| 1991 |
CD43 binds ICAM-1 (CD54) as a ligand, demonstrated by specific binding of Daudi cells to purified immobilized CD43 and inhibition by anti-CD43 antibodies and CD43-containing liposomes; expression of human CD43 in a murine T-cell hybridoma enhanced antigen-specific T-cell activation. |
Cell binding assay with purified immobilized CD43, inhibition with anti-CD43 mAb and CD43-liposomes, T-cell hybridoma transfection |
Nature |
High |
1683685
|
| 1991 |
CD43-mediated T-cell activation requires its intracellular domain (which is hyperphosphorylated during activation); expression of CD43 cDNA in antigen-responsive murine T-cell hybridoma enhanced antigen-specific activation; antigen-presenting cells bind specifically to immobilized purified CD43. |
cDNA transfection of CD43 and cytoplasmic domain mutants into T-cell hybridoma, purified CD43 binding assay |
Nature |
High |
2023632
|
| 1992 |
CD43 expressed on opposing cells interferes with T-cell LFA-1 binding to ICAM-1; this anti-adhesive effect is dependent on sialic acid residues on CD43, as neuraminidase treatment of CD43-positive HeLa cells diminished the effect. |
T-lymphocyte adhesion assay to CD43-transfected HeLa cells; antibody blocking; neuraminidase treatment |
Proceedings of the National Academy of Sciences of the United States of America |
High |
1594606
|
| 1989 |
CD43 engagement activates phospholipase C signaling pathway in T cells and monocytes: anti-CD43 mAb L10 induced phosphoinositide hydrolysis, generating diacylglycerol and inositol phosphates, PKC translocation from cytosol to membrane, and increased intracellular Ca2+; CD43 signaling proceeds independently of TCR/CD3. |
Phosphoinositide hydrolysis assay, PKC translocation assay, intracellular Ca2+ measurement in PBMC, T cells, monocytes, and leukemic T cell lines |
Journal of immunology (Baltimore, Md. : 1950) |
High |
2542404
|
| 1995 |
CD43-deficient mice show enhanced T-cell proliferation, increased homotypic adhesion, and increased ICAM-1 and fibronectin binding, demonstrating that CD43 negatively regulates T-cell activation and adhesion; CD43-knockout mice also showed augmented anti-vaccinia CTL response but increased viral load. |
CD43-knockout mouse generation, in vitro proliferation assays (ConA, anti-CD3, SEB, allostimulation), adhesion assays, viral infection model |
Nature |
High |
7566153
|
| 1995 |
CD43 functions as a CD28-independent costimulatory receptor on murine T cells; expression cloning identified murine CD43 as the antigen for mAb R2/60, which synergizes with TCR engagement to induce T-cell proliferation independently of CD28. |
Expression cloning, T-cell proliferation assay with anti-CD43 mAb in CD28-deficient mice |
The Journal of experimental medicine |
High |
7790813
|
| 1996 |
CD43 cross-linking induces association of CD43 with Fyn kinase via Fyn's SH3 domain binding to a proline-rich sequence (300ERQPAPALPPKPPKP314) in CD43's cytoplasmic tail; CD43 cross-linking also results in Fyn tyrosine phosphorylation. |
Co-immunoprecipitation, GST-Fyn SH3 pulldown from T-cell lysates, synthetic peptide competition assay, tyrosine phosphorylation assay |
The Journal of biological chemistry |
High |
8910342
|
| 1998 |
CD43 cross-linking in human T lymphocytes induces tyrosine phosphorylation of Shc and Vav, formation of a Shc/GRB2/Vav complex, enhanced Vav-SLP-76 complex formation, and ERK2 activation and nuclear translocation; CD43-mediated signals activate the MAP kinase pathway leading to IL-2 gene expression. |
Co-immunoprecipitation, tyrosine phosphorylation assay, luciferase reporter assay (Fos SRE), ERK2 kinase activation assay |
