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Relevant bibliographies by topics / P-selectin ligand protein

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Journal articles

Academic literature on the topic 'P-selectin ligand protein'

Author: Grafiati

Published: 4 May 2024

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Journal articles on the topic "P-selectin ligand protein"

1

Lenter, M., A. Levinovitz, S. Isenmann, and D. Vestweber. "Monospecific and common glycoprotein ligands for E- and P-selectin on myeloid cells." Journal of Cell Biology 125, no. 2 (1994): 471–81. http://dx.doi.org/10.1083/jcb.125.2.471.

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E- and P-selectin are inducible cell adhesion molecules on endothelial cells, which function as Ca(2+)-dependent lectins and mediate the binding of neutrophils and monocytes. We have recently identified a 150-kD glycoprotein ligand for E-selectin on mouse myeloid cells, using a recombinant antibody-like form of mouse E-selectin. Here, we report that this ligand does not bind to an analogous P-selectin fusion protein. Instead, the chimeric P-selectin-IgG protein recognizes a 160-kD glycoprotein on the mouse neutrophil progenitor 32D cl 3, on mature mouse neutrophils and on human HL60 cells. The

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2

Frenette, Paul S., Cécile V. Denis, Linnea Weiss, et al. "P-Selectin Glycoprotein Ligand 1 (Psgl-1) Is Expressed on Platelets and Can Mediate Platelet–Endothelial Interactions in Vivo." Journal of Experimental Medicine 191, no. 8 (2000): 1413–22. http://dx.doi.org/10.1084/jem.191.8.1413.

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The platelet plays a pivotal role in maintaining vascular integrity. In a manner similar to leukocytes, platelets interact with selectins expressed on activated endothelium. P-selectin glycoprotein ligand 1 (PSGL-1) is the main P-selectin ligand expressed on leukocytes. Searching for platelet ligand(s), we used a P-selectin–immunoglobulin G (IgG) chimera to affinity purify surface-biotinylated proteins from platelet lysates. P-selectin–bound ligands were eluted with ethylenediaminetetraacetic acid. An ∼210-kD biotinylated protein was isolated from both human neutrophil and platelet preparation

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3

HARMS, Gesche, Regine KRAFT, Gerlinde GRELLE, Bärbel VOLZ, Jens DERNEDDE, and Rudolf TAUBER. "Identification of nucleolin as a new L-selectin ligand." Biochemical Journal 360, no. 3 (2001): 531–38. http://dx.doi.org/10.1042/bj3600531.

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Apart from leucocyte–endothelial interactions, the adhesion molecule L-selectin mediates the homotypic adhesion of leucocytes during recruitment at sites of acute inflammation, as well as intercellular adhesion of haematopoietic progenitor cells during haematopoiesis. There is evidence that, in addition to P-selectin glycoprotein ligand-1, other as-yet-unidentified proteins function as L-selectin ligands on human leucocytes and haematopoietic progenitor cells. In the present study, we show: (i) by affinity chromatography on L-selectin–agarose; (ii) by protein identification using MS; and (iii)

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4

Thomas, Susan N., Ronald L. Schnaar, and Konstantinos Konstantopoulos. "Podocalyxin-like protein is an E-/L-selectin ligand on colon carcinoma cells: comparative biochemical properties of selectin ligands in host and tumor cells." American Journal of Physiology-Cell Physiology 296, no. 3 (2009): C505—C513. http://dx.doi.org/10.1152/ajpcell.00472.2008.

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Selectins facilitate metastasis and tumor cell arrest in the microvasculature by mediating binding of selectin-expressing host cells to ligands on tumor cells. We recently identified CD44 variant isoforms as functional P-, but not E-/L-, selectin ligands on colon carcinoma cells. Furthermore, a ∼180-kDa sialofucosylated glycoprotein(s) mediated selectin binding in CD44-knockdown cells. Using immunoaffinity chromatography and tandem mass spectrometry, we identify podocalyxin-like protein (PCLP) as an alternative selectin ligand. Blot rolling and cell-free flow-based adhesion assays disclose tha

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5

Guyer, DA, KL Moore, EB Lynam, et al. "P-selectin glycoprotein ligand-1 (PSGL-1) is a ligand for L-selectin in neutrophil aggregation." Blood 88, no. 7 (1996): 2415–21. http://dx.doi.org/10.1182/blood.v88.7.2415.bloodjournal8872415.

