Affinage

SELP

P-selectin · UniProt P16109

Round 2 corrected
Length
830 aa
Mass
90.8 kDa
Annotated
2026-04-28
130 papers in source corpus 43 papers cited in narrative 43 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

P-selectin (SELP/CD62P/GMP-140) is a Ca²⁺-dependent lectin that functions as the principal rapid-response adhesion receptor on activated platelets and endothelial cells, mediating the initial tethering and rolling of neutrophils, monocytes, and lymphocyte subsets on the vascular wall during inflammation and hemostasis. Stored in platelet α-granules and endothelial Weibel-Palade bodies alongside von Willebrand factor, SELP is mobilized to the plasma membrane within minutes by thrombin, histamine, oxidants, or complement C5b-9; its 35-residue cytoplasmic tail is necessary and sufficient for granule targeting, and an alternatively spliced soluble form circulates in plasma (PMID:2411738, PMID:2472431, PMID:1378326, PMID:1372646). The N-terminal lectin domain recognizes sialyl-Lewis x on glycoprotein ligands—principally PSGL-1 (which also requires tyrosine sulfation for high-affinity binding), but also CD24, GP Ibα, CD44, sulfatides, and the chondroitin sulfate chains of versican—through a shallow binding groove defined by critical residues Lys113, Tyr48, and Tyr94 (PMID:7505206, PMID:11081633, PMID:7681324, PMID:9129046, PMID:10499919, PMID:10950950). Beyond adhesion, engagement of PSGL-1 triggers outside-in signaling through FGR/SYK to extend β₂ integrins on rolling leukocytes, induces procoagulant tissue-factor-bearing microparticle release, anchors ultra-large VWF strings to endothelium, promotes neutrophil superoxide production, and—when blocked after thrombus formation—facilitates fibrinolysis and thrombus resolution (PMID:20445017, PMID:12858167, PMID:14630802, PMID:7690799, PMID:38385292).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 1985 High

    The discovery that GMP-140 redistributes from platelet α-granule membranes to the cell surface upon thrombin activation established it as an activation-dependent surface marker and suggested a role in post-activation cell-cell interactions.

    Evidence Immunogold labeling of resting versus thrombin-stimulated human platelets

    PMID:2411738

    Open questions at the time
    • No function for the surface-expressed protein was known
    • Endothelial expression had not been examined
  2. 1989 High

    Cloning of the SELP cDNA and parallel localization studies revealed a modular lectin-type adhesion molecule stored in both platelet α-granules and endothelial Weibel-Palade bodies, with alternative splicing generating a soluble isoform, and showed that it specifically mediates Ca²⁺-dependent adhesion of activated platelets to neutrophils and monocytes.

    Evidence cDNA sequencing, immunogold double-labeling with vWF in endothelial cells, platelet-leukocyte rosetting assays with antibody blocking and Ca²⁺ chelation, biosynthetic labeling

    PMID:2463989 PMID:2466574 PMID:2467701 PMID:2470733 PMID:2472431 PMID:2478294

    Open questions at the time
    • Precise carbohydrate ligand not yet defined
    • Counter-receptor identity unknown
    • Mechanism of granule targeting not resolved
  3. 1990 High

    Gain-of-function transfection of GMP-140 into COS cells demonstrated that SELP alone is sufficient to mediate Ca²⁺-dependent neutrophil adhesion, and genomic analysis revealed a 17-exon gene with each exon encoding a distinct structural domain.

    Evidence COS cell transfection adhesion assay with purified protein controls; genomic cloning and PCR-confirmed splice variants

    PMID:1689464 PMID:1701178

    Open questions at the time
    • Specific carbohydrate determinant recognized by the lectin domain still debated (Lex vs. sLex)
    • In vivo rolling function not yet demonstrated
  4. 1991 High

    Identification of sialyl-Lewis x as the core carbohydrate recognition motif, together with the demonstration that SELP-mediated tethering operates independently of CD18 integrins but cooperates with PAF signaling for firm adhesion, defined the two-step adhesion cascade paradigm; additional stimuli (oxidants, complement C5b-9) were shown to mobilize SELP to the endothelial surface.

