Recognition of consensus CHO structure in ligands for selectins by novel antibody against sialyl Lewis X

Tamatani, Takuya; Suematsu, Makoto; Tezuka, Katsunari; Hanzawa, N.; Tsuji, Takashi; Ishimura, Yuzuru; Kannagi, Reiji; Toyoshima, Satoshi; Homma, M.

doi:10.1152/ajpheart.1995.269.4.h1282

Cited by 18 publications

(16 citation statements)

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“…These data indicate that the sLe x -related HECA452 epitope is different from the CSLEX-1 epitope but similar to the sLe x -related epitopes defined by 2F3 and 2H5. These data agree with published evidence that the CSLEX-1 epitope is absent in the mouse (30,33) and that the mAb 2H5 recognizes its epitope on mouse neutrophils (33).…”

Section: Antigen-specific Activation Of the T Cell Clone 4g3 Induces supporting

confidence: 92%

The Binding of T Cell-expressed P-selectin Glycoprotein Ligand-1 to E- and P-selectin Is Differentially Regulated

Borges

Pendl

Eytner

et al. 1997

Journal of Biological Chemistry

101

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The HECA452 carbohydrate epitope, also termed cutaneous lymphocyte antigen, is known to bind to E-selectin and defines a human T cell subset preferentially found in inflamed skin. Activated T cells can express a functional form of the P-selectin glycoprotein ligand-1 (PSGL-1), the major ligand known for P-selectin. Here we show that PSGL-1 can exist in two forms, of which only one carries the HECA452 epitope and binds to Eselectin, while the other only binds to P-selectin. We have analyzed the glycoprotein ligands for E-and Pselectin on the mouse CD8 ؉ T cell clone 4G3 at 4, 8, and 12 days after antigen-specific activation. Only at day 4 did the cells bind to E-selectin, whereas cells at all three activation stages bound to P-selectin. Expression of the HECA452 epitope correlated with E-selectin binding. In affinity isolation experiments, PSGL-1 was isolated as the major ligand by E-selectin-IgG and by P-selectinIgG; however, PSGL-1 only bound to E-selectin at day 4, whereas it bound to P-selectin at all three activation stages. Immunoprecipitated PSGL-1 from cells at day 4, but not from cells at days 8 and 12, was recognized in immunoblots by monoclonal antibody HECA452. In immunoblots of total extracts of cells at day 4, HECA452 recognized a 240/140-kDa pair of protein bands as the major antigen. These bands could be completely removed by depletion of cell extracts with anti-PSGL-1 antibodies. Our data suggest that the carbohydrate requirements for binding of PSGL-1 to P-selectin differ from those necessary for binding to E-selectin. Furthermore, we conclude that the major glycoprotein carrier for the HECA452 epitope on activated 4G3 cells is PSGL-1.

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Section: Antigen-specific Activation Of the T Cell Clone 4g3 Induces supporting

confidence: 92%

The Binding of T Cell-expressed P-selectin Glycoprotein Ligand-1 to E- and P-selectin Is Differentially Regulated

Borges

Pendl

Eytner

et al. 1997

Journal of Biological Chemistry

101

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“…18 The MoAbs were WT-3 (anti-rat CD18), WT-5 (anti-rat CD11b), and HRL-3 (anti-rat L-selectin), generous gifts from Prof Masayuki Miyasaka, Osaka University School of Medicine, 18 and 2H5 (anti-sialyl Lewis X-like carbohydrate structure [SLeX]). 29 Separately, secretagogue activation of mast cells by H 2 O 2 was examined by measuring the release of the enzyme ␤-hexosaminidase (␤-hex), as described in the previous method, 30,31 with modifications. The density of degranulated and undegranulated mast cells in the mesenteric tissue was also studied using the toluidine blue staining method as described previously.…”

Section: Methodsmentioning

confidence: 99%

Induction of Heme Oxygenase-1 Suppresses Venular Leukocyte Adhesion Elicited by Oxidative Stress

