Mechanisms of eosinophil adherence to cultured vascular endothelial cells. Eosinophils bind to the cytokine-induced ligand vascular cell adhesion molecule-1 via the very late activation antigen-4 integrin receptor.

Dobrina, Aldo; Menegazzi, Renzo; Carlos, Timothy M.; Nardon, Ermanno; Cramer, Rita; Zacchi, T; Harlan, John M.; Patriarca, Pierluigi

doi:10.1172/jci115278

Cited by 255 publications

(90 citation statements)

References 33 publications

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“…Finally, acetylation of choline lysophospholipids to produce PAF in HCAEC may also play an important role in heart disease. Although PAF remains endothelial cell-associated (21), increased PAF production results in increased binding of neutrophils to the endothelial cell surface (25,31) and may play a role in the adhesive interaction of other cells such as eosinophils (8), thus contributing to progressing atherothrombosis and inflammatory processes in the coronary vasculature.…”

Section: Discussionmentioning

confidence: 99%

Calcium-independent phospholipase A₂-catalyzed plasmalogen hydrolysis in hypoxic human coronary artery endothelial cells

Meyer¹,

McHowat²

2007

American Journal of Physiology-Cell Physiology

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Meyer MC, McHowat J. Calcium-independent phospholipase A2-catalyzed plasmalogen hydrolysis in hypoxic human coronary artery endothelial cells. Am J Physiol Cell Physiol 292: C251-C258, 2007. First published August 30, 2006; doi:10.1152/ajpcell.00120.2006.-Thrombin stimulation of human coronary artery endothelial cells (HCAEC) results in activation of a membrane-associated, calcium-independent phospholipase A2 (iPLA2) that selectively hydrolyzes membrane plasmalogen phospholipids. Rupture of an atherosclerotic plaque and occlusion of the coronary vasculature results in a coronary ischemic event in which HCAEC in the ischemic area would be exposed to dramatic decreases in oxygen tension in addition to thrombin exposure. We exposed HCAEC to hypoxia in the presence or absence of thrombin stimulation and measured iPLA 2 activation, membrane phospholipid hydrolysis, and the accumulation of biologically active phospholipid metabolites. HCAEC exposed to hypoxia, thrombin stimulation, or a combination of the two conditions demonstrated an increase in iPLA2 activity and an increase in arachidonic acid release from plasmenylcholine. Thrombin stimulation of normoxic HCAEC did not result in an accumulation of choline lysophospholipids, but hypoxia alone and in combination with thrombin stimulation led to a significant accumulation of lysoplasmenylcholine (LPlsCho). We propose that the presence of hypoxia inhibits LPlsCho catabolism, at least in part, as a result of the accumulation of long-chain acylcarnitines. The combination of increased production and decreased catabolism of LPlsCho is necessary for its accumulation. Pretreatment with bromoenol lactone to inhibit iPLA2 blocked membrane phospholipid hydrolysis and production of membrane phospholipid-derived metabolites. The increase in iPLA2 activity and the subsequent accumulation of membrane phospholipid-derived metabolites in HCAEC exposed to hypoxia or thrombin stimulation alone, and particularly in combination, have important implications in inflammation and arrhythmogenesis in atherosclerosis/thrombosis and subsequent myocardial ischemia. myocardial ischemia; arrhythmogenesis; thrombosis SUDDEN CARDIAC DEATH in humans invariably results from malignant ventricular arrhythmias secondary to acute myocardial ischemia precipitated by the evolution of an intracoronary thrombus (3,7,32). We have demonstrated previously that thrombin stimulation of human coronary artery endothelial cells (HCAEC) results in hydrolysis of membrane plasmalogen phospholipids by a Ca 2ϩ -independent phospholipase A 2 (iPLA 2 ) that leads to the generation of several phospholipid metabolites that may play an important role in inflammation or arrhythmogenesis in the heart (21).Once blood flow is interrupted or severely reduced by increased or complete occlusion of a coronary artery precipitating an ischemic event, the endothelial cells in the ischemic area would be exposed to dramatic decreases in oxygen tension in addition to exposure to thrombin. Results from studies involving release of arachido...