    Evidence Carbohydrate competition and glycosyltransferase-transfection binding assays; antibody blocking of GMP-140 and CD11/CD18 on histamine/thrombin-stimulated endothelium; oxidant and complement stimulation with Ca²⁺/kinase inhibitors; radioligand binding with neuraminidase

    PMID:1699666 PMID:1704009 PMID:1704376 PMID:1712483 PMID:1717478 PMID:1717488 PMID:2470750

    Open questions at the time
    • Identity of the high-molecular-weight glycoprotein counter-receptor not yet cloned
    • Signaling events downstream of leukocyte engagement unclear
    • Role of sulfatide binding in vivo unknown
  5. 1992 High

    Biochemical identification of a ~120 kDa glycoprotein counter-receptor on neutrophils, demonstration that the last 23 amino acids of the SELP cytoplasmic tail are necessary and sufficient for regulated granule sorting, and detection of a circulating soluble monomeric form in plasma resolved key questions about ligand identity, trafficking, and physiology.

    Evidence Affinity chromatography with ¹²⁵I-P-selectin and systematic immunodepletion; domain-swap chimeras in AtT20 cells with immunogold EM; ELISA and gel filtration of plasma SELP

    PMID:1372646 PMID:1378326 PMID:1378449

    Open questions at the time
    • Counter-receptor cDNA not cloned
    • Structural basis of lectin-domain–ligand interaction unknown
    • Role of lymphocyte binding not defined in vivo
  6. 1993 High

    Expression cloning of PSGL-1 as the principal glycoprotein ligand for P-selectin, together with site-directed mutagenesis mapping the lectin-domain binding groove to residues Lys113, Tyr48, and Tyr94, established both sides of the P-selectin–ligand interface and showed that PSGL-1 requires fucosylation for function.

    Evidence HL-60 cDNA expression cloning with COS-cell reconstitution; homology-modeled mutagenesis panel with myeloid cell binding assays

    PMID:7505206 PMID:7681324 PMID:7690799

    Open questions at the time
    • Crystal structure of the P-selectin–PSGL-1 complex not yet solved
    • Contribution of tyrosine sulfation to PSGL-1 binding unknown
    • Distinction between multiple P-selectin ligands in vivo not resolved
  7. 1997 High

    Identification of CD24 as an additional P-selectin ligand on neutrophils and tumor cells expanded the ligand repertoire beyond PSGL-1 and implicated P-selectin in cancer-associated platelet adhesion.

    Evidence CD24 purification, bead-based P-selectin-IgG binding, CD24 transfection into tumor cells with platelet adhesion readout

    PMID:9129046

    Open questions at the time
    • Relative contribution of CD24 versus PSGL-1 in vivo not determined
    • Structural basis of CD24–P-selectin interaction unknown
  8. 1999 High

    GP Ibα was identified as a Ca²⁺-independent P-selectin counter-receptor whose recognition requires tyrosine sulfation but not sLex, distinguishing its binding mode from that of PSGL-1 and demonstrating ligand diversity.

    Evidence P-selectin-transfected cell adhesion to immobilized GP Ibα, rolling on histamine-stimulated endothelium, antibody blocking

    PMID:10499919

    Open questions at the time
    • Structural basis of GP Ibα–P-selectin contact not defined
    • Functional role in platelet–platelet or platelet–VWF interactions uncertain
  9. 2000 High

    Crystal structures of the P-selectin lectin-EGF fragment co-complexed with sLex and with the sulfated N-terminus of PSGL-1 provided atomic-resolution understanding of how dual recognition of sLex and sulfated tyrosine yields high-affinity binding, and versican's chondroitin sulfate chains were identified as extracellular matrix ligands.

    Evidence X-ray crystallography of P-selectin LE domain with ligands; solid-phase binding of soluble P-selectin to versican and GAG competition

    PMID:10950950 PMID:11081633

    Open questions at the time
    • Full-length P-selectin structure with all consensus repeats not determined
    • Role of versican binding in leukocyte recruitment in vivo untested
  10. 2003 High

    P-selectin was shown to anchor ultra-large VWF strings to endothelial surfaces and to generate procoagulant tissue-factor-bearing microparticles through PSGL-1 engagement, linking SELP directly to coagulation and thrombus propagation.

