CD11b/CD18-coated microspheres attach to E-selectin under flow

Crutchfield, K L; Patil, Vivek R. Shinde; Campbell, Craig J.; Parkos, Charles A.; Allport, Jennifer R.; Goetz, Douglas J.

doi:10.1002/jlb.67.2.196

Cited by 37 publications

(33 citation statements)

References 57 publications

(108 reference statements)

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“…[34][35][36] However, mouse L-selectin has been shown not to bind mouse E-selectin, making this an unlikely ligand in our study. 35 E-selectin ligand-1 (ESL-1), 37,38 CD66-nonspecific cross-reacting antigen, 39 CD43, 40 and ␤ 2 integrin 41,42 have all been proposed as potential ligands on leukocytes for E-selectin, although CD43 does not appear to support rolling and to our knowledge ␤ 2 integrin and CD66 are not down-regulated. Recently, a family of glycolipids, namely ␣2,3-sLe x glycosphingolipids, have also been shown to support E-selectin-dependent rolling.…”

Section: Discussionmentioning

confidence: 88%

A down-regulatable E-selectin ligand is functionally important for PSGL-1–independent leukocyte–endothelial cell interactions

Zanardo

Bonder

Hwang

et al. 2004

Blood

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P-selectin glycoprotein-1 (PSGL-1) supports P-selectin-dependent rolling in vivo and in vitro. However, controversy exists regarding the importance of PSGL-1-dependent and -independent E-selectin rolling. Using antibodies against PSGL-1 and PSGL-1 ؊/؊ mice, we demonstrated abolition of P-selectin-dependent rolling but only partial inhibition of E-selectinmediated rolling in the cremaster microcirculation following local administration of tumor necrosis factor ␣ (TNF-␣). In vitro studies demonstrated that binding of recombinant mouse E-selectin chimera to PSGL-1 ؊/؊ neutrophils was dramatically decreased in mice treated systemically but not locally with TNF-␣. Further, PSGL-1 blockade abolished E-selectindependent rolling in wild-type mice following systemic TNF-␣ administration but not local TNF-␣ administration. Together, these data support an E-selectin ligand present on PSGL-1 ؊/؊ neutrophils that is down-regulatable upon systemic but not local activation. To determine whether the PSGL-1-independent E-selectin ligand was physiologically important, we used a P-and E-selectin-dependent cutaneous contact hypersensitivity model. Binding studies showed no E-selectin ligand down-regulation in this model. The few cells that rolled on E-selectin ligand following PSGL-1 antibody administration or in PSGL-1 deficiency were sufficient to induce profound contact hypersensitivity. In conclusion, E-selectin mediates PSGL-1-dependent and independent rolling and the latter can be down-regulated by systemic activation and can replace PSGL-1 to support the development of

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Section: Discussionmentioning

confidence: 88%

A down-regulatable E-selectin ligand is functionally important for PSGL-1–independent leukocyte–endothelial cell interactions

Zanardo

Bonder

Hwang

et al. 2004

Blood

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“…This presents the question of why PSGL-1 should be the only molecule capable of supporting residual leukocyte rolling on P-selectin when many other sialylated/fucosylated molecules (eg, L-selectin, 32 ESL-1, 33 CD24, 34 and CD18 35,36 ) exist on the surface of leukocytes and are capable of interacting with the selectins. Explaining PSGL-1-independent, P-selectin-dependent leukocyte rolling is not straightforward, given the absence of surgically induced rolling in PSGL-1-deficient mice, 16 but we believe that our findings with PSGL-1 antibody pretreatment and recent data from others 26 offer a plausible solution.…”

Section: Discussionmentioning

confidence: 99%

L- and P-Selectins Collaborate to Support Leukocyte Rolling in Vivo When High-Affinity P-Selectin-P-Selectin Glycoprotein Ligand-1 Interaction Is Inhibited

Ridger¹,

Hellewell²,

Norman³

2005

The American Journal of Pathology

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P-selectin glycoprotein ligand-1 (PSGL-1) binding to Pselectin controls early leukocyte rolling during inflammation. Interestingly, antibodies and pharmacological inhibitors (eg, rPSGL-Ig) that target the N-terminus of PSGL-1 reduce but do not abolish P-selectin-dependent leukocyte rolling in vivo whereas PSGL-1-deficient mice have almost no P-selectin-dependent rolling. We have investigated mechanisms of P-selectin-dependent, PSGL-1-independent rolling using intravital microscopy. Initially we used fluorescent microspheres to study the potential of L-selectin and the minimal selectin ligand sialyl Lewis x (sLe x ) to interact with postcapillary venules in the absence of PSGL-1. Microspheres coated with combinations of L-selectin and sLe x interacted with surgically stimulated cremaster venules in a P-selectin-dependent manner. Microspheres coated with either L-selectin or sLe x alone showed less evidence of interaction. We also investigated leukocyte rolling in the presence of PSGL-1 antibody or inhibitor (rPSGL-Ig), both of which partially inhibited P-selectin-dependent leukocyte rolling. Residual rolling was substantially inhibited by L-selectin-blocking antibody or a previously described sLe x mimetic (CGP69669A). Together these data suggest that leukocytes can continue to roll in the absence of optimal P-selectin/PSGL-1 interaction using an alternative mechanism that involves P-selectin-, L-selectin-, and sLe and present attractive targets for anti-inflammatory drugs. P-Selectin may be a good target for cardiovascular disease therapy, 2-5 although notable clinical trial disappointments 6,7 suggest that effective P-selectin inhibition may be more challenging than expected.Natural ligand mimicry is a common drug development approach. Elements of PSGL-1 required for high-affinity P-selectin recognition include a sialylated, fucosylated O-glycan and tyrosine sulfation at appropriate positions near the N-terminus. 8 Drugs mimicking one or more of these elements could theoretically inhibit P-selectin. Inhibitors based on the carbohydrate selectin ligand, sLe x , are effective, albeit in high doses, against E-selectindependent leukocyte rolling in vivo but have no measurable effect on established P-selectin-dependent rolling.

