Phosphatidylserine‐related adhesion of human erythrocytes to vascular endothelium

Closse, C.; Dachary‐Prigent, Jeanne; Boisseau, M. R.

doi:10.1046/j.1365-2141.1999.01718.x

Cited by 289 publications

(240 citation statements)

References 12 publications

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“…Eryptotic cells may further adhere to the vascular wall [3,17,28,60,72] and foster blood clotting [3,16,75]. Thus, phosphatidylserine-exposing erythrocytes may compromise the microcirculation.…”

Section: Discussionmentioning

confidence: 99%

Hemin-induced suicidal erythrocyte death

2009

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Several diseases, such as malaria, sickle cell disease, and ischemia/reperfusion may cause excessive formation of hemin, which may in turn trigger hemolysis. A variety of drugs and diseases leading to hemolysis triggers suicidal erythrocyte death or eryptosis, i.e., cell membrane scrambling and cell shrinkage. Eryptosis is elicited by increased cytosolic Ca 2+ activity and by ceramide. The present study explored whether hemin stimulates eryptosis. Cell membrane scrambling was estimated from annexin Vbinding to phosphatidylserine exposed at the cell surface, cell shrinkage from forward scatter in fluorescence-activated cell sorter analysis, cytosolic Ca 2+ activity from Fluo3 fluorescence and ceramide formation from fluorescencelabeled antibody binding. Exposure to hemin (1-10 μM) within 48 h significantly increased annexin V-binding, decreased forward scatter, increased cytosolic Ca 2+ activity, and stimulated ceramide formation. In conclusion, hemin stimulates suicidal cell death, which may in turn contribute to the clearance of circulating erythrocytes and thus to anemia.

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Section: Discussionmentioning

confidence: 99%

Hemin-induced suicidal erythrocyte death

2009

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“…Control cells were prepared in parallel without any treatments. To investigate the PS dependence of the adhesion, RBC with enhanced PS exposure were incubated with annexin V as reported previously (6,8,11,24). In brief, RBC with enhanced PS exposure were incubated with 8.8 g/ml annexin V at 37°C for 30 min on a mixer at 400 rpm prior to the adhesion assay.…”

Section: Methodsmentioning

confidence: 99%

Section: The Adhesion Of Red Blood Cells (Rbc)mentioning

confidence: 99%

“…RBC with enhanced PS exposure were obtained by the treatment of normal RBC with the calcium ionophore A23187 (6,24,25) and suspended in solutions containing dextran to mimic the impact of nonadsorbing macromolecules. Dextran is a neutral polyglucose that has been shown to be depleted from the RBC surface (26,27) and that is frequently used for in vitro hemorheological studies (28); adhesion efficiency was quantified with a flow adhesion assay (29).…”

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confidence: 99%

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Specific Binding of Red Blood Cells to Endothelial Cells Is Regulated by Nonadsorbing Macromolecules

Yang

Koo

Lin

et al. 2010

Journal of Biological Chemistry

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Abnormal adhesion of red blood cells to the endothelium has been linked to the pathophysiology of several diseases associated with vascular disorders. Various biochemical changes, including phosphatidylserine exposure on the outer membrane of red blood cells as well as plasma protein levels, have been identified as being likely to play a key role, but the detailed interplay between plasma factors and cellular factors remains unknown. It has been proposed that the adhesionpromoting effect of plasma proteins originates from ligand interaction, but evidence substantiating this assumption is often missing. In this work, we identified an alternative pathway by demonstrating that nonadsorbing macromolecules can also have a marked impact on the adhesion efficiency of red blood cells with enhanced phosphatidylserine exposure to endothelial cells. It is concluded that this adhesion-promoting effect originates from macromolecular depletion interaction and thereby presents an alternative mechanism by which plasma proteins could regulate cell-cell interactions. These findings should thus be of potential value for a detailed understanding of the pathophysiology of diseases associated with vascular complications and might be applicable to a wide range of cellcell interactions in plasma or plasma-like media. The adhesion of red blood cells (RBC)2 to endothelial cells (EC) is usually insignificant. However, increased RBC adhesion to endothelial cells has been observed in various clinical states such as sickle cell disease, ␤-thalassemia, and diabetes mellitus, and the degree of RBC-EC adhesiveness has been linked to the vascular complications associated with these diseases (1-5). There is now general agreement that various cell surface alterations control the increased RBC adhesiveness in such disease states. For example, an enhanced phosphatidylserine (PS) exposure on the outer leaflet of the RBC membrane has been linked to abnormal RBC-EC adhesion in sickle cell disease, hereditary hydrocytosis, and chronic uremia (6 -8). Usually this anionic phospholipid is located exclusively on the inner leaflet of the RBC membrane but is translocated to the outer leaflet in hemoglobinopathies and oxidative stress states (9). The role of PS in adhesion has not been fully understood, but RBC with enhanced PS exposure have been identified to establish specific interactions with EC or the endothelial matrix via several receptors including thrombospondin, ␣ V ␤ 3 , CD36, and PS receptor (6, 10, 11).Moreover, several plasma factors have been identified to be involved in abnormal RBC adhesion to EC. For example, fibrinogen enhances the adhesion of pathological RBC to EC (12, 13), which is consistent with the observation that the onset of vaso-occlusive crisis in sickle cell disease is always accompanied by a temporally elevated level of this acute phase protein (12,14). However, the underlying mechanisms behind the increased adhesion efficiency in the presence of this acute phase protein remain obscure. It has been suggested that fibrinogen acts...

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“…Interaction of phosphatidylserine in liposomal membranes with ECs has indeed been described, 41 and the adhesion of human erythrocytes to vascular endothelium has been reported to be dramatically increased by phosphatidylserine present on the erythrocyte surface. 42 It is, therefore, not unlikely that a similar mechanism contributes to the selective transduction of ECs by RGD ± AVPs which contain phosphatidylserine as a major constituent. This hypothesis will be explored in more detail in future experiments.…”

Section: Cell Type Selectivity Of Transductionmentioning

confidence: 99%

Highly efficient transduction of endothelial cells by targeted artificial virus-like particles

et al. 2001

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Targeting the tumor vasculature by gene therapy is a potentially powerful approach, but suitable vectors have not yet been described. We have designed a new type of liposomal vector, based on the composition of anionic retroviral envelopes, that is serum -resistant and nontoxic. These artificial virus -like envelopes ( AVEs ) were endowed with a cyclic RGD -containing peptide as a targeting device for the a v û 3 -integrin on tumor endothelial cells ( ECs ) . The packaging of plasmid DNA complexed with low -molecularweight, nonlinear polyethyleneimine into these AVEs yielded artificial virus -like particles ( AVPs ) that transduced ECs with efficiencies of up to 99%. In contrast, transduction of a variety of other cell types by these RGD ± AVPs was comparably inefficient under the same experimental conditions. This EC selectivity was mediated, in part, but not exclusively, by the RGD ligand, as suggested by the reduced, but still relatively high, transduction efficiency seen with AVPs lacking RGD. The interaction of anionic lipids of the AVPs with ECs may therefore contribute to the observed selective and highly efficient transduction of this cell type. These findings suggest that the targeted AVE technology is a useful approach to create highly efficient nonviral vectors.

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Phosphatidylserine‐related adhesion of human erythrocytes to vascular endothelium

Cited by 289 publications

References 12 publications

Hemin-induced suicidal erythrocyte death

Hemin-induced suicidal erythrocyte death

Specific Binding of Red Blood Cells to Endothelial Cells Is Regulated by Nonadsorbing Macromolecules

Highly efficient transduction of endothelial cells by targeted artificial virus-like particles

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