    Evidence Co-immunoprecipitation from histamine-activated endothelium, AFM bond-strength measurement, Psgl1⁻/⁻ mouse microparticle studies, hemophilia A mouse rescue by microparticle infusion

    PMID:12858167 PMID:14630802

    Open questions at the time
    • Mechanism by which P-selectin–VWF interaction facilitates ADAMTS13 cleavage not fully resolved
    • Source of tissue factor on microparticles not definitively assigned
  11. 2010 High

    Dissection of the signaling cascade downstream of PSGL-1 engagement on rolling neutrophils revealed that P-selectin triggers FGR/SYK-dependent extension of LFA-1, establishing the molecular link between selectin-mediated rolling and integrin activation.

    Evidence Microfluidic rolling assays with conformational reporter antibodies for LFA-1, kinase inhibitors, PSGL-1 blocking

    PMID:20445017

    Open questions at the time
    • Full signaling cascade from PSGL-1 to FGR/SYK activation not mapped
    • Whether the same pathway operates for monocytes and lymphocytes untested
  12. 2024 High

    Post-thrombotic P-selectin blockade was shown to reduce leukocyte infiltration, neutrophil ROS production, monocyte tissue factor expression, and thrombus density while promoting urokinase-mediated fibrinolysis, demonstrating that P-selectin actively sustains thrombus burden after formation.

    Evidence Mouse IVC stenosis model with anti-P-selectin antibody, intravital microscopy, flow cytometry, scanning EM, uPA measurement

    PMID:38385292

    Open questions at the time
    • Translatability to human venous thromboembolism not established
    • Whether soluble P-selectin contributes to thrombus maintenance in this model unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include the full-length structure of P-selectin with all nine complement repeats, the relative in vivo contributions of non-PSGL-1 ligands (CD24, GP Ibα, CD44, versican) to different inflammatory and thrombotic contexts, the complete outside-in signaling network triggered by PSGL-1 engagement, and the therapeutic window for P-selectin blockade in human thromboinflammatory disease.
  • No full-length crystal or cryo-EM structure
  • Relative ligand contributions in different disease models remain genetically unresolved
  • Clinical translation data not captured in the mechanistic timeline

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098631 cell adhesion mediator activity 7 GO:0048018 receptor ligand activity 3
Localization
GO:0031410 cytoplasmic vesicle 5 GO:0005886 plasma membrane 4 GO:0005576 extracellular region 2
Pathway
R-HSA-168256 Immune System 5 R-HSA-1500931 Cell-Cell communication 4 R-HSA-5653656 Vesicle-mediated transport 4 R-HSA-109582 Hemostasis 2
Partners
CD24FGRGP1BASELPLGSYKTLR4VCANVWF

