» Articles » PMID: 10193323

Increased Sialylation of Oligosaccharides on IgG Paraproteins--a Potential New Tumour Marker in Multiple Myeloma

Overview
Journal J Clin Pathol
Specialty Pathology
Date 1999 Apr 8
PMID 10193323
Citations 11
Authors
Affiliations
Soon will be listed here.
Abstract

Aims: To investigate whether changes in carbohydrate structure of IgG are related to malignancy and stage of disease in myeloma and monoclonal gammopathy of uncertain significance (MGUS).

Methods: 61 patients were studied at diagnosis: 14 with MGUS, nine with stage I multiple myeloma, 11 with stage II, 21 with stage III, and five with solitary plasmacytoma. IgG was extracted from serum by protein G affinity chromatography. Oligosaccharides were cleaved from the protein backbone enzymatically by N-glycosidase F. Oligosaccharide analysis was performed by high pressure anion exchange chromatography with pulsed electrochemical detection (HPAE-PED).

Results: Up to 15 oligosaccharide peaks were identified in three major fractions: neutral, monosialylated, and disialylated. Patients with myeloma showed an increase in the proportion of sialylated oligosaccharides in comparison with patients with MGUS. The ratio of neutral to sialylated oligosaccharides (N:S) was reduced at all stages of myeloma compared with MGUS: MGUS, 11.35; myeloma stage I, 7.6 (p = 0.047); stage II, 5.20 (p = 0.035); stage III, 3.60 (p = 0.0002); plasmacytoma, 7.5 (p = 0.046). The N:S ratio was independent of paraprotein concentration (r = 0.05).

Conclusions: The ratio of neutral to sialylated oligosaccharides may act as a new marker of malignancy in IgG paraproteinaemia and warrants further investigation.

Citing Articles

The genetics and epidemiology of N- and O-immunoglobulin A glycomics.

Visconti A, Rossi N, Bondt A, Ederveen A, Thareja G, Koeleman C Genome Med. 2024; 16(1):96.

PMID: 39123268 PMC: 11312925. DOI: 10.1186/s13073-024-01369-6.


Glycation Interferes with the Expression of Sialyltransferases in Meningiomas.

Selke P, Bork K, Zhang T, Wuhrer M, Strauss C, Horstkorte R Cells. 2021; 10(12).

PMID: 34943806 PMC: 8699175. DOI: 10.3390/cells10123298.


Immunoglobulin G Glycosylation in Diseases.

Pezer M Exp Suppl. 2021; 112:395-431.

PMID: 34687018 DOI: 10.1007/978-3-030-76912-3_13.


Proteomics-inspired precision medicine for treating and understanding multiple myeloma.

Ho M, Bianchi G, Anderson K Expert Rev Precis Med Drug Dev. 2021; 5(2):67-85.

PMID: 34414281 PMC: 8372187. DOI: 10.1080/23808993.2020.1732205.


Sialylated Immunoglobulins for the Treatment of Immuno-Inflammatory Diseases.

Markina Y, Gerasimova E, Markin A, Glanz V, Wu W, Sobenin I Int J Mol Sci. 2020; 21(15).

PMID: 32751832 PMC: 7432344. DOI: 10.3390/ijms21155472.


References
1.
AXELSSON U, Bachmann R, Hallen J . Frequency of pathological proteins (M-components) om 6,995 sera from an adult population. Acta Med Scand. 1966; 179(2):235-47. DOI: 10.1111/j.0954-6820.1966.tb05453.x. View

2.
CLAMP J, Putnam F . THE CARBOHYDRATE PROSTHETIC GROUP OF HUMAN GAMMA-GLOBULIN. J Biol Chem. 1964; 239:3233-40. View

3.
Yogeeswaran G, Salk P . Metastatic potential is positively correlated with cell surface sialylation of cultured murine tumor cell lines. Science. 1981; 212(4502):1514-6. DOI: 10.1126/science.7233237. View

4.
Takasaki S, Mizuochi T, Kobata A . Hydrazinolysis of asparagine-linked sugar chains to produce free oligosaccharides. Methods Enzymol. 1982; 83:263-8. DOI: 10.1016/0076-6879(82)83019-x. View

5.
Pamblanco M, Strecker G, Montreuil J, SPIK G, Dorland L, van Halbeek H . Primary structure of the N-glycosidically linked sialoglycans of secretory immunoglobulins A from human milk. Eur J Biochem. 1982; 125(2):383-8. DOI: 10.1111/j.1432-1033.1982.tb06694.x. View