell receptor (BCR) in multiple myeloma, and the way it might affect receptor function. In this work IgG BCRs isolated from the individual lysates of peripheral blood lymphocytes (PBL) of 32 patients with IgG multiple myeloma and healthy controls were investigated for the expression of sialic acid (SA), galactose (Gal) and N-acetylglucosamine (GlcNAc), the sugars known to specify the glycoforms of human serum IgG. The degree of glycosylation and signaling status of all 32 isolated myeloma IgG BCRs were correlated and compared with the glycosylation of the IgG paraproteins isolated from sera of the same patients. It was shown that BCR IgG in myeloma is more heavily sialylated when compared with normal controls, that the increased sialylation of IgG BCR is associated with higher levels of tyrosine phosphorylation (signaling activity) of the IgG BCR supramolecular complex and that BCR IgG and serum IgG paraprotein from the same patient differed in all cases in the levels of terminal sugar expression. The results suggest that the development of the malignant clone in MM from post-switch B cells expressing IgG BCR at their surfaces to plasma cells secreting IgG paraprotein may be followed by permanent glycosylation changes in the IgG molecules.", publisher = "Springer, Dordrecht", journal = "Glycoconjugate Journal", title = "Glycosylation of IgG B cell receptor (IgG BCR) in multiple myeloma: relationship between sialylation and the signal activity of IgG BCR", pages = "392-383", number = "4", volume = "25", doi = "10.1007/s10719-007-9101-9" }
Ilić, V., Milošević-Jovčić, N., Petrović, S., Marković, D., Stefanović, G.,& Ristić, T.. (2008). Glycosylation of IgG B cell receptor (IgG BCR) in multiple myeloma: relationship between sialylation and the signal activity of IgG BCR. in Glycoconjugate Journal Springer, Dordrecht., 25(4), 383-392. https://doi.org/10.1007/s10719-007-9101-9
Ilić V, Milošević-Jovčić N, Petrović S, Marković D, Stefanović G, Ristić T. Glycosylation of IgG B cell receptor (IgG BCR) in multiple myeloma: relationship between sialylation and the signal activity of IgG BCR. in Glycoconjugate Journal. 2008;25(4):383-392. doi:10.1007/s10719-007-9101-9 .
Ilić, Vesna, Milošević-Jovčić, Nadežda, Petrović, Sonja, Marković, Dragana, Stefanović, Gordana, Ristić, Tatjana, "Glycosylation of IgG B cell receptor (IgG BCR) in multiple myeloma: relationship between sialylation and the signal activity of IgG BCR" in Glycoconjugate Journal, 25, no. 4 (2008):383-392, https://doi.org/10.1007/s10719-007-9101-9 . .