Evidence

Reading pass · 43 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1985 GMP-140 (SELP/P-selectin) is an alpha-granule membrane protein of platelets that is redistributed to the plasma membrane upon thrombin stimulation, as demonstrated by immunogold labeling of resting versus activated platelets. Immunocytochemistry with monoclonal antibody S12, immunogold labeling, and saponin permeabilization on resting and thrombin-stimulated platelets The Journal of cell biology High 2411738
1989 GMP-140 (SELP) cDNA encodes a cysteine-rich protein with modular domains: an N-terminal lectin domain, an EGF-like domain, nine tandem complement-binding consensus repeats, a transmembrane domain, and a cytoplasmic tail. Alternative splicing predicts a soluble secreted form lacking the transmembrane segment. cDNA cloning and sequence analysis from platelet/endothelial cell libraries Cell High 2466574
1989 GMP-140 (SELP) is synthesized by vascular endothelial cells and is stored in Weibel-Palade bodies, co-localizing with von Willebrand factor, as demonstrated by immunogold double-labeling; histamine stimulation rapidly redistributes GMP-140 to the plasma membrane. Immunoperoxidase tissue distribution, [35S]cysteine biosynthetic labeling, immunogold double-label on frozen thin sections, histamine stimulation The Journal of clinical investigation High 2472431
1989 PADGEM/GMP-140 (SELP) on activated platelets mediates adhesion to neutrophils, monocytes, HL-60, and U937 cells; this interaction is inhibited by anti-PADGEM antibodies and EDTA (Ca2+-dependence), but not by anti-GPIIb-IIIa or anti-thrombospondin antibodies, establishing SELP as the specific adhesion receptor. Platelet-leukocyte rosetting assay, antibody blocking, phospholipid vesicle binding assay Cell High 2478294
1989 PADGEM/GMP-140 (SELP) is localized to Weibel-Palade bodies of endothelial cells (co-localizing with vWF by double immunofluorescence), and disappears from these structures upon secretagogue stimulation. Immunofluorescence double-labeling with anti-PADGEM and anti-vWF antibodies, secretagogue stimulation Blood High 2467701
1989 GMP-140 (SELP) stimulated secretion from endothelial Weibel-Palade bodies is accompanied by rapid redistribution of GMP-140 to the cell surface, occurring within 3 min of histamine stimulation and subsequently removed by an endocytic mechanism; surface expression is agonist-dose dependent and parallels vWF secretion. Dual-label immunofluorescence, monoclonal antibody S12 binding kinetics, paraformaldehyde fixation and 4°C arrest to trap surface expression The Journal of biological chemistry High 2470733
1989 GMP-140 (SELP) contains 28.8% carbohydrate by weight (including sialic acid, neutral sugars, N-acetylglucosamine), and N-linked oligosaccharides account for >50 kDa of apparent molecular weight. Biosynthesis involves a 98–125 kDa high-mannose precursor that matures to 140 kDa within 40–60 min. The majority of the protein mass is extracytoplasmic. Amino acid composition, enzymatic removal of N-linked oligosaccharides, pulse-chase biosynthetic labeling, protease treatment of activated platelets plus Western blot The Journal of biological chemistry High 2463989
1989 GMP-140 (SELP) binds heparin in a divalent cation-independent manner; binding is inhibited by excess heparin and other sulfated glycans (fucoidan, dextran sulfate) but not by chondroitin sulfates, establishing GMP-140 as a heparin-binding protein. Heparin-Sepharose affinity chromatography, radioiodinated GMP-140 binding to heparin-Matrex beads with competitive inhibition assays Biochemical and biophysical research communications Medium 2480118
1990 GMP-140 (SELP) expressed on activated endothelial cells mediates rapid neutrophil adhesion; neutrophils and HL-60 cells bind specifically to COS cells transfected with GMP-140 cDNA and to purified GMP-140-coated surfaces; binding requires extracellular Ca2+ but not active neutrophil metabolism. COS cell transfection with GMP-140 cDNA, adhesion assays with purified protein-coated microtiter wells, antibody blocking, metabolic inhibitors, Ca2+ chelation Nature High 1689464
1990 GMP-140 (SELP) gene spans >50 kb and contains 17 exons, with almost all exons encoding distinct structural domains (lectin, EGF, each of the nine consensus repeats, transmembrane region). The soluble and 8-repeat variant forms arise from alternative splicing of distinct exons. Genomic library cloning, restriction mapping, exon sequencing, PCR amplification of alternative transcripts from platelet and endothelial cell RNA The Journal of biological chemistry High 1701178
