Disease relevance of Spn

• Quantitative bacteriology showed that macrophages (M(phi)) from wild-type mice (CD43(+/+)) bound M. avium, Mycobacterium bovis (bacillus Calmette-Guérin), and Mycobacterium tuberculosis (strain H37Rv), whereas M(phi) from CD43 knockout mice (CD43(-/)-) did not [1].
• To drive expression of leukosialin in mature B cells, the immunoglobulin heavy chain enhancer was fused to the mCD43 gene. mCD43-immunoglobulin heavy chain enhancer transgenic mice display splenomegaly due to increased numbers of B cells [2].
• Amplification and rearrangement of melF/mouse CD43 (leukosialin) gene encoding a highly glycosylated membrane protein gp120 in Friend erythroleukemia cells [3].
• In leukocytes such as thymocytes and basophilic leukemia cells, a glycosilated integral membrane protein called CD43 (leukosialin or sialophorin), which is defective in patients with Wiskott-Aldrich syndrome, was highly concentrated in the cleavage furrow during cytokinesis [4].
• Evidence that leukosialin, CD43, is intensely sulfated in the murine T lymphoma line RDM-4 [5].

High impact information on Spn

• CD43 (sialophorin, leukosialin, leukocyte large sialoglycoprotein), a heavily sialylated molecule found on most leukocytes and platelets, was initially identified as a major glycoprotein of mouse, rat and human T cells [6].
• We have resolved B220+ IgM- B-lineage cells in mouse bone marrow into four fractions based on differential cell surface expression of determinants recognized by S7 (leukosialin, CD43), BP-1, and 30F1 (heat stable antigen) [7].
• Concentration of an integral membrane protein, CD43 (leukosialin, sialophorin), in the cleavage furrow through the interaction of its cytoplasmic domain with actin-based cytoskeletons [4].
• Disregulation of leukosialin (CD43, Ly48, sialophorin) expression in the B-cell lineage of transgenic mice increases splenic B-cell number and survival [2].
• Our results therefore suggest that O-linked oligosaccharides on leukosialin express lineage restricted and even maturation restricted antigenic structures that might serve as cell lineage specific markers [8].

Biological context of Spn

• The gene has been found to be encoded on four separate exons, and it thus differs from the cell surface mucin leukosialin, whose coding region is contained on one exon, but is similar to glycophorin and CD34, other cell surface mucins whose genes are divided into multiple coding exons [9].
• The nucleotide sequence of Ly 48 (mouse leukosialin, sialophorin): the mouse homolog of CD43 [10].
• A lack of introns has previously been observed for the human leukosialin gene (Shelley, C. S., Remold-O'Donnell, E., Rosen, F. S. and Whitehead, A. S., Biochem. J., submitted) [11].
• CD43 (leukosialin), a sialylated glycoprotein expressed on the surface of most hematopoietic cells, has been implicated in cell adhesion and signaling [12].
• The other mouse gene was an intronless pseudogene for a leukosialin-related sequence [11].

Anatomical context of Spn

• We studied the role of CD43 (leukosialin/sialophorin), the negatively charged sialoglycoprotein of leukocytes, in the binding of mycobacteria to host cells [1].
• Cocapping studies and immunoprecipitation experiments performed with GA3 and L10, an anti-sialophorin monoclonal antibody reacting with leukosialin (Gp 105) on K562 cells, demonstrate that the antigen detected by GA3 on K562 cells is identical to leukosialin [8].
• CD43 (leukosialin) expression has previously been demonstrated on the surface of developing B cells in mouse bone marrow and on plasma cells induced in vitro, but not on peripheral B cells in spleen [13].
• CD43 (sialophorin, gpL115) is a sialoglycoprotein expressed on a wide variety of blood cells including lymphocytes, monocytes, neutrophils, and platelets [14].
• Protein sequence and gene structure for mouse leukosialin (CD43), a T lymphocyte mucin without introns in the coding sequence [11].

Associations of Spn with chemical compounds

• Specific labeling of the sialoglycoproteins of RDM-4 cells indicates that leukosialin, the most intensely labeled protein, comigrates with the sulfated protein on SDS-PAGE at varying acrylamide concentrations [5].

Other interactions of Spn

• Blocking studies with various antibodies revealed that leukosialin (S11 monoclonal antibodies) and TNF alpha were important for Thy-1+DEC migration [15].
• Soluble forms of leukosialin or lamp-1 may be useful as therapeutic agents for the inhibition of E-selectin-mediated binding to tumor cells [16].
• Results from lectin chromatography and N-glycanase and neuraminidase studies suggest that the 3E8 antigen is a heavily sialylated O-linked glycoprotein [17].

Analytical, diagnostic and therapeutic context of Spn

• To determine whether Ly 48 is expressed by specific subsets of epidermal cells (ECs) such as Langerhans cells, keratinocytes, or dendritic epidermal T cells (DETCs), we utilized flow cytometry to detect staining of ECs by a panel of four monoclonal antibodies (S11, S15, S7, and 3E8) that recognize two different epitopes of the leukosialin antigen [18].

References