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In inflammation, activated neutrophils adhere to endothelial cells and aggregate with one another. While beta 2-integrin and L-selectin are essential for aggregation, their ligands remain to be identified. We have previously shown that L-selectin mediates a carbohydrate-dependent interaction in aggregation (Simon et al: J Immunol 149:2765, 1992; Rochon et al: J Immunol 152:1385, 1994). We have suggested that the L-selectin counter-structure is a mucinlike protein and proposed that aggregation occurs through a two-step process involving L-selectin, beta 2-integrin, and their distinct counter-st

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6

Moore, K. L., N. L. Stults, S. Diaz, et al. "Identification of a specific glycoprotein ligand for P-selectin (CD62) on myeloid cells." Journal of Cell Biology 118, no. 2 (1992): 445–56. http://dx.doi.org/10.1083/jcb.118.2.445.

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P-selectin (CD62, GMP-140, PADGEM), a Ca(2+)-dependent lectin on activated platelets and endothelium, functions as a receptor for myeloid cells by interacting with sialylated, fucosylated lactosaminoglycans. P-selectin binds to a limited number of protease-sensitive sites on myeloid cells, but the protein(s) that carry the glycans recognized by P-selectin are unknown. Blotting of neutrophil or HL-60 cell membrane extracts with [125I]P-selectin and affinity chromatography of [3H]glucosamine-labeled HL-60 cell extracts were used to identify P-selectin ligands. A major ligand was identified with

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7

Zöllner, Olaf, Martin C. Lenter, James E. Blanks, et al. "L-Selectin from Human, but Not from Mouse Neutrophils Binds Directly to E-Selectin." Journal of Cell Biology 136, no. 3 (1997): 707–16. http://dx.doi.org/10.1083/jcb.136.3.707.

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L-Selectin on neutrophils as well as inducible E- and P-selectin on endothelium are involved in the recruitment of neutrophils into inflamed tissue. Based on cell attachment assays, L-selectin was suggested to function as a carbohydrate presenting ligand for E- and P-selectin. However, previous affinity isolation experiments with an E-selectin–Ig fusion protein had failed to detect L-selectin among the isolated E-selectin ligands from mouse neutrophils. We show here that L-selectin from human neutrophils, in contrast to mouse neutrophils, can be affinity-isolated as a major ligand from total c

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8

Moore, K. L., K. D. Patel, R. E. Bruehl, et al. "P-selectin glycoprotein ligand-1 mediates rolling of human neutrophils on P-selectin." Journal of Cell Biology 128, no. 4 (1995): 661–71. http://dx.doi.org/10.1083/jcb.128.4.661.

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Neutrophils roll on P-selectin expressed by activated platelets or endothelial cells under the shear stresses in the microcirculation. P-selectin glycoprotein ligand-1 (PSGL-1) is a high affinity ligand for P-selectin on myeloid cells. However, it has not been demonstrated that PSGL-1 contributes to the rolling of neutrophils on P-selectin. We developed two IgG mAbs, PL1 and PL2, that appear to recognize protein-dependent epitopes on human PSGL-1. The mAbs bound to PSGL-1 on all leukocytes as well as on heterologous cells transfected with PSGL-1 cDNA. PL1, but not PL2, blocked binding of 125-I

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9

Spertini, O., A. S. Cordey, N. Monai, L. Giuffrè, and M. Schapira. "P-selectin glycoprotein ligand 1 is a ligand for L-selectin on neutrophils, monocytes, and CD34+ hematopoietic progenitor cells." Journal of Cell Biology 135, no. 2 (1996): 523–31. http://dx.doi.org/10.1083/jcb.135.2.523.

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Selectins play a critical role in initiating leukocyte binding to vascular endothelium. In addition, in vitro experiments have shown that neutrophils use L-selectin to roll on adherent neutrophils, suggesting that they express a nonvascular L-selectin ligand. Using a L-selectin/IgM heavy chain (mu) chimeric protein as an immunocytological probe, we show here that L-selectin can bind to neutrophils, monocytes, CD34+ hematopoietic progenitors, and HL-60 and KG-1 myeloid cells. The interaction between L-selectin and leukocytes was protease sensitive and calcium dependent, and abolished by cell tr

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10

Evangelista, Virgilio, Stefano Manarini, Rita Sideri, et al. "Platelet/Polymorphonuclear Leukocyte Interaction: P-Selectin Triggers Protein-Tyrosine Phosphorylation–Dependent CD11b/CD18 Adhesion: Role of PSGL-1 as a Signaling Molecule." Blood 93, no. 3 (1999): 876–85. http://dx.doi.org/10.1182/blood.v93.3.876.

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Abstract Polymorphonuclear leukocyte (PMN) adhesion to activated platelets is important for the recruitment of PMN at sites of vascular damage and thrombus formation. We have recently shown that binding of activated platelets to PMN in mixed cell suspensions under shear involves P-selectin and the activated β2-integrin CD11b/CD18. Integrin activation required signaling mechanisms that were sensitive to tyrosine kinase inhibitors.1 Here we show that mixing activated, paraformaldehyde (PFA)-fixed platelets with PMNs under shear conditions leads to rapid and fully reversible tyrosine phosphorylat

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