1990 CD15 (lacto-N-fucopentaose III, Lex) on neutrophils and monocytes is a component of the PADGEM/GMP-140 (SELP) ligand; anti-CD15 antibodies inhibit leukocyte-platelet binding, and the CD15 trisaccharide directly inhibits binding of HL-60 cells to PADGEM-expressing COS cells and purified PADGEM vesicles. Antibody blocking with panel of anti-leukocyte antibodies, carbohydrate inhibition assays with synthetic oligosaccharides, COS-cell PADGEM transfection adhesion assay Cell High 1699666
1991 GMP-140 (SELP) binds to a glycoprotein receptor on neutrophils via a lectin-like mechanism; binding is Ca2+-dependent, reversible, saturable (~1.5 nM half-maximal), and abolished by protease treatment or neuraminidase (alpha 2-3 and alpha 2-8 linked sialic acids). Anti-CD15 (Lex) antibody does not block binding, indicating that sialic acid-containing structures beyond simple Lex are required. Radioligand binding assay with [125I]GMP-140, enzyme treatments (protease, neuraminidase), blocking antibodies, Ca2+ chelation The Journal of cell biology High 1704009
1991 CD62/P-selectin (SELP) and ELAM-1 recognize the same carbohydrate ligand, sialyl-Lewis x (sLex), on neutrophils and monocytes; binding of CD62-expressing cells to sLex structures was demonstrated by cell adhesion assays. Cell adhesion assays using sLex-expressing cells versus control cells, antibody blocking Proceedings of the National Academy of Sciences of the United States of America High 1712483
1991 GMP-140 (SELP) recognizes alpha(2-3)sialylated, alpha(1-3)fucosylated lactosaminoglycans (sialyl Lewis x sequence) on both myeloid and non-myeloid cells; sialic acid is required (cells expressing Lex without sialyl-Lex do not bind), but HL-60 myeloid cells bind with higher affinity than CHO cells expressing sLex alone, indicating additional structural requirements beyond the minimal tetrasaccharide. Purified GMP-140 binding to cells naturally expressing specific oligosaccharides and cells transfected with glycosyltransferase cDNAs; neuraminidase treatment The Journal of cell biology High 1717488
1991 CD62/P-selectin (SELP) binds to sulfatides (3-sulfated galactosyl ceramides), which constitute the principal ligand on some tumor cell plasma membranes and are excreted by granulocytes; sulfatides adsorbed to plastic bind CD62 as avidly as myeloid or tumor cells, suggesting a role in facilitating leukocyte disengagement from CD62 at inflammatory sites. Cell adhesion assays to sulfatide-coated plastic, competition with sulfatides, granulocyte sulfatide excretion measurement Cell High 1717159
1991 LECAM-1 (L-selectin) on neutrophils presents sialyl Lewis x oligosaccharide ligands to GMP-140 (SELP) and ELAM-1 on vascular endothelium; LECAM-1 is concentrated on neutrophil microvilli and anti-LECAM-1 antibodies or removal of surface LECAM-1 inhibit neutrophil binding to GMP-140/ELAM-1 transfectants by up to 70%. Cell binding assays to selectin-transfected cells, anti-LECAM-1 antibody blocking, selective LECAM-1 removal, immunolocalization to microvilli Cell High 1716182
1991 GMP-140 (SELP) on activated endothelium tethers neutrophils without requiring CD11/CD18 integrin activation, but potentiates subsequent PAF-induced CD11/CD18-dependent firm adhesion. Coexpression of GMP-140 and PAF by histamine- or thrombin-stimulated endothelium is required for maximal PMN adhesion through a juxtacrine mechanism. Antibody blocking of GMP-140 and CD11/CD18, fluid-phase GMP-140 competition, purified GMP-140 functional assays, histamine/thrombin stimulation of endothelial cells The Journal of cell biology High 1717478
1991 Oxygen radicals (H2O2, t-butylhydroperoxide, menadione) induce prolonged surface expression of GMP-140 (SELP) on endothelial cells, promoting neutrophil adhesion; this process does not require de novo protein synthesis and is completely blocked by anti-GMP-140 antibody or soluble GMP-140. Oxidant treatment of endothelial cells, neutrophil adhesion assay, antibody blocking, protein synthesis inhibition, antioxidant treatment The Journal of cell biology High 1704376
1991 Complement C5b-9 induces surface expression of GMP-140 (SELP) on endothelial cells via Ca2+ influx across the plasma membrane; the response is blocked by removal of external calcium and partially inhibited by sphingosine (protein kinase C inhibitor); C5b-8 without C9 is insufficient. Complement activation on antibody-sensitized endothelial cells, C8-deficient serum controls, intracellular Ca2+ measurement, external Ca2+ removal, sphingosine inhibition The Journal of biological chemistry High 2470750
