E Selectin And P Selectin

Main Outcome Measures After 5 days of diet, mice were administered iodine 125–labeled anti–Pselectin antibody (or iodine 125–labeled anti–Eselectin antibody) and iodine 131–labeled nonbinding antibody to quantify Pselectin (or Eselectin) expression in organs (lung, liver, kidney, small intestine, colon, stomach, pancreas.

E selectin and p selectin. Eselectin, also known as CD62 antigenlike family member E (CD62E), endothelialleukocyte adhesion molecule 1 (ELAM1), or leukocyteendothelial cell adhesion molecule 2 (LECAM2), is a selectin cell adhesion molecule expressed only on endothelial cells activated by cytokinesLike other selectins, it plays an important part in inflammationIn humans, Eselectin is encoded by the SELE gene. Formerly sold as BE Endothelial Leukocyte Adhesion Molecule1 (ELAM1, Eselectin) belongs to the selectin family of adhesion molecules Together with LECAM1 (Lselectin) and GMP140 (Pselectin), Eselectin mediates the initial interactions of leukocytes and platelets with endothelial cells. Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P and Eselectin bound to SLe(X) and PSGL1 Cell 00 Oct.

Eselectin (CD62E) is an endothelial cell specific selectin that is expressed only after activation with proinflammatory cytokines In vitro experiments have shown that IL1, TNFalpha and bacterial wall components like lipopolysaccharides induce the transcription of Eselectin in a NFkB dependent signaling cascade. Pselectin is an adhesion molecule translocated to the surface of endothelial cells and platelets under inflammatory stimuli, and its potential as a biomarker in inflammatory conditions has driven preclinical studies to investigate its application for molecular imaging of inflammation Clinical imaging of Pselectin expression for disease characterization could have an important role in. Eselectin is a 115 kDa type I transmembrane protein and a member of the selectin family of adhesion molecules Eselectin is expressed on cytokineactivated endothelial cells Along with Lselectin and Pselectin, Eselectin mediates the initial interactions of leukocytes and platelets with endothelial cells Eselectin is thought to play a.

Both P and Eselectin are cognate ligands for monocyte receptor, PSGL1 PSGL1 initiates adhesion, rolling, recruitment, and extravasation of leukocytes, as shown in flow systems and in vivo (49, 50), but its role in monocyte activation and differentiation is unexplored We used an agonist antiPSGL1 antibody (fig S8, A and B) to investigate. ESelectin and PSelectin are related (44% amino acid sequence identity) adhesion molecules containing multiple short complementlike repeats and an Nterminal C‑type lectin domain in their extracellular regions ESelectin is expressed on activated vascular endothelial cells and PSelectin occurs on activated platelets and endothelial cells. Pselectin is an adhesion molecule translocated to the surface of endothelial cells and platelets under inflammatory stimuli, and its potential as a biomarker in inflammatory conditions has driven preclinical studies to investigate its application for molecular imaging of inflammation Clinical imaging of Pselectin expression for disease characterization could have an important role in.

Eselectin, is a kDa glycoprotein expressed on inflamed vascular endothelial cells in response to the inflammatory cytokines TNFα and IL1β As well as the role Eselectin plays in. Pselectin on platelets and endothelial cells and Eselectin on endothelial cells are leukocyte receptors that recognize lineagespecific carbohydrates on neutrophils and monocytes The proposed ligands for these receptors contain the Le(x) core and sialic acid. E and Pselectin differences, similarities and implications for the design of Pselectin antagonists Chimia (rau) 11;65(4)2103 Authors Florian P C.

The expression of Pselectin and Eselectin on dermal vessels that was highest at 12 hours and 3 hours, respectively (P 005) Numerous platelet aggregates recognized by the antiPselectin antibody were present in the lumina of vessels and in perivascular tissues These results demonstrate that TNF can induce the expression. Pselectin, the largest selectin, is stored in αgranules of platelets and in Weibel–Palade bodies of endothelial cells, and is translocated to the cell surface of. Pselectin glycoprotein ligand1 (PSGL1) derived from human neutrophils is also a highefficiency ligand for endotheliumexpressed Eselectin under flow It mediates.