The Journal of biological chemistry |
High |
9603925
|
| 1998 |
CD43 is actively excluded from the T cell–APC contact site in an antigen-dependent manner; CD3 signaling alone can induce this exclusion. CD45 is not excluded, indicating this is a specific property of CD43. |
Fluorescence microscopy of T cell–APC conjugates |
Journal of immunology (Baltimore, Md. : 1950) |
Medium |
9862667
|
| 1999 |
Crosslinking CD34 or CD43 on immature hematopoietic KG1a cells activates the same signaling pathway (Lyn, Syk, and novel tyrosine-phosphorylated proteins) leading to cytoadhesion; cap formation of CD34 or CD43 colocalizes with F-actin, and cap formation is required for Syk and pp77 phosphorylation and cytoadhesion (blocked by cytochalasin D). |
Co-immunoprecipitation, cytochalasin D inhibition, anti-phosphotyrosine Western blot, immunofluorescence |
Blood |
Medium |
10339479
|
| 1996 |
CD43 ligation of a hyposialylated CD43 isoform (recognized by mAb J393) on Jurkat T cells induces apoptosis via tyrosine kinase activation; herbimycin A diminished apoptosis and phosphatase inhibitor enhanced it; CD43-mediated apoptosis is potentiated by co-engagement of CD3/TCR or integrins CD18/CD29; apoptosis is associated with decreased nuclear NF-κB. |
Apoptosis assay, tyrosine phosphorylation assay, kinase/phosphatase inhibitor treatment, NF-κB nuclear localization |
The Journal of biological chemistry |
Medium |
8910360
|
| 2000 |
CD43 ligation on normal peripheral human T cells is sufficient to induce IL-2, CD69, and CD40-L gene expression and activate NF-AT, AP-1 (c-Jun containing), and NF-κB (p65) transcription factors; this is partially inhibited by cyclosporin A (Ca2+ pathway) and staurosporine (PKC pathway). |
EMSA for transcription factor DNA binding, cytokine/activation marker expression assays, pharmacological inhibition |
The Journal of biological chemistry |
Medium |
10908570
|
| 2001 |
CD43 is a T cell counterreceptor for sialoadhesin (Siglec-1) on macrophages; CD43 expressed in COS cells supports increased binding to immobilized sialoadhesin; binding is sialic acid-dependent and requires Arg97 in the sialoadhesin binding site; both core 1 and core 2 O-glycan forms of CD43 support binding. |
Sialoadhesin-Fc pulldown/precipitation from T-cell lysates, COS cell expression with sialoadhesin binding assay, Siglec-1 R97A mutant, CHO cells expressing defined CD43 glycoforms |
Journal of immunology (Baltimore, Md. : 1950) |
High |
11238599
|
| 2001 |
CD43 mediates dendritic cell maturation upon cross-linking: anti-CD43 F(ab')2 (but not monovalent Fab) induced upregulation of HLA-DR, CD54, CD40, CD80, CD86, CD83, cytokine release (IL-1β, IL-6, TNF-α, IL-12, IL-10), intracellular Ca2+ rise, and tyrosine phosphorylation of a 25-kDa protein in dendritic cells. |
Flow cytometry for surface marker upregulation, ELISA for cytokines, Ca2+ flux assay, tyrosine phosphorylation assay; comparison of intact Ab vs F(ab')2 vs Fab |
Journal of immunology (Baltimore, Md. : 1950) |
Medium |
10352244
|
| 2002 |
hnRNP-K and Purα act together to repress transcriptional activity of the CD43 gene promoter during activation of K562 cells; these proteins bind single-stranded DNA sequences in the CD43 promoter; CD43 mRNA levels are dramatically downregulated during K562 activation, coinciding with promoter repression. |
Transcriptional reporter assay, RT-PCR for CD43 mRNA, identification of hnRNP-K and Purα as promoter-binding repressors |
Blood |
Medium |
12411317
|
| 2002 |
