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
Abstract
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
Publication date:
4.1.2007.
Visits: 1.879 *