Main Outcome Measures After 5 days of diet, mice were administered iodine 125–labeled anti–Pselectin antibody (or iodine 125–labeled anti–Eselectin antibody) and iodine 131–labeled nonbinding antibody to quantify Pselectin (or Eselectin) expression in organs (lung, liver, kidney, small intestine, colon, stomach, pancreas. The specificity of L, P, or Eselectin/μ chimera binding to PSGL1 was indicated by the abrogation of binding in the presence of 5 m m EDTA or 100 μg/ml of appropriate antiL, P, or Eselectin blocking mAb (LAM1–3, WAPS 122, and H18/7) 5000 cells were analyzed in each experiment on an Epics XLMCL cytofluorimeter (Beckman Instruments). Inhibition of Eselectin expression in thrombintreated endothelium resulted in prolonged Pselectin expression well beyond the normal 60min time frame One potential explanation is cross talk between Pselectin and Eselectin in the human system Evidence to support cross talk between Pselectin and Eselectin has been reported in mice.

Objective To investigate the expression of P‐ and E‐selectin and intercellular adhesion molecule 1 (ICAM‐1) in the vasculature of mouse cremaster muscles both with and without tumor necrosis factor. The three selectins, Eselectin (CD62E), Lselectin (CD62L) and Pselectin (CD62P), are related both structurally and functionally They have been extensively studied. ESelectin (CD62E) and PSelectin (CD62P) are related (44% amino acid sequence identity) adhesion molecules containing multiple short complementlike repeats and an.

Although of Pselectin in the liver could be detected in centrilobular Pselectin is preformed and stored in WeibelPalade bodies and portal veins and some portal capillaries on day 1 pi of endothelial cells, platelets, and megakaryocytes of un and became slightly reduced between days 2 and 3 pi stimulated animals,15 Pselectin was only. Pselectin and Eselectin are part of a family of adhesion molecules classified as selectins on the basis of their structural homology (1417) Pselectin recognizes the CD15 antigen on leukocytes;. Pselectin glycoprotein ligand1 (PSGL1, also called CD162), the bestcharacterized selectin ligand, binds to both P and Eselectin and is expressed by HSPCs, as well as by mature myeloid cells.

Carbohydrates on tumor cells have been shown to play an important role in tumor metastasis We demonstrated before that CD24, a M r 35,000–60,000 mucinetype glycosylphosphatidylinositollinked cell surface molecule, can function as ligand for Pselectin and that the sialylLex carbohydrate is essential for CD24mediated rolling of tumor cells on Pselectin. Pselectin that is expressed on the surface of the endothelium mediates abnormal rolling and static adhesion of sickle erythrocytes to the vessel surface in vitro 13,14 Translocation of. ESelectin and PSelectin are related (44% amino acid sequence identity) adhesion molecules containing multiple short complementlike repeats and an Nterminal C‑type lectin domain in their extracellular regions ESelectin is expressed on activated vascular endothelial cells and PSelectin occurs on activated platelets and endothelial cells.

Both Eand Pselectins are expressed on human arterial luminal endothelial cells of atherosclerotic plaques (195, 196), and mouse studies have shown that Eselectin and/or Pselectin deficiency substantially reduces the formation of atherosclerotic plaques, suggesting an overlapping function of these two selectins in the development of. Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P and Eselectin bound to SLe(X) and PSGL1 Cell 00 Oct 27;103(3) PMID. Pselectin is an adhesion molecule translocated to the surface of endothelial cells and platelets under inflammatory stimuli, and its potential as a biomarker in inflammatory conditions has driven preclinical studies to investigate its application for molecular imaging of inflammation Clinical imaging of Pselectin expression for disease characterization could have an important role in.

The selectin opment of AIA was significantly (P < 001) inhibited by family of adhesion molecules (P, E, and Lselectin) mAb to E but not to Pselectin (mean score on day 14 mediates the initial rolling of leukocytes along the control 102, antiE 28, antiP 91). The expression levels of E and Pselectin and vascular cell adhesion molecule1 (VCAM1) in glomeruli of different histopathologic grades of MRL/MpJlpr/lpr (MRL/lpr) lupus mice was studied using lasercapture microdissection of the glomeruli, followed by reverse transcriptionpolymerase chain reaction (RTPCR) analysisThe glomerular lesions in SCID mice injected with the 2B113 and 7B68. There was no correlation btween Pselectin and Eselectin, but there was a significant correlation between Eselectin and ICAM1 in all patients The plasma levels of GMP140 in patients with nonsmall cell lung cancer were much higher than those of the controls.

