P-selectin glycoprotein ligand 1 is a ligand for L-selectin on neutrophils, monocytes, and CD34+ hematopoietic progenitor cells.

Spertini, Olivier; Cordey, A S; Monai, N.; Giuffrè, Laura; Schapira, Marc

doi:10.1083/jcb.135.2.523

Cited by 203 publications

(129 citation statements)

References 73 publications

Supporting

Mentioning

125

Contrasting

Order By: Relevance

“…Antibodies and other ligands may interact with other selectins or lectin receptors resulting in nonspecific stimulatory or inhibitory effects. In particular, for an agent such as soluble PSGL-1 various studies have shown concomitant blockage of L-selectin 31,32 and E-selectin. 30,39 In addition, the local availability of the blocking antibodies may be compromised particularly in the presence of extensive occlusion of the vasculature.…”

Section: Discussionmentioning

confidence: 99%

“…For instance, PSGL-1 has been shown to serve as a ligand for L-selectin. [30][31][32] Finally, no study has investigated the potential role of P-selectin in platelet adhesion or deposition in ischemic tissue. Therefore, the purpose of this study was to investigate whether P-selectin mediates hepatic I/Rp injury using mice specifically lacking P-selectin adhesion molecules, with a particular focus placed on PMN and platelet adhesion.…”

mentioning

confidence: 99%

See 1 more Smart Citation

P–Selectin Mediates Reperfusion Injury Through Neutrophil and Platelet Sequestration in the Warm Ischemic Mouse Liver

Yadav¹,

et al. 1999

View full text Add to dashboard Cite

Hepatic damage following ischemia-reperfusion injury involves polymorphonuclear leukocytes (PMN) and platelet sequestration, however the mechanisms of adhesion remain elusive. In this study, using gene-targeted deficient mice, we evaluated P-selectin and its contribution to PMN and platelet adhesion in hepatic damage. In an in vivo warm ischemia model, hepatic injury was assessed by serum transaminase levels, survival, PMN adhesion by histological analysis, and platelet sequestration by immunostaining. Serum transaminase levels were strikingly reduced (by up to threefold) in the P-selectin deficient mice, particularly at 90 minutes of ischemia, when compared with wild-type controls. PMN adhesion and platelet sequestration was also significantly decreased in P-selectin deficient mice following 90 minutes of partial ischemia. Animal survival was significantly improved after 75 minutes of total hepatic ischemia in P-selectin deficient mice when compared with wild-type mice. Survival was also achieved after 90 minutes of ischemia in the mutant mice whereas none of the wild-type animals survived. These data show that P-selectin plays a critical role in PMN and platelet adhesion following ischemia-reperfusion injury to the liver. (HEPATOLOGY 1999; 29:1494-1502.)The pathogenesis of cell damage following reperfusion of ischemic tissue is an incompletely understood series of events. 1,2 Various mechanisms have been proposed including enhanced production of inflammatory mediators, 3-5 recruitment of polymorphonuclear leukocytes (PMN), 6,7 and blockage of blood flow. 7-9 The leukocyte-endothelial interaction that occurs following ischemia/reperfusion (I/Rp) injury has been shown to be important for microvascular dysfunction and release of cytotoxic mediators such as reactive oxygen intermediates and a variety of proteases. 10-12 We 13 and others 5,6,9,14,15 have shown leukocyte accumulation to be a critical determinant of hepatic I/Rp injury. Other blood elements including platelets adhere to the hepatic sinusoids in conditions of ischemia, 16,17 but little is known about their contribution to the injury.The adhesion of PMN and platelets to the vascular endothelium involves a variety of adhesion receptors. [18][19][20][21] The selectin family (P-, E-, and L-selectin) are the first to be engaged in the process, 19 with P-selectin acting at the earliest stage of interaction between PMN and the endothelium. P-selectin is found in the ␣ granules of resting platelets and Weibel-Palade bodies of endothelial cells, 18 and expression of P-selectin on the cell surface can occur within minutes under stimulation by mediators of inflammation such as thrombin, histamine, complement, and peroxide. 22 P-selectin is able to tether leukocytes to the endothelial surface through its ligand P-selectin glycoprotein ligand-1 (PSGL-1), which leads to their activation. 23 Once leukocytes attach, they can interact with flowing PMN and platelets through the action of P-and L-selectin, 23 which may lead to further adhesion of PMN and platelets as we...