1991 Immobilized GMP-140 (SELP) supports neutrophil adhesion without CD18 integrin activation and inhibits superoxide anion generation and cell spreading; fluid-phase GMP-140 also inhibits TNF-alpha-induced superoxide generation in neutrophils, establishing an anti-inflammatory signaling role. Neutrophil adhesion to GMP-140-coated plastic, superoxide assay, anti-GMP-140 Fab reversal, TNF-alpha activation with fluid-phase GMP-140 Proceedings of the National Academy of Sciences of the United States of America High 1706523
1991 Soluble (fluid-phase) GMP-140 (SELP) specifically inhibits CD18-dependent adhesion of TNF-alpha-activated neutrophils to resting endothelium, but does not inhibit resting neutrophil adhesion to TNF-activated endothelium, demonstrating a selective anti-inflammatory function. Soluble GMP-140 competition assays with TNF-alpha-activated neutrophils or endothelium, CD18-blocking antibodies Science (New York, N.Y.) High 1696029
1992 A major glycoprotein ligand for P-selectin (SELP) on myeloid cells was identified at ~120 kDa (reducing conditions) or ~250 kDa (non-reducing); binding is Ca2+-dependent, protease-sensitive, requires sialic acid (neuraminidase abolishes binding), and is not L-selectin, LAMP-1, LAMP-2, or leukosialin. Blotting of neutrophil/HL-60 extracts with [125I]P-selectin, affinity chromatography with [3H]glucosamine-labeled extracts, enzyme treatments (sialidase, PNGase F), immunodepletion with antibodies to candidate proteins The Journal of cell biology High 1378449
1992 The cytoplasmic domain (last 23 amino acids of the 35-residue tail) of P-selectin (SELP) is both necessary and sufficient for sorting of the protein into regulated secretory granules; deletion of this region redirects P-selectin to the plasma membrane in AtT20 cells, and replacement of tissue factor's cytoplasmic tail with the P-selectin tail redirects tissue factor to granules. Transfection of P-selectin cDNA and deletion/chimeric constructs into COS-7, CHO-K1, and AtT20 cells; immunogold electron microscopy; cAMP stimulation; Western blot Molecular biology of the cell High 1378326
1992 Plasma contains a soluble form of GMP-140 (SELP) at ~0.25 µg/mL in men, which lacks the transmembrane domain (consistent with alternative splicing), elutes as a monomer by gel filtration, and binds the same neutrophil receptor as membrane-bound GMP-140. ELISA detection, 100,000g ultracentrifugation, plasma protein purification, analytical gel filtration, neutrophil binding assay The Journal of experimental medicine High 1372646
1992 P-selectin (SELP) binds to a subset of peripheral blood lymphocytes (CD4+, CD8+, CD16+, preferentially CD45RO+ memory cells) and can mediate adhesion of activated platelets to lymphocytes; binding is Ca2+-dependent and blocked by sialidase pretreatment. Multi-color immunofluorescence with purified P-selectin, platelet-lymphocyte adhesion assay, Ca2+ chelation, sialidase treatment Biochemical and biophysical research communications Medium 1378721
1992 GMP-140 (SELP) binds to chronically antigen-stimulated CD4+ T cells (but not freshly isolated T cells) via sialic acid-dependent, EDTA-sensitive (Ca2+-dependent) structures, and augments GM-CSF production while inhibiting IL-8 production upon co-stimulation with anti-TCR antibody. GMP-140-IgG Fc chimera binding assay, neuraminidase/trypsin treatment, EDTA inhibition, cytokine measurement by ELISA European journal of immunology Medium 1378017
1992 GMP-140 (SELP) binds to carcinoma cells (colon, lung, breast) via a ligand distinct from that on myeloid HL-60 cells; neuraminidase treatment of breast carcinoma cells does not abolish (and sometimes increases) GMP-140 binding, whereas it abolishes binding to HL-60 cells, indicating tumor cells present a different (sialic acid-independent) P-selectin ligand. Soluble GMP-140-IgG chimera immunohistology on tumor tissue sections, binding assays to carcinoma cell lines, neuraminidase treatment Proceedings of the National Academy of Sciences of the United States of America Medium 1372439
1993 Critical residues in the lectin domain of P-selectin (SELP) required for myeloid cell binding were identified: Lys113, Tyr48, and Tyr94. Single substitutions (Lys113Ala, Tyr48Ala, Tyr48Phe, Tyr94Ala, Tyr94Phe) abolish binding. These residues form a shallow groove on the molecule modeled on the rat mannose-binding protein crystal structure. Homology modeling of lectin domain on mannose-binding protein crystal structure; site-directed mutagenesis; myeloid cell binding assays with mutant P-selectin constructs Biochemistry High 7681324