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Section: Discussionmentioning

confidence: 99%

Calcium-independent phospholipase A₂-catalyzed plasmalogen hydrolysis in hypoxic human coronary artery endothelial cells

Meyer¹,

McHowat²

2007

American Journal of Physiology-Cell Physiology

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“…and prepared for direct microscopy analysis following previously described procedures (23). After surgical setup, the ileal mesentery was exposed and the microvascular trafficking of fluorescent labeled leukocytes (AO, i.v.…”

Section: Intravital Microscopy Analysismentioning

confidence: 99%

“…After 30-min incubation at 37°C, unbound leukocytes were removed by washing, whereas the number of adherent cells was evaluated by a colorimetric assay using tetramethylbenzidine as a substrate for myeloperoxidase, as previously described (23). Percentage of PMN adherence was calculated using a calibration curve.…”

Section: Pmn Adhesion Assaymentioning

confidence: 99%

The Neutrophil-Activating Protein of Helicobacter pylori Crosses Endothelia to Promote Neutrophil Adhesion In Vivo

Polenghi

Bossi

Fischetti

et al. 2007

The Journal of Immunology

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Helicobacter pylori induces an acute inflammatory response followed by a chronic infection of the human gastric mucosa characterized by infiltration of neutrophils/polymorphonuclear cells (PMNs) and mononuclear cells. The H. pylori neutrophil-activating protein (HP-NAP) activates PMNs, monocytes, and mast cells, and promotes PMN adherence to the endothelium in vitro. By using intravital microscopy analysis of rat mesenteric venules exposed to HP-NAP, we demonstrated, for the first time in vivo, that HP-NAP efficiently crosses the endothelium and promotes a rapid PMN adhesion. This HP-NAP-induced adhesion depends on the acquisition of a high affinity state of β2 integrin on the plasma membrane of PMNs, and this conformational change requires a functional p38 MAPK. We also show that HP-NAP stimulates human PMNs to synthesize and release a number of chemokines, including CXCL8, CCL3, and CCL4. Collectively, these data strongly support a central role for HP-NAP in the inflammation process in vivo: indeed, HP-NAP not only recruits leukocytes from the vascular lumen, but also stimulates them to produce messengers that may contribute to the maintenance of the flogosis associated with the H. pylori infection.

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“…In contrast, VCAM-1 antibodies are extremely effective at inhibiting eosinophil but not neutrophil adherence (Bochner et al 1991). Furthermore, anti-VLA-4 antibodies inhibit eosinophil, but not neutrophil, adhesion to IL-1 stimulated endothelium (Dobrina et al 1991, Walsh et al 1991. These results indicate that specific induction of VCAM-1 on endothelial cells could selectively promote eosinophil adherence.…”

Section: Eosinophil-endothelial Interactionsmentioning

confidence: 99%

Expression and function of beta1 integrins on human eosinophils

Seminario

Bochner

1997

Mem. Inst. Oswaldo Cruz

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Mechanisms of eosinophil adherence to cultured vascular endothelial cells. Eosinophils bind to the cytokine-induced ligand vascular cell adhesion molecule-1 via the very late activation antigen-4 integrin receptor.

Cited by 255 publications

References 33 publications

Calcium-independent phospholipase A₂-catalyzed plasmalogen hydrolysis in hypoxic human coronary artery endothelial cells

Calcium-independent phospholipase A₂-catalyzed plasmalogen hydrolysis in hypoxic human coronary artery endothelial cells

The Neutrophil-Activating Protein of Helicobacter pylori Crosses Endothelia to Promote Neutrophil Adhesion In Vivo

Expression and function of beta1 integrins on human eosinophils

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