Compartments Pselectin to secretory granules, Eselectin to the plasma membrane, and Lselectin to the tips of microfolds on leukocytes Selectin ligands There are many candidate ligands for selectins, but only Pselectin glycoprotein ligand 1 (PSGL1) has been extensively characterized at the molecular, cellular and functional level (Fig 2). An almost opposing picture emerged for Pselectin all cells of the sLeA/egative group bound Pselectins under static, but not under flow conditions The “noncanonical” ligands for E vs Pselectin are therefore functional under divergent conditions. E‐ and P‐selectin mediate the rolling of leucocytes on EC, prior to integrin‐mediated arrest and subsequent transmigration into tissues 9, 10 They are expressed on the surface of EC in response to inflammatory stimuli such as TNFα and IL‐1.

Formerly sold as BE Endothelial Leukocyte Adhesion Molecule1 (ELAM1, Eselectin) belongs to the selectin family of adhesion molecules Together with LECAM1 (Lselectin) and GMP140 (Pselectin), Eselectin mediates the initial interactions of leukocytes and platelets with endothelial cells. Selectins bind to carbohydrate ligands in a calciumdependent manner and play critical roles in host defense and possibly in tumor metastasis To isolate peptides that mimic Eselectin ligands, we screened a phage peptide library using Eselectin as a target molecule This attempt unexpectedly failed, probably because the binding affinity of Eselectin to its ligand is low. Main Outcome Measures After 5 days of diet, mice were administered iodine 125–labeled anti–Pselectin antibody (or iodine 125–labeled anti–Eselectin antibody) and iodine 131–labeled nonbinding antibody to quantify Pselectin (or Eselectin) expression in organs (lung, liver, kidney, small intestine, colon, stomach, pancreas.

Pselectin on platelets and endothelial cells and Eselectin on endothelial cells are leukocyte receptors that recognize lineagespecific carbohydrates on neutrophils and monocytes The proposed ligands for these receptors contain the Le(x) core and sialic acid. PSelectin (also designated GMP140 or CD62P), expressed on activated platelets and endothelial cells, and ESelectin (also designated ELMA1 or CD62E), expressed on endothelial cells, exhibit overlapping ligand specificities Both recognize sialylLe (x) as a ligand and bind to specific carbohydrates on neutrophils and monocytes. If PSGL1 is the sole ligand for Pselectin on Th1 cells in vivo, then the migration of PSGL1 −/ − cells observed when they were injected into PSGL1 / mice must be mediated by Eselectin, as P and Eselectin together mediate Th1 cell migration into the inflamed skin 8 This predicts that PSGL1 is not required for Eselectin–mediated.

E‐selectin and P‐selectin are thought to be important in the infiltration of T lymphocytes in inflammation, but their role in cytokine‐induced cutaneous inflammatory reactions has not been examined A technique for quantifying labeled T lymphocyte migration to cytokine‐induced dermal inflammation in mice was developed. LNF 111,' which includes a Le" core, inhibits the binding of cells expressing Pselectin with CD15positive. Compartments Pselectin to secretory granules, Eselectin to the plasma membrane, and Lselectin to the tips of microfolds on leukocytes Selectin ligands There are many candidate ligands for selectins, but only Pselectin glycoprotein ligand 1 (PSGL1) has been extensively characterized at the molecular, cellular and functional level (Fig 2).

Objective To investigate the expression of P‐ and E‐selectin and intercellular adhesion molecule 1 (ICAM‐1) in the vasculature of mouse cremaster muscles both with and without tumor necrosis factor. The infused E coli produce high circulating levels of LPS, which, like TNFα, augments Eselectin but not Pselectin mRNA in HUVEC24Previous immunohistochemical analysis showed that E coliinduces expression of Eselectin protein in venular endothelium within 2 hours after injection into baboons37 After 4 hours, we observed consistent. Eselectin, is a kDa glycoprotein expressed on inflamed vascular endothelial cells in response to the inflammatory cytokines TNFα and IL1β As well as the.

Pselectin has a functional role in metastasis of tumor similar to Eselectin 13 Pselectin is expressed on the surface of both stimulated endothelial cell and activated platelet and helps cancer cells invade into bloodstream for metastasis and provided locally with multiple growth factors respectively 14. Insights into the molecular basis of leukocyte tethering and rolling revealed by structures of P and Eselectin bound to SLe(X) and PSGL1 Cell 00 Oct 27;103(3) PMID. Pselectin on platelets and endothelial cells and Eselectin on endothelial cells are leukocyte receptors that recognize lineagespecific carbohydrates on.