1993 P-selectin activation of monocytes and neutrophils through contact with activated platelets induces superoxide anion release; this is inhibited by anti-P-selectin antibody, anti-sialyl-Lewis X antibody, or soluble recombinant P-selectin fusion protein, establishing P-selectin-mediated outside-in signaling. Superoxide anion measurement in platelet-leukocyte co-cultures, platelet membrane fraction assays, antibody and soluble receptor blocking Journal of immunology High 7690799
1994 The P-selectin (SELP) binding sites for myeloid cells and sulfatides are overlapping; Tyr48Ser or Lys113Arg substitutions create correctly folded but non-binding P-selectin mutants for both HL-60 cells and sulfatides, indicating these residues define the shared binding pocket. Extended mutagenesis panel with myeloid cell binding assays and sulfatide competition Biochemistry High 7508745
1993 Expression cloning from HL-60 cells identified PSGL-1 (P-selectin glycoprotein ligand-1) as a functional glycoprotein ligand for P-selectin (SELP); coexpression of the protein and a fucosyltransferase in COS cells is required for P-selectin binding; the ligand is expressed as a 220 kDa homodimer. Expression cloning from HL-60 cDNA library, COS-cell transfection with PSGL-1 and fucosyltransferase cDNAs, P-selectin binding assay, anti-P-selectin antibody blocking Cell High 7505206
1995 P-selectin (SELP) binds primitive hematopoietic progenitors (CD34+ cells including CFU-GM and pre-CFU); binding requires divalent cations, is protease-sensitive, and is abolished by neuraminidase. PSGL-1 mRNA is expressed by CD34+ cells, suggesting PSGL-1 as a major P-selectin ligand on hematopoietic progenitors. P-selectin binding assays on CD34+ cells, clonogenic assays, temperature independence testing, enzyme treatments, RT-PCR for PSGL-1, anti-P-selectin antibody blocking Blood Medium 7540063
1999 Platelet glycoprotein Ibalpha (part of the GP Ib-IX-V complex) is identified as a counter-receptor for P-selectin (SELP); this interaction does not require Ca2+, core-2 carbohydrate branching, or alpha(1,3)-fucosylation (unlike PSGL-1 binding) but is inhibited by sulfated proteoglycans and by antibodies to a tyrosine-sulfated region of GP Ibalpha. P-selectin-transfected cell adhesion to immobilized GP Ibalpha, GP Ibalpha-transfected cell rolling on P-selectin and histamine-stimulated endothelium, anti-P-selectin and anti-GP Ibalpha antibody blocking, Ca2+ chelation The Journal of experimental medicine High 10499919
2000 Crystal structures of P-selectin lectin-EGF domain bound to sLex and to the N-terminal domain of PSGL-1 (modified by tyrosine sulfation and sLex) reveal the molecular basis of high-affinity PSGL-1 recognition: PSGL-1 sulfated tyrosine contacts the P-selectin lectin domain at a site distinct from but adjacent to the sLex binding groove. X-ray crystallography of P-selectin LE domain co-complexed with sLex and with PSGL-1 N-terminal peptide Cell High 11081633
2000 Versican, a large chondroitin sulfate/dermatan sulfate proteoglycan, binds P-selectin (SELP) via its chondroitin sulfate (CS) chains; binding is inhibited by CS B, CS E, and heparan sulfate but not other glycosaminoglycans, and soluble P-selectin directly binds immobilized CS B and CS E. Solid-phase binding assay of P-selectin to versican, glycosaminoglycan competition, direct binding of soluble P-selectin to immobilized CS chains, cross-blocking with L-selectin The Journal of biological chemistry High 10950950
2003 P-selectin (SELP) anchors newly released ultralarge von Willebrand factor (ULVWF) strings to the endothelial cell surface; CHO cells expressing P-selectin adhere to immobilized ULVWF; anti-VWF antibody co-immunoprecipitates P-selectin from histamine-activated endothelial cells; anti-P-selectin antibody blocks ULVWF string formation; the minimal ULVWF-P-selectin bond strength is ~7.2 pN. CHO-P-selectin adhesion to immobilized ULVWF, co-immunoprecipitation from histamine-activated endothelium, antibody blocking of string formation, atomic force microscopy bond strength measurement Blood High 14630802
2003 P-selectin (SELP) interaction with PSGL-1 generates procoagulant microparticles; P-sel-Ig chimeras induce microparticle formation in human blood via PSGL-1; Psgl1-/- mice produce fewer microparticles after P-sel-Ig infusion; infused microparticles bearing tissue factor bind to thrombi and enhance fibrin formation in hemophilia A mice, normalizing tail-bleeding time. P-selectin-Ig chimera treatment of human blood, Psgl1-/- mouse experiments, flow cytometry for microparticles, infusion of procoagulant microparticles into hemophilia A mice, fibrin kinetics and tail-bleeding assay Nature medicine High 12858167
