a(CHEBI:"phosphatidyl-L-serine")
The Zn2þ (20 mM)-induced expression of PS on erythrocytes, which was inhibited by TPEN, was not observed by other divalent cations, including Mg2þ and Ca2þ (Fig. 2A). PubMed:29544683
The Zn2þ (20 mM)-induced expression of PS on erythrocytes, which was inhibited by TPEN, was not observed by other divalent cations, including Mg2þ and Ca2þ (Fig. 2A). PubMed:29544683
These RBC microparticles can initiate and propogate thrombin generation (Rubin et al, 2013). PubMed:25307023
Elevated cholesterol, oxy-cholesterol, lyso-phospholipid and decreased phosphatidylserine were found in atheromatous lipids compared to controls (supplemental Table II). PubMed:20378845
Stored RBCs undergo a complex structural and metabolic impairment that includes leakage of hemoglobin from the cells and hemolysis, reduced energy and NO production, formation of toxic products, such as lysophospholipids and free iron, phosphatidylserine exposure and shedding MPs [59]. PubMed:28458720
Under conditions of apoptosis or RBC damage, such as high shear rates, inflammation, or oxidative stress, RBCs can lose membrane asymmetry and expose phosphatidylserine [43]. PubMed:28458720
Phosphatidylserine externalization and shedding are mediated by increased cellular Ca-flux and play an important role in natural RBC senescence [44]. PubMed:28458720
Phosphatidylserine externalization and shedding are mediated by increased cellular Ca-flux and play an important role in natural RBC senescence [44]. PubMed:28458720
An increase in RBC phosphatidylserine exposure in -thalassemia patients has been shown to be connected with eryptosis, the suicidal death of RBCs [49]. PubMed:28458720
Eryptosis is the apoptotic-like suicidal process of erythrocytes, and is characterized by cell shrinkage and phosphatidylserine (PS) expression on the outer membrane. PubMed:29544683
HRG and HSA both inhibited PS expression when their concentrations were increased to 10 and 100 mg/mL (Fig. 2B). PubMed:29544683
To determine the role of PS in the Zn2þ-induced aggregation of erythrocytes, we used Annexin V to block PS expression on the erythrocyte membrane. PubMed:29544683
HRG and HSA both inhibited PS expression when their concentrations were increased to 10 and 100 mg/mL (Fig. 2B). PubMed:29544683
Surprisingly, HRG at high concentration (100 mg/mL) significantly decreased PS expression on erythrocytes. PubMed:29544683
Although a significant difference in PS expressionwas not observed among the CLP groups treated with PBS, HSA or HRG, incubation of erythrocytes for 4 h enabled the observation of beneficial effects of HRG on PS expression on erythrocytes (Fig. 5B). PubMed:29544683
The abnormal phospholipid membrane asymmetry present in the RBCs of b-thalassaemia and SCD patients, with resultant phosphatidylserine exposure, appears to play a significant role in the aetiology of the observed hypercoagulable state and in the link between haemolysis and thrombosis (Ataga et al, 2007). PubMed:25307023
Furthermore, phosphatidylserine is actively maintained on the inner leaflet of the bilayer membrane and, when externalized, is a recognition signal for cell clearance or for activation of coagulation (Zwaal & Schroit, 1997). PubMed:25307023
Because of the large numbers of RBCs present in the blood, even a small fraction of RBCs with phosphatidylserine exposure can result in prothrombotic conditions. PubMed:28458720
Elevated cholesterol, oxy-cholesterol, lyso-phospholipid and decreased phosphatidylserine were found in atheromatous lipids compared to controls (supplemental Table II). PubMed:20378845
The abnormal phospholipid membrane asymmetry present in the RBCs of b-thalassaemia and SCD patients, with resultant phosphatidylserine exposure, appears to play a significant role in the aetiology of the observed hypercoagulable state and in the link between haemolysis and thrombosis (Ataga et al, 2007). PubMed:25307023
Phosphatidylserine externalization and shedding are mediated by increased cellular Ca-flux and play an important role in natural RBC senescence [44]. PubMed:28458720
The abnormal phospholipid membrane asymmetry present in the RBCs of b-thalassaemia and SCD patients, with resultant phosphatidylserine exposure, appears to play a significant role in the aetiology of the observed hypercoagulable state and in the link between haemolysis and thrombosis (Ataga et al, 2007). PubMed:25307023
The abnormal phospholipid membrane asymmetry present in the RBCs of b-thalassaemia and SCD patients, with resultant phosphatidylserine exposure, appears to play a significant role in the aetiology of the observed hypercoagulable state and in the link between haemolysis and thrombosis (Ataga et al, 2007). PubMed:25307023
Because of the large numbers of RBCs present in the blood, even a small fraction of RBCs with phosphatidylserine exposure can result in prothrombotic conditions. PubMed:28458720
Furthermore, phosphatidylserine is actively maintained on the inner leaflet of the bilayer membrane and, when externalized, is a recognition signal for cell clearance or for activation of coagulation (Zwaal & Schroit, 1997). PubMed:25307023
These RBC microparticles can initiate and propogate thrombin generation (Rubin et al, 2013). PubMed:25307023
In addition to cell-free Hb, membrane structural modification, externalization of phosphatidylserine,21 decreased cell membrane deformability,22,23 and increased endothelial adherence24 could alter vascular NO homeostasis. PubMed:27308950
Under conditions of apoptosis or RBC damage, such as high shear rates, inflammation, or oxidative stress, RBCs can lose membrane asymmetry and expose phosphatidylserine [43]. PubMed:28458720
An increase in RBC phosphatidylserine exposure in -thalassemia patients has been shown to be connected with eryptosis, the suicidal death of RBCs [49]. PubMed:28458720
Eryptosis is the apoptotic-like suicidal process of erythrocytes, and is characterized by cell shrinkage and phosphatidylserine (PS) expression on the outer membrane. PubMed:29544683
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If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.