ESelectin and PSelectin are related (44% amino acid sequence identity) adhesion molecules containing multiple short complementlike repeats and an Nterminal C‑type lectin domain in their extracellular regions ESelectin is expressed on activated vascular endothelial cells and PSelectin occurs on activated platelets and endothelial cells. Pselectin glycoprotein ligand1 (PSGL1, also called CD162), the bestcharacterized selectin ligand, binds to both P and Eselectin and is expressed by HSPCs, as well as by mature myeloid cells. Selectins Selectins are a family of three closely related glycoproteins (Pselectin expressed on platelets and leukocytes, Eselectin expressed on endothelial cells, and.

Objective To investigate the expression of P‐ and E‐selectin and intercellular adhesion molecule 1 (ICAM‐1) in the vasculature of mouse cremaster muscles both with and without tumor necrosis factor a (TNF‐α) treatment Methods Mice received injections of monoclonal antibody to P‐selectin, E‐selectin, or ICAM‐1 before fixation to restrict detection to antigen expressed on the. Lselectin, also known as SELL or CD62L, is a member of the selectin family of adhesion molecules that includes Eselectin and Pselectin (PMID , , ) Lselectin is a protein with the calculated molecular mass of 42 kDa but actually kDa on neutrophils and 74 kDa on lymphocytes because of the highly glycosylation. Carbohydrates on tumor cells have been shown to play an important role in tumor metastasis We demonstrated before that CD24, a M r 35,000–60,000 mucinetype glycosylphosphatidylinositollinked cell surface molecule, can function as ligand for Pselectin and that the sialylLex carbohydrate is essential for CD24mediated rolling of tumor cells on Pselectin.

ESelectin and PSelectin are related (44% amino acid sequence identity) adhesion molecules containing multiple short complementlike repeats and an Nterminal C‑type lectin domain in their extracellular regions ESelectin is expressed on activated vascular endothelial cells and PSelectin occurs on activated platelets and endothelial cells. Robert Scott, Travis Moore, John France, Steven Rychnovsky, Pauline McEwan, Washington Hospital Center, Washington DC, Mirvant Corporation, Santa Barbara, CA 1115 am Background In humans, rupture of vulnerable plaques is one of the leading causes of 8122 ESelectin and PSelectin Are Markers of Aortic Plaque cardiovascularrelated mortality. Pselectin that is expressed on the surface of the endothelium mediates abnormal rolling and static adhesion of sickle erythrocytes to the vessel surface in vitro 13,14 Translocation of.

Selectins bind to carbohydrate ligands in a calciumdependent manner and play critical roles in host defense and possibly in tumor metastasis To isolate peptides that mimic Eselectin ligands, we screened a phage peptide library using Eselectin as a target molecule This attempt unexpectedly failed, probably because the binding affinity of Eselectin to its ligand is low. (The Pselectin and Eselectin genes are tightly linked on 1q) The entire set of Pselectin polymorphisms provided a heterozygosity of 91% The polymorphisms were tightly associated with one another and displayed patterns of linkage disequilibrium suggesting the existence of highly conserved ancestral haplotypes. In rat AIA, using L‐, P‐, and E‐selectin adhesion‐blocking mAb for an acute, short‐term, selectin‐blocking experiment, we demonstrated that the migration (2 hours) of radiolabeled blood neutrophils and monocytes to joints at the peak of joint inflammation is largely mediated by P‐selectin, and E‐selectin contributes to migration.

E and Pselectins synergistically inhibit bleomycininduced pulmonary fibrosis Horikawa M(1), Fujimoto M, Hasegawa M, Matsushita T, Hamaguchi Y, Kawasuji A, Matsushita. Detect Mouse E Selectin/SELE with 10pg/ml sensitivity Format 96well plate with removable strips Compatible samples cell culture supernatants, serum and plasma (heparin, citrate) This is a TMB colorimetric sandwich ELISA kit with short assay time and fast experiment set up E Selectin/SELE tissue specificity Cite This Product. Pselectin was not, however, detected in normal arterial endothelium or in endothelium overlying inactive fibrous plaques 38 Adhesion of monocytes and related cell lines to these tissues were inhibited by an antibody directed towards Pselectin that correlated with the specific endothelial localization of this adhesion molecule 39 In a baboon.