High impact information on SIGLEC10

• Finally, although Siglec-11 shows marked sequence similarity to human Siglec-10 in its extracellular domain, the cytosolic tail appears only distantly related [1].
• Cloning and characterization of Siglec-10, a novel sialic acid binding member of the Ig superfamily, from human dendritic cells [2].
• The identification of Siglec-10 as a new Siglec family member and its expression profile, together with its sialic acid-dependent binding capacity, suggest that it may be involved in cell-cell recognition by interacting with sialylated ligands expressed on specific cell populations [2].
• The full-length Siglec-10 cDNA encodes a type 1 transmembrane protein containing four extracellular immunoglobulin-like domains, a transmembrane region, and a cytoplasmic tail with two classical immunoreceptor tyrosine-based inhibitory motifs [2].
• Various cells and cell lines including monocytes and dendritic cells express Siglec-10 [2].

Biological context of SIGLEC10

• We have obtained a novel cDNA clone from a human dendritic cell cDNA library encoding a protein with sequence and structural features of the Siglec family, hence designated as Siglec-10 [2].
• Siglec-10 exhibited a high degree of sequence similarity to CD33-related Siglecs and mapped to the same region, on chromosome 19q13 [3].
• We confirmed the recruitment of SHP-1 to the Siglec-10 cytoplasmic tail by Western blot analysis and demonstrated that this interaction depends on tyrosine phosphorylation [4].
• Finally, we demonstrated that Siglec-10 was not able to bind SAP/SH2d1A, indicating that the so-called CD150-like motif in Siglec-10 might be a docking site for other signal transduction mediators [4].
• Therefore, the nature of these SLGs from pollen-recessive haplotypes of B. rapa is different from that of SLG2 of B. oleracea [5].

Anatomical context of SIGLEC10

• When expressed on COS-7 cells, Siglec-10 was able to bind human red blood cells and soluble sialoglycoconjugates in a sialic acid-dependent manner [2].
• The molecular properties and expression pattern suggest that Siglec-10 may function as an inhibitory receptor within the innate immune system [3].
• The expression of Siglec-10 Sv3 in T- and B-cells was detected by RT-PCR [4].
• Binding assays determined that the extracellular domain of siglec-10 was capable of binding to peripheral blood leukocytes [6].
• Siglec-10 was identified through database mining of an asthmatic eosinophil EST library [6].

Associations of SIGLEC10 with chemical compounds

• Siglec-5 bound preferentially to GQ1b, but weakly to GT1b, whereas siglec-10 interacted only with GT1b ganglioside [7].
• Previously, SLG2 from a pollen-recessive haplotype, S2, of Brassica oleracea was found to produce two different transcripts, one for the secreted type glycoprotein and the other for a putative membrane-anchored form of SLG [5].

Other interactions of SIGLEC10

• Flow cytometry confirmed surface expression of all these molecules except for CD22 and Siglec-10, where levels were low or undetectable [8].
• CD34+ precursor cells from peripheral blood constitutively expressed surface CD33, Siglec-5 and Siglec-10 [8].
• One common characteristic of all Siglec-10 splice forms (except for Siglec-10 Sv2) is their cytoplasmic tail with two ITIMs and one CD150-like sequence [4].

Analytical, diagnostic and therapeutic context of SIGLEC10

• However, Western blotting was able to detect MC expression of CD22 and Siglec-10, suggesting that these proteins were mostly cytoplasmic [8].
• Using the Stanford G3 radiation hybrid panel we were able to localize the genomic sequence of siglec-10 within the cluster of genes on chromosome 19q13.3-4 that encode other siglec family members [6].

References