Serum sialyltransferase and fucosyltransferase activities in patients with multiple myeloma

Frithz, Göran; Ronquist, Gunnar; Ericsson, Per

doi:10.1016/0277-5379(85)90107-5

Cited by 12 publications

(5 citation statements)

References 15 publications

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“…Nishiura et al (52) found hypogalactosylated IgG paraproteins and reduced galactosyltransferase activity in bone marrow cells from patients with multiple myeloma. In contrast, other studies showed high levels of oversialylated IgG Abs in the serum from patients with multiple myeloma and increased sialyltransferase activity in their peripheral mononuclear cells (53)(54)(55). Therefore, the high sialylation observed in the anaphylactic IgG1 might be due to increased glycosyltransferase, specially sialyltransferase, activity mediated by distinct enzymes during its synthesis.…”

Section: Discussionmentioning

confidence: 82%

Sialic Acid Residues Are Essential for the Anaphylactic Activity of Murine IgG1 Antibodies

Silva

Casabuono

Jacysyn

et al. 2008

The Journal of Immunology

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Glycosylation of the Ab molecule is essential for maintaining the functional structure of Fc region and consequently for Ab-mediated effector functions, such as binding to cells or complement system activation. Alterations in the composition of the sugar moiety can dramatically influence Ab activity; however, it is not completely clear how differences in the N-linked oligosaccharide structure impact the biological function of Abs. We have described that murine IgG1 Abs can be separated according to their ability to elicit in vivo anaphylaxis in a fraction of anaphylactic and other of non-anaphylactic molecules. Furthermore, we showed that the N-linked oligosaccharide chain is essential for the structural conformation of the anaphylactic IgG1, the binding to FcγRIII on mast cells, and, consequently, for the ability to mediate anaphylactic reactions. In this study, we evaluated the contribution of individual sugar residues to this biological function. Differences in the glycan composition were observed when we analyzed oligosaccharide chains from anaphylactic or non-anaphylactic IgG1, mainly the presence of more sialic acid and fucose residues in anaphylactic molecules. Interestingly, the enzymatic removal of terminal sialic acid residues in anaphylactic IgG1 resulted in loss of the ability to trigger mast cell degranulation and in vivo anaphylactic reaction, similarly to the deglycosylated IgG1 Ab. In contrast, fucose removal did not affect the anaphylactic function. Therefore, we demonstrated that the ability of murine IgG1 Abs to mediate anaphylaxis is directly dependent on the amount of sialic acid residues associated to the oligosaccharide chain attached to the Fc region of these molecules.

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Section: Discussionmentioning

confidence: 82%

Sialic Acid Residues Are Essential for the Anaphylactic Activity of Murine IgG1 Antibodies

Silva

Casabuono

Jacysyn

et al. 2008

The Journal of Immunology

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“…Frithz et al reported an increase in sialyltransferase and fucosyltransferase activities in serum in 19 untreated patients with myeloma. 29 Patients at the later stages of disease showed higher activity than those at earlier stages. Six subjects followed for 20 months on treatment had a fall in sialyltransferase activity that correlated with the fall in paraprotein concentration.…”

Section: Discussionmentioning

confidence: 95%

“…This finding is consistent with previous reports of increased sialyltransferase activity in the mononuclear cells from such patients. 29 30 32 Previous workers have not been able to detect significant increases in either total serum sialic acid or mononuclear cell sialic acid concentrations. This could be explained as follows.…”

Section: Discussionmentioning

confidence: 99%

Increased sialylation of oligosaccharides on IgG paraproteins--a potential new tumour marker in multiple myeloma.

et al. 1998

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“…Nishiura et al [31] found hypogalactosylated IgG paraproteins and reduced GalT activity in bone marrow cells from patients with multiple myeloma, while Fleming et al [13], Frithz et al [14] and Cohen et al [3] demonstrated oversialylation of IgG paraproteins, an increase in ST activity in serum and peripheral mononuclear cells in patients with myeloma, all suggesting that the dysregulation of enzyme activities causing glycosylation abnormalities in immunoglobulins may perhaps reflect hyper-activation of B cells. Indeed, we found that the IgG BCR is in an activated state in myeloma [17] and that there is a correlation between sialylation of BCR IgG and IgG BCR activation state in this disease.…”

Section: Discussionmentioning

confidence: 99%

Glycosylation of IgG B cell receptor (IgG BCR) in multiple myeloma: relationship between sialylation and the signal activity of IgG BCR

et al. 2008

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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.

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Serum sialyltransferase and fucosyltransferase activities in patients with multiple myeloma

Cited by 12 publications

References 15 publications

Sialic Acid Residues Are Essential for the Anaphylactic Activity of Murine IgG1 Antibodies

Sialic Acid Residues Are Essential for the Anaphylactic Activity of Murine IgG1 Antibodies

Increased sialylation of oligosaccharides on IgG paraproteins--a potential new tumour marker in multiple myeloma.

Glycosylation of IgG B cell receptor (IgG BCR) in multiple myeloma: relationship between sialylation and the signal activity of IgG BCR

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