Erythrocyte deformability — A partner of the inflammatory response

Silva-Herdade, Ana Santos; Andolina, Giulia; Faggio, Caterina; Calado, Ângelo; Saldanha, Carlota

doi:10.1016/j.mvr.2016.04.011

Cited by 50 publications

(30 citation statements)

References 24 publications

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“…Thus, emodin-induced cell membrane scrambling was in part, but not exclusively triggered by entry of extracellular Ca 2+ . Erythrocyte cell membrane scrambling is further stimulated by oxidative stress [118]. Reactive oxygen species (ROS) was thus quantified utilizing 2′,7′-dichlorodihydrofluorescein diacetate (DCFDA).…”

Section: Resultsmentioning

confidence: 99%

Triggering of Erythrocyte Cell Membrane Scrambling by Emodin

Mischitelli

Jèmaà²,

Almasry³

et al. 2016

Cell Physiol Biochem

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Background/Aims: The natural anthraquinone derivative emodin (1,3,8-trihydroxy-6-methylanthraquinone) is a component of several Chinese medicinal herbal preparations utilized for more than 2000 years. The substance has been used against diverse disorders including malignancy, inflammation and microbial infection. The substance is effective in part by triggering suicidal death or apoptosis. Similar to apoptosis of nucleated cells erythrocytes may enter suicidal erythrocyte death or eryptosis, characterized by cell shrinkage and cell membrane scrambling with phosphatidylserine translocation to the erythrocyte surface. Signaling involved in the triggering of eryptosis include increase of cytosolic Ca²⁺ activity ([Ca²⁺]_i), oxidative stress and ceramide. The present study aimed to test, whether emodin induces eryptosis and, if so, to elucidate underlying cellular mechanisms. Methods: Phosphatidylserine abundance at the cell surface was estimated from annexin-V-binding, cell volume from forward scatter, [Ca²⁺]_i from Fluo3-fluorescence, ROS formation from DCFDA dependent fluorescence, and ceramide abundance utilizing specific antibodies. Results: Exposure of human erythrocytes for 48 hours to emodin (≥ 10 µM) significantly increased the percentage of annexin-V-binding cells, and at higher concentrations (≥ 50 µM) significantly increased forward scatter. Emodin significantly increased Fluo3-fluorescence (≥ 10 µM), DCFDA fluorescence (75 µM) and ceramide abundance (75 µM). The effect of emodin on annexin-V-binding was significantly blunted but not abolished by removal of extracellular Ca²⁺. Conclusions: Emodin triggers phospholipid scrambling of the erythrocyte cell membrane, an effect at least in part due to stimulation of Ca²⁺ entry and paralleled by oxidative stress and ceramide appearance at the erythroctye surface.

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Section: Resultsmentioning

confidence: 99%

Triggering of Erythrocyte Cell Membrane Scrambling by Emodin

Mischitelli

Jèmaà²,

Almasry³

et al. 2016

Cell Physiol Biochem

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“…The abnormality of WBV can increase the resistance of blood fluidity and slow down the blood flow velocity, thus leading to the cardiovascular risk. Hct is the most important factor for WBV [29–32]. In Table 2, compared with model group, BSP-1b, BSP-2 and BSP-3 could significantly decrease WBV at all shear rates (0.001 < p < 0.05, p < 0.001), as well as BSP-1b, BSP-2 and BSP-3 could significantly decrease Hct ( p < 0.001).…”