CD43 distribution on T cells is regulated by a membrane-proximal ezrin-binding site; failure to displace CD43 from the immunological synapse does not inhibit primary T cell activation, but CD43 expression at T cell–matrix contact does not negatively regulate motility while it may regulate LFA-1 de-adhesion. |
Fluorescence microscopy with CD43 mutants lacking ezrin-binding site, T-cell activation and motility assays |
Journal of immunology (Baltimore, Md. : 1950) |
Medium |
11937524
|
| 2003 |
CD43 recruits the ζ-chain as part of its signaling pathway in human T lymphocytes and NK cells; CD43 engagement leads to ζ-chain tyrosine phosphorylation creating docking sites for ZAP-70 and Vav; Lck is required for ζ-chain phosphorylation downstream of CD43; CD43 engagement concentrates the ζ-chain toward the bead attachment site. |
Co-immunoprecipitation, in vitro kinase assay, ζ-chain redistribution imaging, Lck-deficient JCaM.1 cell experiments |
Journal of immunology (Baltimore, Md. : 1950) |
High |
12902492
|
| 2004 |
CD43 negative regulation of T-cell activation operates through an intracellular mechanism, not steric hindrance: a GPI-linked CD43 ectodomain construct failed to reverse CD43−/− T-cell hyperproliferation; an intracellular-only CD43 (small ectodomain of hCD16 fused to CD43 cytoplasmic tail) reversed hyperproliferation; exclusion of the CD43 intracellular region from the immunological synapse is required for regulation of IL-2 production. |
Reconstitution of CD43 mutants (GPI-linked ectodomain, intracellular-only chimera, ERM-binding mutant) in CD43−/− T cells; proliferation and IL-2 production assays |
The Journal of experimental medicine |
High |
15117976
|
| 2005 |
CD43 functions as an E-selectin ligand on activated T cells; a 130-kDa glycoform of CD43 is precipitated by E-selectin-IgG chimera from Th1 cells in a sialic acid-dependent manner; CD43-IgG chimera generated in CHO cells expressing FucT-VII and C2GnT supports E-selectin-dependent cell rolling under flow conditions. |
E-selectin-IgG pulldown/immunoprecipitation, O-sialoglycoprotein endopeptidase treatment, mAb 1B11 identification, CHO cell reconstitution with defined glycosyltransferases, flow chamber rolling assay |
Journal of immunology (Baltimore, Md. : 1950) |
High |
16339541
|
| 2005 |
CD34 and CD43 act as negative regulators of mast cell adhesion; loss of CD43 and/or CD34 causes gene-dose-dependent increase in mast cell homotypic aggregation; reexpression of CD34 or CD43 reverses this phenotype; loss of these sialomucins also prevents mast cell repopulation in vivo. |
CD34/CD43 double-KO mouse mast cell analysis, re-expression rescue experiments, in vitro aggregation assay, in vivo reconstitution |
Immunity |
High |
15664158
|
| 2006 |
CD43 bearing either core 1 or core 2 O-glycans binds galectin-1 and is required for maximal T-cell susceptibility to galectin-1-induced death; galectin-1 binding clusters CD43 on the T-cell surface; loss of CD43 reduced galectin-1-induced death and galectin-1 binding by ~50%. |
CD43-deficient T cells, galectin-1 binding assay, galectin-1 death assay, CD43 fusion proteins with defined glycoforms (core 1 vs core 2), microscopy for CD43 clustering |
Journal of immunology (Baltimore, Md. : 1950) |
High |
17015718
|
| 2007 |
CD43 collaborates with PSGL-1 to mediate E-selectin-dependent T-cell migration into inflamed skin in vivo; CD43-deficient Th1 cells showed reduced E-selectin-binding activity; PSGL-1/CD43 double-deficient Th1 cells show the most profound decrease, demonstrating additive roles. |
CD43−/− and PSGL-1−/− mice, E-selectin binding assay, in vivo adoptive transfer migration assay to inflamed skin |
Journal of immunology (Baltimore, Md. : 1950) |
High |
17277158
|
| 2007 |