1997 CD24, a mucin-type GPI-linked glycoprotein on neutrophils and tumor cells, is a ligand for P-selectin (SELP); CD24-coated beads bind P-selectin-IgG; binding depends on divalent cations and is abolished by O-sialoglycoprotein endopeptidase but not sialidase; transfection of CD24 into adenocarcinoma cells enhances P-selectin-dependent platelet binding. CD24 purification and bead coating, P-selectin-IgG binding assay, enzyme treatments, CD24 transfection, platelet adhesion assay, phospholipase C removal Blood High 9129046
2006 Lipopolysaccharide (LPS) from EHEC O157 binds to platelets through a complex of TLR4 and CD62P (SELP), leading to platelet activation; TLR4 colocalizes with CD62P on the platelet membrane; Tlr4-deficient mice do not bind O157LPS; CD62P further contributes to LPS-triggered platelet activation on endothelial cells in perfusion experiments. Immunofluorescence co-localization of TLR4 and CD62P on platelets, Tlr4-/- mouse in vivo LPS injection, flow cytometry for platelet activation (GPIIb/IIIa, CD40L), perfusion experiments with TLR4/CD62P-blocking antibodies Blood High 16514062
2010 Rolling of human neutrophils on P-selectin (SELP) induces the extended (but not high-affinity) conformation of LFA-1 (alpha-L beta-2 integrin) through signaling dependent on PSGL-1, Src family kinase FGR, and SYK, allowing binding to immobilized extension-reporter antibodies during rolling. Human neutrophil rolling assays on P-selectin under flow, reporter antibody binding assays (KIM127, NKI-L16, mAb24), PSGL-1 blocking, kinase inhibitors, microfluidics-based reporter assay Blood High 20445017
2011 PSGL-1, CD44, and ESL-1 on mature leukocytes are physiologic glycoprotein ligands for P-selectin (SELP) on endothelial cells; PSGL-1 and CD44 induce signals that activate beta-2 integrin LFA-1 to promote slow rolling, while ESL-1 activates Mac-1 in adherent neutrophils. Review synthesizing in vivo mouse genetic data (knockout mice for each ligand), intravital microscopy rolling assays, signaling studies (integrin activation) Blood High 22021370
2016 miR-26b and miR-140 directly regulate SELP (P-selectin) mRNA levels in megakaryocytes; overexpression or inhibition of these miRNAs in MEG-01 cells modulates SELP mRNA levels; hyperglycemia in type 2 diabetes suppresses these miRNAs via calpain-mediated Dicer degradation, leading to elevated SELP mRNA and platelet P-selectin surface expression. miRNA mimic/anti-miRNA transfection in MEG-01 megakaryocytes, RT-qPCR for SELP mRNA, calpain inhibitor (calpeptin) rescue, flow cytometry for surface P-selectin Thrombosis and haemostasis Medium 27975100
2024 P-selectin/CD62P blockade after venous thrombus formation reduces monocyte and neutrophil infiltration, decreases reactive oxygen species production by neutrophils and tissue factor expression by classical monocytes, reduces thrombus density, and accelerates fibrinolysis (increased urokinase-type plasminogen activator levels) and thrombus resolution in a mouse inferior vena cava stenosis model. Mouse IVC stenosis thrombosis model, P-selectin-blocking antibody administration post-thrombus formation, intravital microscopy, flow cytometry for platelet-leukocyte aggregates, scanning electron microscopy, ROS assay, tissue factor expression, uPA measurement Arteriosclerosis, thrombosis, and vascular biology High 38385292

Source papers

Stage 0 corpus · 130 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
1999 Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nature genetics 1381 10391209
1990 Rapid neutrophil adhesion to activated endothelium mediated by GMP-140. Nature 930 1689464
1989 GMP-140, a platelet alpha-granule membrane protein, is also synthesized by vascular endothelial cells and is localized in Weibel-Palade bodies. The Journal of clinical investigation 899 2472431
1989 PADGEM protein: a receptor that mediates the interaction of activated platelets with neutrophils and monocytes. Cell 814 2478294
1985 A platelet alpha-granule membrane protein (GMP-140) is expressed on the plasma membrane after activation. The Journal of cell biology 813 2411738
1989 Cloning of GMP-140, a granule membrane protein of platelets and endothelium: sequence similarity to proteins involved in cell adhesion and inflammation. Cell 756 2466574
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
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