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Mouse (Murine) CD43 Protein expressed in Human Cells - ABIN2008256
Pallant, Eskenazi, Mattei, Fournier, Carlsson, Fukuda, Frelinger: Characterization of cDNAs encoding human leukosialin and localization of the leukosialin gene to chromosome 16. in Proceedings of the National Academy of Sciences of the United States of America 1989
this study identifies a new signaling pathway for CD43 through the regulation of alternative functions of pyruvate kinase isoform M2, favoring cell survival following activation
Forty percent of adenoid cystic carcinomas showed staining for CD43, while no cases of basal cell carcinoma were positive
CD43 expression is a novel adverse prognostic factor for patients with diffuse large B-cell lymphomas
CD43 polymorphisms are associated with TB susceptibility.
Host membrane protein PSGL-1 (show SELPLG Proteins), CD43, and CD44 (show CD44 Proteins) association with assembling HIV-1 Gag is driven by polybasic sequences present in the cytoplasmic tails of the membrane proteins and in Gag.
When used as vaccine in mice, the 2/165 phagotope raised antibodies against the UN1/CD43 antigen, indicating that the 2/165 phagotope mimicked the UN1 antigen structure, and could represent a novel immunogen for cancer immunotherapy
CD43 promotes cells transformation by preventing merlin (show NF2 Proteins)-mediated contact inhibition of growth.
We conclude that CD43 is an adverse prognostic marker in DLBCL, and is preferentially expressed in the non-GCB (show GBA Proteins) subgroup.
CD43 regulates the threshold for T cell activation by targeting Cbl (show CBL Proteins) functions.
Taken together, these results show that elevated calcium levels induce CD43 capping, and macrophages remove the cells if their nucleolin (show NCL Proteins) receptors can bind to the poly-N-acetyllactosaminyl chains of capped CD43.
glycosylation status of CD43 protein on leukemia cells is associated with sensitivity to CTL-mediated cytolysis
findings demonstrate that CD43 is a major E-selectin (show SELE Proteins) ligand in Th17 cells that functions independent of P-selectin glycoprotein ligand-1 (show SELPLG Proteins)
CD43 may be an important mediator of macrophage lipid homeostasis, thereby affecting macrophage foam cell formation and ultimately atherosclerotic plaque development.
We have identified a robust physiologic role for CD43 in a relevant animal model and established an important in vivo function for CD43-dependent regulation of IFN-gamma (show IFNG Proteins) production.
Results show that while CD43 binding to ezrin-radixin-moesin (show MSN Proteins) proteins is crucial for S76 phosphorylation, CD43 movement and regulation of T-cell migration can occur through an ERM (show ETV5 Proteins)-independent, phosphorylation-dependent mechanism.
study found that the M. tuberculosis Cpn60.2 molecular chaperone (show HSP90AA1 Proteins) is the major mycobacterial surface ligand that interacts with CD43 to stabilize the interaction between M. tuberculosis and the macrophage
Transient resistance to B16F10 melanoma growth and metastasis in CD43-/- mice.
CD43 engagement and signaling are involved in the costimulatory and antiapoptotic effects of enzymatically inactive mutant trypanosomal trans-sialidase when it binds highly sialylated mucin (show SLC13A2 Proteins) CD43 on the T cell surface.
Cd43 displays dynamic roles in T cell immunity: a positive regulatory role in costimulation and trafficking of T cells to the central nervous system, and a negative regulatory role in the down-modulation of an immune response.
Delayed onset of experimental autoimmune encephalomyelitis in CD43-deficient immunized mice and in recipients of adoptively transferred CD43-/- cells is characterized by significant reduction of T cell trafficking to the brain and spinal cord.
The protein encoded by this gene is a major sialoglycoprotein found on the surface of thymocytes, T lymphocytes, monocytes, granulocytes, and some B lymphocytes. It may be part of a physiologic ligand-receptor complex involved in T-cell activation. During T-cell activation, this protein is actively removed from the T-cell-APC (antigen-presenting cell) contact site, suggesting a negative regulatory role in adaptive immune response.
, leukocyte sialoglycoprotein
, sialophorin (gpL115, leukosialin, CD43)
, W3/13 antigen
, 3E8 antigen
, B-cell differentiation antigen LP-3
, lymphocyte antigen 48