Characterization of human platelet GMP-140 as a heparin-binding protein

Skinner, Michael P.; Fournier, Dominique; Andrews, Robert K.; Gorman, Jeffrey J.; Chesterman, Colin N.; Berndt, Michael C.

doi:10.1016/0006-291x(89)91821-4

Cited by 74 publications

(36 citation statements)

References 16 publications

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“…Along this line of experimental observations, the sulfate-containing molecules, such as heparin and sulfatides, were reported to directly react with P-selectin. Furthermore, heparin and sulfatides were shown to potently inhibit adhesion of leukocytes and cancer cells to P-selectin (35)(36)(37)(38)(39). According to these findings, we propose that the sulfated moieties may function as the key determinant for P-selectin recognition, especially for somatic cancer cells, such as Acc-M cells and ZR-75-30 cells.…”

Section: Discussionmentioning

confidence: 84%

“…Because SLe x and its derivatives (1-5) as well as heparan sulfatelike proteoglycans (22,(35)(36)(37)(38)(39) were previously reported to mediate the binding of P-selectin to leukocytes and certain cancer cells, we examined the carbohydrate structures expressed on Acc-M cells using carbohydrate-specific mAbs. Fig.…”

Section: Cell Surface Expression Of Heparan Sulfate-like Proteoglycansmentioning

confidence: 99%

“…In literature, heparin and its analog, heparan sulfate, have been shown to bind to P-selectin, to inhibit leukocyte adhesion mediated by P-selectin, and to directly mediate adhesion of certain nonblood-borne, epithelial-like cancer cells to P-selectin (22,(35)(36)(37)(38)(39). Given the expression of heparan sulfate-like proteoglycans on the cell surface of Acc-M cells (Fig.…”

Section: Assessment Of Functional Activity For Heparan Sulfate-like Pmentioning

confidence: 99%

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Obligatory Requirement of Sulfation for P-Selectin Binding to Human Salivary Gland Carcinoma Acc-M Cells and Breast Carcinoma ZR-75-30 Cells

Qing

Geng

2002

The Journal of Immunology

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Stimulated endothelial cells and activated platelets express P-selectin, which reacts with P-selectin glycoprotein ligand-1 (PSGL-1) for leukocyte rolling on the stimulated endothelial cells and heterotypic aggregation of the activated platelets on leukocytes. P-selectin also binds to several cancer cells in vitro and promotes the growth and metastasis of human colon carcinoma in vivo. The P-selectin/PSGL-1 interaction requires tyrosine sulfation. However, it is unknown whether sulfation is necessary for P-selectin binding to somatic cancer cells. In this study, we show that P-selectin mediated adhesion of Acc-M cells, a cell line derived from a human adenoid cystic carcinoma of salivary gland. These cells had a moderate expression of heparan sulfate-like proteoglycans, but had no detectable expressions of PSGL-1, CD24, Lewisx, and sialyl Lewisx. Treatment with sodium chlorate (a sulfation biosynthesis inhibitor), but not 4-methylumbelliferyl-β-d-xyloside (a proteoglycan biosynthesis inhibitor) or heparinases, reduced adhesion of these cells to P-selectin. Sodium chlorate also inhibited the P-selectin precipitation of the ∼160-, ∼54-, and ∼36-kDa molecules from the cell surface of Acc-M cells. Furthermore, P-selectin could bind to human breast carcinoma ZR-75-30 cells in a sulfation-dependent manner. Our results thus indicate that sulfation is essential for adhesion of nonblood-borne, epithelial-like human cancer cells to P-selectin.

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Section: Discussionmentioning

confidence: 84%

Section: Cell Surface Expression Of Heparan Sulfate-like Proteoglycansmentioning

confidence: 99%

Section: Assessment Of Functional Activity For Heparan Sulfate-like Pmentioning

confidence: 99%

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Obligatory Requirement of Sulfation for P-Selectin Binding to Human Salivary Gland Carcinoma Acc-M Cells and Breast Carcinoma ZR-75-30 Cells

Qing

Geng

2002

The Journal of Immunology

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“…Numerous polyanions like sulfatides, [33] heparin, [34] lipopolysaccharides (LPS), [35] fucoidin, sulfated dextran, [36] chondroitin sulfate, [37] dermatan sulfate, [38] and sulfated hyaluronic acid [39] have been reported to exhibit P-selectin antagonism. The broad range of charged compounds lacking the carbohydrate epitope suggests tions on the design of P-selectin antagonists.…”

Section: Polyanionsmentioning

confidence: 99%

E- and P-Selectin: Differences, Similarities and Implications for the Design of P-Selectin Antagonists

Binder

Ernst²

2011

Chimia

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Selectins form a family of Ca 2+ -dependent carbohydrate binding proteins that mediate the initial step of leukocyte recruitment in the inflammatory process. Blocking of selectins is therefore considered a promising therapeutic approach to treat acute and chronic inflammatory diseases which are caused by excessive extravasation of leukocytes. This mini-review highlights the major structural differences between E- and P-selectin and summarizes the resulting strategies for the design of selectin antagonists.

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“…Anti-67-kDa elastin/laminin binding protein (67BP) monoclonal antibody (mAb) BCZ 67 (IgM) was kindly provided by Dr. R. P. Mecham (Pulmonary Research, the Jewish Hospital at Washington University, St. Louis, MO) [18]. Anti-E-selectin mAb 68-5H11 (IgG1) [19], anti-P selectin mAb AK4 (IgG1) [20], and anti-L-selectin mAb DREG-56 (IgG1) [21] were purchased from Pharmingen, San Diego, CA; anti-L-selectin mAb SK11 (available as Leu 8, IgG2a) [22], anti-CD44 mAb L178 (IgG1) [23], anti-CD18 mAb L130 (IgG1) [24], and anti-ICAM-1 (CD54) mAb LB-2 (IgG2b) [25] were from Becton Dickinson, San Jose, CA; anti-NCA90 (CD66c) mAb CLBgran10 (IgG1) [6] was from Sanbyo, Uden, The Netherlands; anti-CD4 mAb TH/1 (IgG1), anti-CD11a mAb SPV-L7 (IgG1) [26], anti-CD11b mAb Bear1 (IgG1) [26], anti-CD11c mAb FK24 (IgG1) [27], anti-CD18 mAb CLB-LFA-1 (IgG1) [28], anti-CD 29 mAb SG/I9 [29], anti-CD49d SG/73 [29], and anti-CD49e KH/33 [29] were from Seikagaku Corp., Tokyo, Japan; and anti-CD18 7E4 (IgG1) [30] and anti-CD66b 80H3 (IgG1) [31] were from Immunotech S.A., Marseille, France.…”

Section: Antibodiesmentioning

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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Characterization of human platelet GMP-140 as a heparin-binding protein

Cited by 74 publications

References 16 publications

Obligatory Requirement of Sulfation for P-Selectin Binding to Human Salivary Gland Carcinoma Acc-M Cells and Breast Carcinoma ZR-75-30 Cells

Obligatory Requirement of Sulfation for P-Selectin Binding to Human Salivary Gland Carcinoma Acc-M Cells and Breast Carcinoma ZR-75-30 Cells

E- and P-Selectin: Differences, Similarities and Implications for the Design of P-Selectin Antagonists

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

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