Shear-Dependent Capping of L-Selectin and P-Selectin Glycoprotein Ligand 1 by E-Selectin Signals Activation of High-Avidity β2-Integrin on Neutrophils

Green, Chad E.; Pearson, David; Camphausen, Raymond T.; Staunton, Donald E.; Simon, Scott I.

doi:10.4049/jimmunol.172.12.7780

Cited by 116 publications

(141 citation statements)

References 70 publications

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“…Selectins which initiate the recruitment of leukocytes from the blood stream on inflamed endothelium (21) and combined with  2 -integrin (CD11b/CD18) are required at a later stage for prolonged PMN sequestration within the pulmonary capillaries (17). In addition, cross-linking of L-selectin and P-selectin glycoprotein ligang 1 (PSGL-1) expressed on neutrophils following binding to corresponding selectin ligands can cooperatively provide an important accessory signal to trigger the activation of integrin CD11b/CD18 (22,23). Firm adhesion and transmigration is predominantly dependent on  2 -integrins on PMN interaction with their counterreceptors, believed to be predominantly ICAM-1 (8)(9)(10).…”

Section: Discussionmentioning

confidence: 99%

Inefficiency of C3H/HeN Mice to Control Chlamydial Lung Infection Correlates with Downregulation of Neutrophil Activation During the Late Stage of Infection

Tang

Zhang

et al. 2009

Cell Mol Immunol

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We previously reported that massive infiltration of neutrophils in C3H/HeN (C3H) mice could not efficiently control Chlamydia muridarum (Cm) infection and might contribute to the high susceptibility of these mice to lung infection. To further define the nature of neutrophil responses in C3H mice during chlamydial infection, we examine the expression of adhesion molecules and CD11b related to neutrophils infiltration and activation, respectively, following intranasal Cm infection. The results showed that the expression of selectins (E-selectin, P-selectin and L-selectin), and intercellular cell adhesion molecule-1 (ICAM-1) in the lung of C3H mice increased more significantly than in C57BL/6 (B6) mice, the more resistant strain. These results correlated well with the massive neutrophils infiltration in C3H mice. In contrast, CD11b expression on peripheral blood and lung neutrophils in C3H mice exhibited a significant reduction compared with B6 mice during the late phage of infection (day 14). These findings suggest that the high-level expression of adhesion molecules in C3H mice may enhance neutrophils recruitment to the lung, but the decline of CD11b expression on neutrophils may attenuate neutrophil function. Therefore, CD11b down-regulation on neutrophils may contribute to the failure of C3H mice to control chlamydial lung infection. Cellular & Molecular Immunology. 2009;6(4):253-260.

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Section: Discussionmentioning

confidence: 99%

Inefficiency of C3H/HeN Mice to Control Chlamydial Lung Infection Correlates with Downregulation of Neutrophil Activation During the Late Stage of Infection

Tang

Zhang

et al. 2009

Cell Mol Immunol

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“…These two components were critical for eliciting optimum adhesion efficiency of neutrophils on ICAM-1 expressing substrates in shear flow (27)(28)(29). To examine how ICAM-1 presentation as a monomer or dimer influences the efficiency of LFA-1-mediated adhesion of neutrophils stimulated with IL-8 or 240Q, we examined the kinetics of capture of beads coated with equivalent numbers of monomeric and dimeric ICAM-1 in sheared cell suspension.…”

Section: Resultsmentioning

confidence: 99%

Leukocyte Function-associated Antigen 1-mediated Adhesion Stability Is Dynamically Regulated through Affinity and Valency during Bond Formation with Intercellular Adhesion Molecule-1

Sarantos

Raychaudhuri

Lum

et al. 2005

Journal of Biological Chemistry

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Neutrophil rolling and transition to arrest on inflamed endothelium are dynamically regulated by the affinity of the ␤ 2 integrin CD11a/CD18 (leukocyte function associated antigen 1 (LFA-1)) for binding intercellular adhesion molecule (ICAM)-1. Conformational shifts are thought to regulate molecular affinity and adhesion stability. Also critical to adhesion efficiency is membrane redistribution of active LFA-1 into dense submicron clusters where multimeric interactions occur. We examined the influences of affinity and dimerization of LFA-1 on LFA-1/ICAM-1 binding by engineering a cell-free model in which two recombinant LFA-1 heterodimers are bound to respective Fab domains of an antibody attached to latex microspheres. Binding of monomeric and dimeric ICAM-1 to dimeric LFA-1 was measured in real time by fluorescence flow cytometry. ICAM-1 dissociation kinetics were measured while LFA-1 affinity was dynamically shifted by the addition of allosteric small molecules. High affinity LFA-1 dissociated 10-fold faster when bound to monomeric compared with dimeric ICAM-1, corresponding to bond lifetimes of 25 and 330 s, respectively. Downshifting LFA-1 into an intermediate affinity state with the small molecule I domain allosteric inhibitor IC487475 decreased the difference in dissociation rates between monomeric and dimeric ICAM-1 to 4-fold. When LFA-1 was shifted into the low affinity state by lovastatin, both monomeric and dimeric ICAM-1 dissociated in less than 1 s, and the dissociation rates were within 50% of each other. These data reveal the respective importance of LFA-1 affinity and proximity in tuning bond lifetime with ICAM-1 and demonstrate a nonlinear increase in the bond lifetime of the dimer versus the monomer at higher affinity.Neutrophils circulate in the bloodstream to sites of inflammation where they adhere and transmigrate through the endothelium as the initial step in combating infection and to facilitate wound healing. Recruitment from the circulation involves a multistep process of cell rolling, activation, and arrest. The heterodimeric integrin receptor LFA-1 1 is composed of the ␣L (CD11a) and ␤ 2 (CD18) subunits and is constitutively expressed in a low affinity conformation on the plasma membrane of leukocytes (1-3). Neutrophils encountering chemokines on inflamed endothelium are activated to shift LFA-1 from the low to high affinity conformation, which supports tight binding to endothelial ICAM-1. Increases in integrin affinity correlate in time with adhesion function as recently demonstrated in aggregation of cells expressing ␣4␤1 and vascular cell adhesion molecule (4). ICAM-1 recognizes LFA-1 through an inserted (I) domain in the ␣ subunit. There is strong evidence correlating shifts in I domain conformation to affinity changes in binding ICAM-1. Mutations in I domain residues stabilized distinct structural conformations correlating to LFA-1 affinity. ICAM-1 equilibrium binding constants increase over 4 orders of magnitude ranging between low (i.e. 1600 M), intermediate (i.e. 9 M), and high...