CD43 regulates T-cell trafficking through phosphorylation at Ser76 in its cytoplasmic tail; mutation of Ser76 to alanine greatly diminishes T-cell trafficking to the lymph node while leaving CD43 exclusion from the synapse and CD43-mediated regulation of T-cell proliferation intact; the CD43 extracellular domain is also required for trafficking. |
Tandem mass spectrometry identification of phospho-Ser76, CD43 Ser76Ala mutant reconstitution in CD43−/− T cells, lymph node trafficking assay |
Blood |
High |
17638845
|
| 2009 |
Galectin-1 binds CD43 and CD45 on dendritic cells, inducing unipolar co-clustering of these receptors; galectin-1 activates Syk and PKC signaling in DCs, with phosphorylated Syk recruited to the CD43/CD45 co-cluster; Syk and PKC inhibitors abrogate galectin-1-induced DC activation, IL-6 production, MMP gene upregulation, and enhanced migration. |
Kinome screen, Syk phosphorylation assay, co-cluster imaging, PKC/Syk inhibitors, cytokine ELISA, migration assay, in vivo intradermal injection |
The Journal of biological chemistry |
High |
19635795
|
| 2009 |
The CD43 ectodomain is shed from granulocytes, mast cells, and T cells (but not macrophages); after γ-secretase cleavage, the CD43 cytoplasmic tail (CD43ct) translocates to the nucleus; inhibition of nuclear translocation or γ-secretase cleavage is proapoptotic; CD43ct is modified by SUMO-1 and colocalizes with promyelocytic nuclear bodies; CD43-deficient cells show reduced PML nuclear bodies and increased sensitivity to apoptosis. |
CD43/CD34 transmembrane-domain chimeras, viability assays, nuclear fractionation, SUMO-1 modification assay, γ-secretase inhibitor, PML nuclear body colocalization imaging |
Blood |
High |
19696198
|
| 2011 |
CD43 interaction with ERM proteins is required for CD43 phosphorylation at Ser76; mutation of Ser76 to a phosphomimetic (S76D) enhances T-cell migration and CD43 movement to the distal pole complex while blocking ERM association; protein kinase Cθ can phosphorylate CD43 at Ser76. |
Phospho-specific antibody, CD43 Ser76 mutants (S76A, S76D) reconstitution in CD43−/− T cells, migration assay, ERM co-immunoprecipitation, PKCθ kinase assay |
Molecular biology of the cell |
High |
21289089
|
| 2015 |
CD43 is a dominant E-selectin ligand specifically in Th17 cells, functioning independently of PSGL-1; CD43-deficient Th17 cells show impaired accumulation on E-selectin under flow and impaired rolling on TNF-α-treated microvessels in vivo; CD43−/− mice are protected from EAE with impaired Th17 cell recruitment to spinal cord. |
Flow chamber E-selectin binding assay with PSGL-1−/−, CD43−/−, and double-KO Th17 cells; intravital microscopy; in vivo air pouch recruitment; EAE model |
Journal of immunology (Baltimore, Md. : 1950) |
High |
26700769
|
| 2020 |
Virion-incorporated CD43 (and PSGL-1) inhibit HIV-1 cell-free infection and transinfection by preventing virus attachment to CD4+ cells and CD4− fibroblastic reticular cells, irrespective of Env; the inhibitory effect requires the full-length ectodomain (demonstrated for PSGL-1); CD43 and PSGL-1 cocluster with assembling HIV-1 Gag at the plasma membrane. |
Virion infectivity assay, virus attachment assay (CD4+ and CD4− cells), Env-deleted virus controls, full-length vs truncated PSGL-1 constructs, Gag coclustering imaging |
Proceedings of the National Academy of Sciences of the United States of America |
High |
32193343
|
| 2014 |
CD43 coclusters with assembling HIV-1 Gag at the plasma membrane through polybasic motifs in the CD43 cytoplasmic tail and in the Gag matrix domain; mutation of the polybasic sequence in CD43 cytoplasmic tail reduces its coclustering with Gag; replacement of cytoplasmic tails of non-coclustering proteins with CD43/PSGL-1 tails confers coclustering. |
