This monoclonal antibody also bound to nearly all human peripheral blood B cells, although more recent reports have not replicated this finding.

Siglec-6 expression on human mast cells has since been extended to those isolated and cultured from skin and the mast cell lines HMC-1.2, LUVA, ROSA KITWT, and ROSA KITD816V, regardless of KIT mutation status, even when cell-surface expression of the related receptor Siglec-8 is lost.

By introducing mutated versions of Siglec-6 lacking the key tyrosine residues in the ITIM, the ITSM, or both into a trophoblast cell line and treating the cell with the phosphatase inhibitor pervanadate, it was determined that both motifs are capable of being phosphorylated and that Siglec-6 is able to recruit SHP-2 upon phosphorylation of these motifs.

[18] Furthermore, binding of glycodelin A to trophoblast cell lines was found to reduce ERK1/2 phosphorylation, c-Jun protein and mRNA levels, MMP2 and uPA mRNA levels, and invasiveness in a sialic acid- and Siglec-6-dependent manner, suggesting that Siglec-6 reduces trophoblast invasiveness in response to encountering glycodelin A expression in the decidualized endometrium.

[9] Antibody ligation of Siglec-6 reduced mast cell degranulation in response to lower levels of the stimuli that act through these receptors.

[9] Additionally, the inhibitory effect of Siglec-6 ligation remained for at least 4.5 hours, perhaps due to the observed stability of the receptor on the cell surface following antibody ligation, suggesting that the receptor may continue to participate in inhibitory signaling for prolonged periods of time.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.