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“…43,[92][93][94] Furthermore, human neutrophils may use L-selectin and glycolipids to mediate E-selectin binding 95,96 (Table 1). In vitro, E-selectin binds to human CD66/ carcinoembryonic antigen, 97 integrin Mac-1, 98 podocalyxin-like protein, or melanoma cell adhesion molecule, 99 which may be relevant in specific cellular contexts. Thus, the identification of the full repertoire of ligands for E-selectin is still a matter of debate and active research.…”

Section: Additional Ligands For E-selectinmentioning

confidence: 99%

Leukocyte ligands for endothelial selectins: specialized glycoconjugates that mediate rolling and signaling under flow

Zarbock

Ley

McEver

et al. 2011

Blood

419

393

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Reversible interactions of glycoconjugates on leukocytes with P-and E-selectin on endothelial cells mediate tethering and rolling of leukocytes in inflamed vascular beds, the first step in their recruitment to sites of injury. Although selectin ligands on hematopoietic precursors have been identified, here we review evidence that PSGL-1, CD44, and ESL-1 on mature leukocytes are physiologic glycoprotein ligands for endothelial selectins. Each ligand has specialized adhesive functions during tethering and rolling. Furthermore, PSGL-1 and CD44 induce signals that activate the ␤2 integrin LFA-1 and promote slow rolling, whereas ESL-1 induces signals that activate the ␤2 integrin Mac-1 in adherent neutrophils. We also review evidence for glycolipids, CD43, L-selectin, and other glycoconjugates as potential physiologic ligands for endothelial selectins on neutrophils or lymphocytes. Although the physiologic characterization of these ligands has been obtained in mice, we also note reported similarities and differences with human selectin ligands. (Blood. 2011;118(26):6743-6751) IntroductionThe selectins mediate adhesion of hematopoietic cells to vascular surfaces and to each other. 1 These interactions are important for host defense, hematopoiesis, immune cell surveillance, hemostasis, and inflammation. Each of the 3 selectins is a type I transmembrane protein with an N-terminal C-type lectin domain, an epidermal growth factor-like domain, a series of consensus repeats, a transmembrane domain, and a short cytoplasmic tail. L-selectin is constitutively expressed on most leukocytes. P-selectin is rapidly mobilized from secretory granules to the plasma membranes of platelets and endothelial cells on stimulation. E-selectin expression on endothelial cells is regulated at the transcriptional level by inflammatory mediators, such as tumor necrosis factor-␣.The rolling cell adhesion mediated by selectins is a dynamic process that requires rapid formation and breakage of bonds under flow. 2 Rolling enables cells to receive signals that activate integrins, another class of adhesion receptors, which cause the cells to roll slower and to arrest. 3 Here we discuss how leukocytes, particularly neutrophils, interact with endothelial selectins during inflammation. We review evidence that surprisingly few neutrophil glycoproteins are physiologic selectin ligands, defined by their ability to mediate rolling adhesion. Rolling can be studied with flow chambers in vitro or ex vivo and in transparent tissues or by epifluorescence in vivo.The selectins are Ca 2ϩ -dependent lectins. The minimal glycan determinant for selectin binding is sialyl Lewis x (sLe x ; NeuAc␣2,3Gal␤1,4[Fuc␣1,3]GlcNAc␤1-R). 1 The fucose moiety of sLe x expressed on selectin ligands forms critical interactions with the Ca 2ϩ -coordination site on the lectin domain of selectins. 2 Leukocytes from mice lacking the 2 ␣1,3-fucosyltransferases that add fucose to form sLe x on hematopoietic cells cannot roll on Pand E-selectin. 4 Because sLe x can potentially cap N-and O-gl...

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CD11b/CD18-coated microspheres attach to E-selectin under flow

Cited by 37 publications

References 57 publications

A down-regulatable E-selectin ligand is functionally important for PSGL-1–independent leukocyte–endothelial cell interactions

A down-regulatable E-selectin ligand is functionally important for PSGL-1–independent leukocyte–endothelial cell interactions

L- and P-Selectins Collaborate to Support Leukocyte Rolling in Vivo When High-Affinity P-Selectin-P-Selectin Glycoprotein Ligand-1 Interaction Is Inhibited

Leukocyte ligands for endothelial selectins: specialized glycoconjugates that mediate rolling and signaling under flow

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