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Original scientific paper

Aberrant Glycosylation of Igg Heavy Chain in Multiple Myeloma

Igor Aurer
Gordan Lauc
Jerka Dumić
Dubravko Rendić
Danica Matišić
Marija Miloš
Marija Heffer-Lauc
Mirna Flogel
Boris Labar

Fulltext: english, pdf (221 KB) pages 247-251 downloads: 581* cite
APA 6th Edition
Aurer, I., Lauc, G., Dumić, J., Rendić, D., Matišić, D., Miloš, M., ... Labar, B. (2007). Aberrant Glycosylation of Igg Heavy Chain in Multiple Myeloma. Collegium antropologicum, 31 (1), 247-251. Retrieved from https://hrcak.srce.hr/27277
MLA 8th Edition
Aurer, Igor, et al. "Aberrant Glycosylation of Igg Heavy Chain in Multiple Myeloma." Collegium antropologicum, vol. 31, no. 1, 2007, pp. 247-251. https://hrcak.srce.hr/27277. Accessed 15 May 2021.
Chicago 17th Edition
Aurer, Igor, Gordan Lauc, Jerka Dumić, Dubravko Rendić, Danica Matišić, Marija Miloš, Marija Heffer-Lauc, Mirna Flogel and Boris Labar. "Aberrant Glycosylation of Igg Heavy Chain in Multiple Myeloma." Collegium antropologicum 31, no. 1 (2007): 247-251. https://hrcak.srce.hr/27277
Harvard
Aurer, I., et al. (2007). 'Aberrant Glycosylation of Igg Heavy Chain in Multiple Myeloma', Collegium antropologicum, 31(1), pp. 247-251. Available at: https://hrcak.srce.hr/27277 (Accessed 15 May 2021)
Vancouver
Aurer I, Lauc G, Dumić J, Rendić D, Matišić D, Miloš M, et al. Aberrant Glycosylation of Igg Heavy Chain in Multiple Myeloma. Collegium antropologicum [Internet]. 2007 [cited 2021 May 15];31(1):247-251. Available from: https://hrcak.srce.hr/27277
IEEE
I. Aurer, et al., "Aberrant Glycosylation of Igg Heavy Chain in Multiple Myeloma", Collegium antropologicum, vol.31, no. 1, pp. 247-251, 2007. [Online]. Available: https://hrcak.srce.hr/27277. [Accessed: 15 May 2021]

Abstracts
Although the majority of eukaryotic proteins are glycosylated, there is a dearth of knowledge regarding protein sugar
moieties and their changes in disease. Most multiple myeloma cases are characterized by production of monoclonal
immunoglobulins (Ig). We studied galactosylation and sialylation of IgG heavy chains in 16 patients with IgG myeloma
using lectin blotting and densitometry. In comparison to age and sex matched controls, galactosylation was reduced in
multiple myeloma (median 317 vs. 362, range 153–410 vs. 309–447 relative units, p=0.015, Student’s t-test). Sialylation
was stage dependent; samples from patients with stage IIA had lowest amounts of sialic acid, IIIA intermediate and IIIB
highest (142.6 vs. 185.9 vs. 248.5 relative units, correlation coefficient r=0.55). Both galactosylation and sialylation levels
were independent of age, sex, treatment type, response to treatment, disease duration and IgG and b2 microglobulin
concentration. These data indicate that multiple myeloma is characterized by aberrant immunoglobulin glycosylation.

Keywords
multiple myeloma; immunoglobulins; glycosylation; sialylation; galactosylation

Hrčak ID: 27277

URI
https://hrcak.srce.hr/27277

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