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“…A hallmark of selectin-dependent arrest is the redistribution of surface PSGL-1 into large, high-density clusters [48]. Despite the lack of a clear role in selectindependent neutrophil activation and arrest, it is possible that SNX20 has a role in this surface redistribution.…”

Section: Phospholipid Binding Is Required For Slic-1 Localization To mentioning

confidence: 99%

SLIC‐1/sorting nexin 20: A novel sorting nexin that directs subcellular distribution of PSGL‐1

Schaff¹,

Shih²,

Lorenz³

et al. 2008

Eur J Immunol

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P-Selectin glycoprotein ligand-1 (PSGL-1) is a mucin-like glycoprotein expressed on the surface of leukocytes that serves as the major ligand for the selectin family of adhesion molecules and functions in leukocyte tethering and rolling on activated endothelium and platelets. Previous studies have implicated the highly conserved cytoplasmic domain of PSGL-1 in regulating outside-in signaling of integrin activation. However, molecules that physically and functionally interact with this domain are not completely defined. Using a yeast two-hybrid screen with the cytoplasmic domain of PSGL-1 as bait, a novel protein designated selectin ligand interactor cytoplasmic-1 (SLIC-1) was isolated. Computer-based homology search revealed that SLIC-1 was the human orthologue for the previously identified mouse sorting nexin 20. Direct interaction between SLIC-1 and PSGL-1 was specific as indicated by co-immunoprecipitation and motif mapping. Colocalization experiments demonstrated that SLIC-1 contains a Phox homology domain that binds phosphoinositides and targets the PSGL-1/SLIC-1 complex to endosomes. Deficiency in the murine homologue of SLIC-1 did not modulate PSGL-1-dependent signaling nor alter neutrophil adhesion through PSGL-1. We conclude that SLIC-1 serves as a sorting molecule that cycles PSGL-1 into endosomes with no impact on leukocyte recruitment.Supporting Information for this article is available at http://www.wiley-vch.de/contents/jc_2040/2008/37777_s.pdf IntroductionThe initial tethering and rolling of leukocytes on activated endothelium and platelets is a key biological event mediated by P-selectin glycoprotein ligand-1 (PSGL-1), a mucin-like glycoprotein that functions as a unique high-affinity ligand for the selectin family of adhesion molecules (for reviews, see [1][2][3][4]). Structurally, PSGL-1 is a type I integral membrane protein consisting of an N-terminal selectin-binding domain followed by a region of multiple decameric repeats bearing O-linked glycans, a short transmembrane domain, and lastly a cytoplasmic tail [5][6][7][8][9][10]. Comparison of human and murine PSGL-1 reveals that the 69-amino acid intracellular domain of PSGL-1 is highly conserved. While overall identity between human and Abbreviations: EEA-1: early endosomal antigen-1 Á EGFP: enhanced green fluorescent protein Á ERM: ezrin/radixin/ moesin Á L-E/I: L cell monolayer expressing E-selectin and ICAM-1 Á PI: phosphatidylinositol Á PI 3-kinase: phosphatidylinositol 3-kinase Á PSGL-1: P-selectin glycoprotein ligand-1 Á PtdIns(3)P: phosphatidylinositol 3-phosphate Á PtdIns(3,4)P 2 : phosphatidylinositol 3,4-bisphosphate Á PtdIns(3,4,5)P 3 : phosphatidylinositol 3,4,5-trisphosphate Á PX domain: phox homology domain Á SLIC-1: selectin ligand interactor cytoplasmic-1 Á SNX20: sorting nexin 20 Á TM: transmembrane Ulrich Y. Schaff et al.

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Shear-Dependent Capping of L-Selectin and P-Selectin Glycoprotein Ligand 1 by E-Selectin Signals Activation of High-Avidity β2-Integrin on Neutrophils

Cited by 116 publications

References 70 publications

Inefficiency of C3H/HeN Mice to Control Chlamydial Lung Infection Correlates with Downregulation of Neutrophil Activation During the Late Stage of Infection

Inefficiency of C3H/HeN Mice to Control Chlamydial Lung Infection Correlates with Downregulation of Neutrophil Activation During the Late Stage of Infection

Leukocyte Function-associated Antigen 1-mediated Adhesion Stability Is Dynamically Regulated through Affinity and Valency during Bond Formation with Intercellular Adhesion Molecule-1

SLIC‐1/sorting nexin 20: A novel sorting nexin that directs subcellular distribution of PSGL‐1

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