Section: Resultsmentioning

confidence: 99%

Antithrombotic mechanism of polysaccharides in Blackberry (Rubus spp.) seeds

Wang

Lian

et al. 2017

Food & Nutrition Research

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The blackberry seed was typically removed as a byproduct and waste from blackberry fruits for juices. Developing value-added utilization of berry seeds will significantly expand the market for berry products as well as improve benefit to berry producers. However, the research on blackberry seed is limited. The objective of this paper was to research antithrombotic mechanism of polysaccharides in blackberry seeds. Polysaccharides in blackberry seeds were extracted, purified and identified by high-performance gel permeation chromatography (HPSEC), gas chromatography (GC), fourier transform infrared (FT-IR) spectrometer and nuclear magnetic resonance spectra (NMR). Anticoagulant activities were evaluated in vivo by measuring activated partial thromboplastin time (APTT), thrombin time (TT), prothrombin time (PT), fibrinogen (FIB) and plasma recalcification time (RRT). Four polysaccharides named BSP-1a, BSP-1b, BSP-2 and BSP-3 were isolated from Blackberry (Rubus spp.) seeds. The results indicated that BSP-1b, BSP-2 and BSP-3 exhibited the anticoagulant activity. Therefore, the anti-thrombosis effects of BSP-1b, BSP-2 and BSP-3 were investigated in vivo by 6-Keto-PGF1α, thromboxane B2 (TXB2), endothelial nitric oxide synthase (eNOS), endothelin-1 (ET-1), whole blood viscosity (WBV), plasma viscosity (PV), hematocrit (Hct), erythrocyte sedimentation rate (ESR), APTT, TT, PT and FIB. The results suggested that BSP-1b, BSP-2 and BSP-3 had the inhibition effect on thrombus formation, and the antithrombotic effects were associated with the regulation of vascular endothelium active substance, activating blood flow and anticoagulation effect.

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“…Adherance of phosphatidylserine exposing erythrocytes to the vascular wall [92,93] may further stimulate blood clotting and trigger thrombosis [94][95][96], thus compromising microcirculation [76,94,[97][98][99][100].…”

Section: Discussionmentioning

confidence: 99%

Stimulation of Eryptosis by Caspofungin

Peter

Bissinger²,

Läng³

2016

Cell Physiol Biochem

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Background/Aims: The echinocandin antifungal agent caspofungin has been shown to trigger apoptosis of fungal cells. Beyond that, caspofungin is toxic for host mitochondria. Even though lacking mitochondria, erythrocytes may enter apoptosis-like suicidal erythrocyte death or eryptosis, characterized by cell shrinkage and cell membrane scrambling with phosphatidylserine translocation to the erythrocyte surface. Signaling involved in triggering of eryptosis include increase of cytosolic Ca²⁺ activity ([Ca²⁺]_i), oxidative stress, ceramide, caspase activation and/or activation of p38 kinase, protein kinase C, and casein kinase. The present study explored, whether caspofungin induces eryptosis and, if so, to shed some light on the cellular mechanisms involved. Methods: Flow cytometry was employed to determine phosphatidylserine exposure at the cell surface from annexin-V-binding, cell volume from forward scatter, [Ca²⁺]_i from Fluo3-fluorescence, ROS formation from DCFDA dependent fluorescence, and ceramide abundance utilizing specific antibodies. Hemolysis was quantified from hemoglobin concentration in the supernatant. Results: A 48 hours exposure of human erythrocytes to caspofungin (≥ 30 µg/ml) significantly increased the percentage of annexin-V-binding cells, significantly decreased forward scatter, significantly enhanced hemolysis, but did not significantly increase Fluo3-fluorescence, DCFDA fluorescence or ceramide abundance. The effect of caspofungin on annexin-V-binding was not significantly blunted by removal of extracellular Ca²⁺, by inhibition of caspases with pancaspase inhibitor zVAD (10 µM), or by addition of the antioxidant N-acetyl-cysteine (1 mM), p38 kinase inhibitor SB203580 (2 µM) or protein kinase C inhibitor staurosporine (1 µM). The effect of caspofungin on annexin-V-binding was, however, significantly blunted in the presence of casein kinase inhibitor D4476 (10 µM). Conclusions: Caspofungin triggers cell shrinkage and phospholipid scrambling of the erythrocyte cell membrane, an effect possibly involving activation of casein kinase.

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Erythrocyte deformability — A partner of the inflammatory response

Cited by 50 publications

References 24 publications

Triggering of Erythrocyte Cell Membrane Scrambling by Emodin

Triggering of Erythrocyte Cell Membrane Scrambling by Emodin

Antithrombotic mechanism of polysaccharides in Blackberry (Rubus spp.) seeds

Stimulation of Eryptosis by Caspofungin

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