Quantitative two-color superresolution localization microscopy, Gag matrix domain basic residue mutants, chimeric transmembrane protein tail-swap constructs |
Journal of virology |
High |
25320329
|
| 1997 |
CD43 associates with the cytoskeleton in neutrophils via F-actin; anti-CD43 crosslinking induces CD43 redistribution to caps at the uropod, dependent on the actomyosin system (blocked by cytochalasin B and butanedione monoxime); colchicine and chemotactic factor fNLP also drive CD43 redistribution to the uropod independently of mAb crosslinking, suggesting CD43 is involved in cell polarization. |
Triton X-100 solubility assay for cytoskeletal association, immunofluorescence, electron microscopy, cytochalasin B and BDM inhibition |
Journal of cell science |
Medium |
9224764
|
| 1997 |
Core 2 N-acetylglucosaminyltransferase (C2GnT) modifies CD43 O-glycans, converting the 115-kDa (core 1, S7 epitope) glycoform to the 130-kDa (core 2, 1B11 epitope) glycoform; transfection of C2GnT into EL-4 cells caused gain of 1B11 epitope and loss of S7 epitope, with ~10 kDa molecular weight increase. |
C2GnT transfection into EL-4 cells, flow cytometry with S7 and 1B11 antibodies, SDS-PAGE molecular weight analysis |
Glycobiology |
Medium |
9061371
|
| 1999 |
CD43 expression on T cells mediates T-cell homing to lymph nodes and Peyer's patches; anti-CD43 mAb L11 blocks T-cell binding to HEV in vitro and inhibits T-cell extravasation from blood into lymphoid tissues in vivo, without affecting binding to purified vascular ligands for L-selectin, α4β7, or LFA-1. |
HEV binding assay in vitro, in vivo lymphocyte trafficking assay, antibody blocking with selectin/integrin panel |
The Journal of experimental medicine |
Medium |
9126930
|
| 1999 |
CD43 ligation on T cells induces the CD43-Fyn interaction and mediates homotypic aggregation requiring CD43 association with cytoskeleton; the CD43 signaling pathway leading to Ca2+ mobilization and IL-2 production involves Shc, GRB2, Vav, and ERK2 activation. |
Referenced from 1996 and 1998 papers; reviewed in context of T-cell activation |
Immunologic research |
Low |
10580634
|
| 2003 |
CD43-mediated homotypic aggregation of T lymphocytes requires Src kinases, PLCγ2, PKC, PI3K, ERK1/2, and p38; these signaling molecules regulate actin cytoskeleton remodeling after CD43 ligation; leflunomide blocks Src kinase target recruitment and actin polymerization downstream of CD43, diminishing aggregation. |
Pharmacological inhibitors of Src, PLCγ, PKC, PI3K, ERK, p38; F-actin staining; leflunomide treatment; homotypic aggregation assay |
Journal of leukocyte biology |
Medium |
12972508
|
| 2001 |
CD43-mediated apoptosis in TF-1 myeloid progenitor cells involves repression of AP-1 DNA binding activity and downregulation of 14-3-3 proteins and GM-CSF receptor β; this is followed by translocation of proapoptotic Bad to mitochondria; Daxx overexpression inhibits CD43-mediated apoptosis; co-immobilized anti-ICAM-3/CD99 partly suppress apoptosis. |
Immobilized anti-CD43 mAb apoptosis assay, DNA array screening, AP-1 EMSA, Bad localization assay, Daxx overexpression |
The Journal of biological chemistry |
Medium |
11773067
|
| 2011 |
M-ficolin binds to CD43 on neutrophils in a sialic acid-dependent manner (Y271F mutant unable to bind sialic acid fails to bind neutrophils or modulate their functions); endogenous M-ficolin secreted by fMLP-activated neutrophils binds to CD43; M-ficolin binding induces cell polarization, adhesion, and homotypic aggregation, phenocopying anti-CD43 antibody crosslinking. |