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

P–Selectin Mediates Reperfusion Injury Through Neutrophil and Platelet Sequestration in the Warm Ischemic Mouse Liver

Yadav¹,

et al. 1999

View full text Add to dashboard Cite

show abstract

“…PSGL-1 is a ligand capable of binding P-, Eand L-selectin [7][8][9][10][11][12][13]. The molecule is expressed on several cell types, including human leukocytes and the human myeloid cell line HL-60 [7], [10], [14].…”

Section: Introductionmentioning

confidence: 99%

Partial characterization of the N-linked oligosaccharide structures on P-selectin glycoprotein ligand-1 (PSGL-1)

Aeed¹,

Geng

Asa³

et al. 2001

Cell Res

View full text Add to dashboard Cite

PSGL-1, a specific ligand for P-, E-and L-selectin, was isolated from in vivo [ 3 H]-glucosamine labeled HL-60 cells by a combination of wheat germ agglutinin-agarose and P-or E-selectin-agarose chromatography. N-linked oligosaccharides were released from the purified, denatured ligand molecule by peptide: N-glycosidase F treatment and, following separation by Sephacryl S-200 chromatography, partially characterized using lectin, ion-exchange and size-exclusion chromatography in combination with glycosidase digestions. The data obtained suggest that the N-glycans on PSGL-1 are predominantly core-fucosylated, multiantennary complex type structures with extended, poly-N-acetyllactosamine containing outer chains. A portion of the outer chains appears to be substituted with fucose indicating that the N-glycans, in addition to the Oglycans on PSGL-1, may be involved in selectin binding.

show abstract

“…L-selectin binds to at least four different glycosylated ligands expressed by high endothelial venules of lymph nodes, including glycosylated cell adhesion molecule-1, CD34, mucosal addressin cell adhesion molecule-1, and sulfated glycoprotein 200 (4). L-selectin also binds P-selectin glycoprotein ligand-1 (PSGL-1) 3 on leukocytes (5)(6)(7)(8).…”

mentioning

confidence: 99%

Fucosyltransferase VII-Deficient Mice with Defective E-, P-, and L-Selectin Ligands Show Impaired CD4+ and CD8+ T Cell Migration into the Skin, but Normal Extravasation into Visceral Organs

Erdmann¹,

Scheidegger²,

Koch³

et al. 2002

The Journal of Immunology

View full text Add to dashboard Cite

The first step of leukocyte extravasation, leukocyte rolling, is mediated by E-, P-, and L-selectins. Mice deficient for α-1,3-fucosyltransferase VII (FucTVII)−/− are characterized by deficiency of E-, P-, and L-selectin ligand activity. This model system was used to evaluate the role of the interactions of selectins with their ligands in T and B cell responses. In the present study, FucTVII−/− mice showed reduced CD4+ T cell-mediated contact hypersensitivity reactions of the ears to FITC as well as reduced CD8+ T cell-mediated delayed-type hypersensitivity reactions of the footpads against lymphocytic choriomeningitis virus infection. As Langerhans cell migration to local lymph nodes as well as CD4+ and CD8+ T cell induction were found to be normal, the afferent arm of these reactions was not impaired. The reduced inflammatory reactions of the skin were due to inefficient lymphocyte extravasation into the skin. In contrast, extravasation of CD4+ and CD8+ T cells into visceral organs, such as the ovaries or the brain, was not impaired in FucTVII−/− mice. Elimination of vaccinia virus and of lymphocytic choriomeningitis virus from ovaries and brain, as well as elimination of tumor cells from several visceral organs was normal. Thus, interactions of selectins with their ligands are important for lymphocyte homing into the skin, but not for lymphocyte extravasation into visceral organs.

show abstract

P-selectin glycoprotein ligand 1 is a ligand for L-selectin on neutrophils, monocytes, and CD34+ hematopoietic progenitor cells.

Cited by 203 publications

References 73 publications

P–Selectin Mediates Reperfusion Injury Through Neutrophil and Platelet Sequestration in the Warm Ischemic Mouse Liver

P–Selectin Mediates Reperfusion Injury Through Neutrophil and Platelet Sequestration in the Warm Ischemic Mouse Liver

Partial characterization of the N-linked oligosaccharide structures on P-selectin glycoprotein ligand-1 (PSGL-1)

Fucosyltransferase VII-Deficient Mice with Defective E-, P-, and L-Selectin Ligands Show Impaired CD4+ and CD8+ T Cell Migration into the Skin, but Normal Extravasation into Visceral Organs

Contact Info

Product

Resources

About