The neutrophil selectin LECAM-1 presents carbohydrate ligands to the vascular selectins ELAM-1 and GMP-140

Picker, Louis J.; Warnock, R A; Burns, Alan R.; Doerschuk, Claire M.; Berg, Ellen L.; Butchert, Eugene C.

doi:10.1016/0092-8674(91)90438-5

Cited by 551 publications

(344 citation statements)

References 51 publications

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“…3A). Little or no L-selectin was detected on the rest of the plasmalemma of ␥␦ T cells, concurrent with the data previously reported for human leukocytes [20,21]. In contrast, WC1, a ␥␦ T cell subset marker, localized on the plasmalemma covering the ␥␦ T cell body but was absent on microvilli (Fig.…”

Section: Introductionsupporting

confidence: 79%

“…We also examined the expression of L-selectin on bovine lymphocytes to determine whether, as shown with human leukocytes [20,21], L-selectin is localized to the tips of microvilli. Lymphocytes were isolated as above, stained with DREG 56 (␣-L-selectin) or IL-A29 (␣-WC1) on ice, and visualized with goat anti-mouse IgG1 conjugated to 10 nM colloidal gold particles.…”

Section: Introductionmentioning

confidence: 99%

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Comparative ultrastructure and expression of L-selectin on bovine αβ and γδ T cells

Leid

Speer

Jutila

1998

Journal of Leukocyte Biology

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Compared to most ␣␤ T cells, bovine ␥␦ T cells express two to five times the level of L-selectin and have a much higher capacity to roll on monolayers of endothelial cells, platelets, and leukocytes in assays done under physiological flow. To gain additional insight into the basis for these differences, scanning (SEM) and transmission (TEM) electron microscopy were used to compare the cellular ultrastructure of bovine ␥␦ and ␣␤ T cells and to study the expression of L-selectin on these cells. It is interesting that ␥␦ T cells had more than twice as many microvilli and other surface projections on a per cell basis as ␣␤ T cells. This was not due to the ␥␦ T cell being larger; after adhesion and fixation procedures used for the EM studies, ␥␦ T cells averaged 3.9 ؎ 0.01 m in diameter, whereas ␣␤ T cells were slightly larger (5.7 ؎ 0.01 m in diameter). As previously shown for human neutrophils and lymphocytes, L-selectin was preferentially localized to the tips of the microvilli. In contrast, WC1, a lineage-specific antigen on ␥␦ T cells, was localized on the plasmalemma between the microvilli. Our findings suggest that more effective rolling of ␥␦ T cells in various in vitro flow assays may be due to the greater number of microvilli on ␥␦ T cells leading to a higher number of contact sites during adhesion events. In addition, this physical parameter may explain the increased level of Lselectin expression on ␥␦ versus ␣␤ T cells because L-selectin is clustered at the tips of microvilli. J. Leukoc. Biol. 64: 104-107; 1998.

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Section: Introductionsupporting

confidence: 79%

Section: Introductionmentioning

confidence: 99%

Comparative ultrastructure and expression of L-selectin on bovine αβ and γδ T cells

Leid

Speer

Jutila

1998

Journal of Leukocyte Biology

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“…The process involves sequential action of P-selectin (CD62P, GMP-140 or PADGEM) and  2 -integrins (CD18) [11]. P-selectin interacts with a sialylated carbohydrate backbone by the leukocyte glycoproteins P-selectin glycoprotein ligand-1 (PSGL-1 or CD162) [12] and possibly L-selectin (CD62L) [13]. The selectin mediated tethering and rolling mechanisms of neutrophils and platelets are highly shear dependent.…”

Section: Introductionmentioning

confidence: 99%

Platelets stimulated by IgG-coated surfaces bind and activate neutrophils through a selectin-dependent pathway

2003

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Blood platelets bind rapidly to foreign surfaces and interact with adsorbed proteins and neutrophil granulocytes. We demonstrate by use of luminol-amplified chemiluminescence under stirred and nonstirred conditions that platelets at IgG-coated surfaces amplify the neutrophil extracellular release of reactive oxygen species (ROS). The neutrophil response involved tyrosine phosphorylation, but was only in part induced by neutrophil F c -receptor stimulation. The platelet mediated effects were contact-dependent since the respiratory burst was inhibited when the IgG-stimulated platelets were removed by filtration, but not when they were fixed in paraformaldehyde. Bodipyphallacidin-staining of filamentous actin (F-actin) revealed that an actin-dependent platelet adhesion supported the subsequent adhesion and spreading of neutrophils. The neutrophil ROS-response was lowered when the interaction between platelet P-selectin (CD62P) and neutrophil P-selectin glycoprotein ligand-l (PSGL-1 or CD162) was inhibited. The blocking of L-selectin (CD62L) or blocking of the interaction between platelet glycoprotein (Gp) IIb/IIIa and neutrophil complement receptor 3 (CR3) showed no effect. We conclude that platelet activation on immobilized IgG trigger a contact-dependent "frustrated" phagocytosis by neutrophils, associated with a release of toxic ROS. IgG-stimulated platelets activate neutrophils -Wetterö et al.3