Hayashi

Takamiya

Yamaguchi

et al. 1999

Circulation Research

346

241

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Abstract-This study aimed to examine whether an elevated activity of heme oxygenase (HO)-1 in the tissue attenuates endothelial cell-leukocyte interactions microvessels in vivo. When rats were pretreated with an intraperitoneal injection of hemin, an HO-1 inducer, mesenteric tissues, including their microvessels, displayed a marked induction of HO-1 concurrent with an increase in plasma concentrations of bilirubin-IX␣, the product of HO-catalyzed degradation of protoheme IX. In these rats, oxidative stress such as superfusion with H 2 O 2 and ischemia-reperfusion of the tissues neither induced rolling nor exhibited adherent responses of leukocytes in venules. In contrast, the oxidative stresses evoked marked rolling and adhesion of leukocytes in the control rats without HO-1 induction. The HO-1 induction also downregulated leukocyte adhesion elicited by other pro-oxidant stimuli such as N -nitro-L-arginine methyl ester. The decreases in the oxidant-elicited leukocyte adhesive responses under HO-1-inducing conditions were restored by perfusion with zinc protoporphyrin-IX, an HO inhibitor, but not with copper protoporphyrin-IX, which did not inhibit the enzyme. Furthermore, the effects of zinc protoporphyrin-IX were repressed by superfusion with bilirubin or biliverdin at the micromolar level, but not by the same concentration of carbon monoxide, another product of HO. These results indicate that induction of the HO-1 activity serves as a potential stratagem to prevent oxidant-induced microvascular leukocyte adhesion through the action of bilirubin, a product of HO reaction. (Circ Res. 1999;85:663-671.)

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“…Leukocyte Adhesion Deficiency Type II (LAD II) 1 is a recently described syndrome in which the neutrophils of two unrelated patients do not express sialyl Lewis X (sLe X ) (1,2), the fucose-containing carbohydrate reported to be the ligand for adhesion molecules of the selectin family (3,4). Neutrophils from both patients fail to bind to E-selectin on IL-1 ␤ -activated endothelial cells (1).…”

Section: Introductionmentioning

confidence: 99%

Leukocyte Adhesion Deficiency Type II is a generalized defect of de novo GDP-fucose biosynthesis. Endothelial cell fucosylation is not required for neutrophil rolling on human nonlymphoid endothelium.

Karsan¹,

Cornejo²,

Winn³

et al. 1998

J. Clin. Invest.

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Leukocyte Adhesion Deficiency Type II (LAD II) is a recently described syndrome and the two patients with this defect lack fucosylated glycoconjugates. These glycoconjugates include the selectin ligand, sialyl Lewis X , and various fucosylated blood group antigens. To date, the molecular anomaly in these patients has not been identified. We localized the defect in LAD II to the de novo pathway of GDPfucose biosynthesis, by inducing cell-surface expression of fucosylated glycoconjugates after exposure of lymphoblastoid cell lines from the LAD II patients to exogenous fucose. This defect is not restricted to hematopoietic cells, since similar findings were elicited in both human umbilical vein endothelial cells (HUVEC) and fibroblasts derived from an affected abortus. We have used these LAD II endothelial cells to examine the consequence of fucosylation of endothelial cells on the rolling of normal neutrophils in an in vitro assay. Neutrophil rolling on LPS-treated normal and LAD II HUVEC was inhibited by an E-selectin monoclonal antibody at both high and low shear rates. LAD II HUVEC lacking fucosylated glycoproteins supported leukocyte rolling to a similar degree as normal HUVEC or LAD II cells that were fucose-fed. At low shear rates, an L-selectin antibody inhibited neutrophil rolling to a similar degree whether the LAD II cells had been fucose-fed or not. These findings suggest that fucosylation of nonlymphoid endothelial cells does not play a major role in neutrophil rolling and that fucose is not a critical moiety on the L-selectin ligand(s) on endothelial cells of the systemic vasculature. ( J. Clin. Invest.

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Recognition of consensus CHO structure in ligands for selectins by novel antibody against sialyl Lewis X

Cited by 18 publications

References 0 publications

The Binding of T Cell-expressed P-selectin Glycoprotein Ligand-1 to E- and P-selectin Is Differentially Regulated

The Binding of T Cell-expressed P-selectin Glycoprotein Ligand-1 to E- and P-selectin Is Differentially Regulated

Induction of Heme Oxygenase-1 Suppresses Venular Leukocyte Adhesion Elicited by Oxidative Stress

Leukocyte Adhesion Deficiency Type II is a generalized defect of de novo GDP-fucose biosynthesis. Endothelial cell fucosylation is not required for neutrophil rolling on human nonlymphoid endothelium.

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