Naslov
Aberrant Glycosylation of IgG Heavy Chain in Multiple Myeloma

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

Izvornik
Collegium antropologicum (0350-6134) 31 (2007), 1; 247-251

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
multiple myeloma ; immunoglobulins ; glycosylation ; sialylation ; galactosylation

Sažetak
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.

Izvorni jezik
Engleski

Znanstvena područja
Biologija, Kliničke medicinske znanosti

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