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“…Furthermore, it has been reported that neutrophil L-selectin is almost completely shed by fMLP stimulation [38], whereas E-selectin and P-selectin are up-regulated on EC by TNF-␣ [2] or thrombin stimulation [39]. In addition, neutrophil L-selectin has been shown to directly bind to E-and P-selectin molecules [5,40,41]. This study has demonstrated that AIF inhibits adherence of resting neutrophils to thrombin-and TNF-␣-stimulated EC, and the inhibitory action of AIF is more effective under the rotating condition than the static condition ( Fig.…”

Section: Discussionmentioning

confidence: 99%

“…For example, the selectin family of adhesion molecules such as L-selectin mediates the initial adherence of neutrophils to EC, which allows neutrophils to roll along the vessel wall [4]. Furthermore, L-selectin and nonspecific cross-reacting antigens (NCAs) have been shown to mediate neutrophil adherence to EC through the binding to E-selectin [5,6]. After activation by a chemoattractant such as interleukin-8, neutrophils undergo immediate changes, including shedding of L-selectin from cell surfaces [7] and upregulation and/or conformational changes of ␤ 2 -integrins (CD11/ CD18) and NCAs [8,9].…”

Section: Introductionmentioning

confidence: 99%

Modulation of neutrophil adherence to endothelial cells by platelet-derived adherence-inhibiting factor through interactions with selectin molecules

Iwabuchi

Nagaoka

Yamashita

1998

Journal of Leukocyte Biology

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Platelet-derived adherence-inhibiting factor (AIF) has been demonstrated to regulate the neutrophil binding to type IV collagen. In this study, we have examined the effect of AIF on neutrophil adherence to confluently cultured human umbilical vein endothelial cells (EC). AIF inhibited neutrophil adherence to thrombin-or tumor necrosis factor ␣ (TNF-␣)-stimulated EC by 75 or 43%, respectively, but hardly affected neutrophil adherence to resting EC. It is interesting to note that the inhibitory activity of AIF was reduced by N-formyl-methionyl-leucyl-phenylalanine (fMLP) stimulation of neutrophils. Pretreatment of neutrophils or EC with AIF inhibited neutrophil adherence to thrombin-or TNF-␣-stimulated EC, suggesting that neutrophils and EC have AIF-binding proteins. Using AIF-Sepharose affinity chromatography, AIF-binding proteins containing L-selectin were isolated from 125 I-labeled resting neutrophils. However, L-selectin was markedly decreased in the AIF-binding fraction from fMLP-stimulated neutrophils. With the use of AIF-affinity chromatography, P-and E-selectins were obtained in the AIF-binding fractions from resting, thrombin-, and TNF-␣-stimulated EC. It is important to note that P-and E-selectin were greatly increased in the AIFbinding fractions from thrombin-and TNF-␣-stimulated EC, respectively. Furthermore, AIF was able to bind to L-selectin-IgG chimeric protein and inhibit the binding of chimeric protein to thrombinor TNF-␣-stimulated EC. In addition, AIF inhibited the binding of anti-P-or anti-E-selectin monoclonal antibody to the lysates of thrombin-or TNF-␣-stimulated EC. Together these observations indicate that AIF could recognize L-, P-, and Eselectins, and modulate neutrophil adherence to EC through interactions with selectin molecules. J.

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The neutrophil selectin LECAM-1 presents carbohydrate ligands to the vascular selectins ELAM-1 and GMP-140

Cited by 551 publications

References 51 publications

Comparative ultrastructure and expression of L-selectin on bovine αβ and γδ T cells

Comparative ultrastructure and expression of L-selectin on bovine αβ and γδ T cells

Platelets stimulated by IgG-coated surfaces bind and activate neutrophils through a selectin-dependent pathway

Modulation of neutrophil adherence to endothelial cells by platelet-derived adherence-inhibiting factor through interactions with selectin molecules

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