Recombinant M-ficolin binding assay with blocking anti-CD43 mAb, Western blot of neutrophil lysate with rM-ficolin, Y271F sialic-acid-binding mutant, immunofluorescence colocalization, functional adhesion/aggregation assay |
Journal of leukocyte biology |
High |
22167719
|
| 1999 |
CD43 ligation on NK cells induces secretion of RANTES, MIP-1α, and MIP-1β chemokines (blocked by tyrosine kinase inhibitor genistein); increases cytotoxic activity; and activates PYK-2 tyrosine kinase. |
ELISA for chemokines, cytotoxicity assay, anti-phosphotyrosine immunoprecipitation, PYK-2 kinase assay, genistein inhibition |
Blood |
Medium |
10515880
|
| 2021 |
MSC-derived ICAM-1 interacts with CD43 on activated T cells; blockade of either ICAM-1 on MSCs or CD43 on T cells reversed rapid suppression of proinflammatory cytokine (TNF-α, IFN-γ) mRNA expression; ICAM-1/CD43 interaction disrupts CD43-mediated TCR microcluster formation to limit T-cell activation, and suppresses TCR-proximal signaling and Ca2+ flux. |
ICAM-1 and CD43 blocking antibodies in MSC-T cell coculture; cytokine mRNA quantification; TCR microcluster imaging; Ca2+ signaling assay |
Frontiers in immunology |
Medium |
33692786
|
| 2008 |
CD43 regulates Th2 differentiation; CD43−/− T cells show decreased calcium flux upon TCR ligation and preferentially differentiate into Th2 cells in vitro, associated with increased GATA-3 nuclear translocation; CD43−/− mice exhibit increased Th2-mediated allergic airway inflammation in vivo. |
CD43−/− T cells, Ca2+ flux assay, Th1/Th2 differentiation protocol, GATA-3 nuclear translocation assay, allergic airway disease model |
Journal of immunology (Baltimore, Md. : 1950) |
Medium |
18490738
|
| 2004 |
CD43 expressed by cancer cell lines (PSN-1, SW1222) mediates adhesion to human peritoneal mesothelial cells (HPMC) via interaction with ICAM-1; anti-CD43 antibody significantly reduced tumor cell adhesion to HPMC; β2 integrin inhibition did not reduce this adhesion. |
Western blot and flow cytometry for CD43 expression, fluorometric adhesion assay with inhibitory anti-CD43 antibody vs anti-β2 integrin antibody |
Biological chemistry |
Medium |
15449712
|
| 1989 |
CD43 is rapidly superphosphorylated on serine residues within minutes of phorbol ester (PMA) treatment of lymphocytes; ConA and anti-CD3 also cause CD43 superphosphorylation, albeit delayed; CD43 is constitutively superphosphorylated on serine and tyrosine in continuously growing T, B, and non-lymphoid cell lines. |
Metabolic radiolabeling with 32P, immunoprecipitation of CD43, SDS-PAGE |
Scandinavian journal of immunology |
Medium |
2531463
|
| 1986 |
gpL115 (CD43) is a heavily glycosylated transmembrane sialoglycoprotein; purification established that it is 52% carbohydrate by weight (asialo form), with major O-linked carbohydrate residues being galactose and N-acetylgalactosamine in equimolar amounts; amino acid composition shows high proline and serine/threonine content typical of mucin-like proteins. |
Sequential affinity chromatography purification (lentil lectin, wheat germ lectin, peanut lectin Sepharose), amino acid composition analysis, carbohydrate analysis |
The Journal of biological chemistry |
High |
3711098
|
| 2019 |
CD43 functions as an E-selectin ligand on PSGL-1-deficient lymphoblasts; knockdown of CD43 on NALL-1 B-precursor ALL cells resulted in reduced rolling on E-selectin and decreased tissue engraftment in immunodeficient mice. |
Flow adhesion assay, E-selectin binding, RNA interference knockdown of CD43, xenograft engraftment assay in irradiated immunodeficient mice |
Cancers |
Medium |
31461905
|