Erythrocytes as a preferential target of oxidative stress in blood

Fujii, Junichi; Homma, Takujiro; Kobayashi, Sho; Warang, Prashant; Madkaikar, Manisha; Mukherjee, Malay B.

doi:10.1080/10715762.2021.1873318

Cited by 36 publications

(35 citation statements)

References 175 publications

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“…It appears that the storage levels of "protect, repair or destroy" components are not neutral to post-storage proteasome activities; a finding that may be relevant to transfusion outcomes. The interesting change in the correlation sign observed between the storage levels of oxidative stress and post-mixing proteasome activity in early versus late storage further supports-and expands to a post-storage environmentthe hypothesis that proteasome machinery is both effective against [31] and affected by [32] the oxidative burden [8]. This interplay between redox equilibrium and protein quality control was anticipated.…”

Section: Stored Rbc Features In Recipient Plasma and Temperaturementioning

confidence: 58%

The Post-Storage Performance of RBCs from Beta-Thalassemia Trait Donors Is Related to Their Storability Profile

Anastasiadi

Paronis

Arvaniti

et al. 2021

IJMS

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Blood donors with beta-thalassemia traits (βThal+) have proven to be good “storers”, since their stored RBCs are resistant to lysis and resilient against oxidative/proteotoxic stress. To examine the performance of these RBCs post-storage, stored βThal+ and control RBCs were reconstituted in plasma donated from transfusion-dependent beta-thalassemic patients and healthy controls, and incubated for 24 h at body temperature. Several physiological parameters, including hemolysis, were evaluated. Moreover, labeled fresh/stored RBCs from the two groups were transfused in mice to assess 24 h recovery. All hemolysis metrics were better in the group of heterozygotes and distinguished them against controls in the plasma environment. The reconstituted βThal+ samples also presented higher proteasome activity and fewer procoagulant extracellular vesicles. Transfusion to mice demonstrated that βThal+ RBCs present a marginal trend for higher recovery, regardless of the recipient’s immune background and the RBC storage age. According to correlation analysis, several of these advantageous post-storage characteristics are related to storage phenotypes, like the cytoskeleton composition, low cellular fragility, and enhanced membrane proteostasis that characterize stored βThal+ RBCs. Overall, it seems that the intrinsic physiology of βThal+ RBCs benefits them in conditions mimicking a recipient environment, and in the circulation of animal models; findings that warrant validation in clinical trials.

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Section: Stored Rbc Features In Recipient Plasma and Temperaturementioning

confidence: 58%

The Post-Storage Performance of RBCs from Beta-Thalassemia Trait Donors Is Related to Their Storability Profile

Anastasiadi

Paronis

Arvaniti

et al. 2021

IJMS

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“…The repeatable correlation between the proteasome activities and the intracellular ROS further supports the responsiveness of the 20S proteasome toward oxidative-driven defects [ 29 ]. It is tempting to hypothesize that ROS levels positively correlate with proteasome activity until the middle of the storage period because the proteasome is still capable of counteracting the accelerated storage-driven oxidative stress.…”

Section: Discussionmentioning

confidence: 78%

“…The same trend for high proteasome activity has been reported in G6PD-deficient stored RBCs [ 18 ], which is another distinct genetic group characterized by sustained levels of oxidative stress. Consequently, the elevated proteasome activity in the membrane could represent an adaptation of RBCs to redox imbalance in vivo [ 29 ], which might be recalled by them to better preserve the proteome stability and overall functionality when exposed to additional oxidative challenges, including those imposed by the storage-induced accelerated aging. Although the specific activity of the proteasome in the membrane of RBCs has not been studied so far, high proteasome activities have been reported in the ROS-enriched cytosol of RBCs from sickle cell disease patients [ 34 ], which further increased following treatment with hydroxycarbamide [ 35 ].…”

Section: Discussionmentioning

confidence: 99%

Red Blood Cell Proteasome in Beta-Thalassemia Trait: Topology of Activity and Networking in Blood Bank Conditions

et al. 2021

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Proteasomes are multi-catalytic complexes with important roles in protein control. Their activity in stored red blood cells (RBCs) is affected by both storage time and the donor’s characteristics. However, apart from their abundancy in the membrane proteome, not much is known about their topology, activity, and networking during the storage of RBCs from beta-thalassemia trait donors (βThal+). For this purpose, RBC units from fourteen βThal+ donors were fractionated and studied for proteasome activity distribution and interactome through fluorometric and correlation analyses against units of sex- and aged-matched controls. In all the samples examined, we observed a time-dependent translocation and/or activation of the proteasome in the membrane and a tight connection of activity with the oxidative burden of cells. Proteasomes were more active in the βThal+ membranes and supernatants, while the early storage networking of 20S core particles and activities showed a higher degree of connectivity with chaperones, calpains, and peroxiredoxins, which were nonetheless present in all interactomes. Moreover, the βThal+ interactomes were specially enriched in kinases, metabolic enzymes, and proteins differentially expressed in βThal+ membrane, including arginase-1, piezo-1, and phospholipid scramblase. Overall, it seems that βThal+ erythrocytes maintain a considerable “proteo-vigilance” during storage, which is closely connected to their distinct antioxidant dynamics and membrane protein profile.

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“…The toxin stimulates lipid peroxidation system leading to the production of lipid peroxides that hemolysate red blood cells [17]. Among the main pathological after effects of free radical-induced tissue lipid peroxidation are greater cellular distortion, decreased erythrocyte survival by augmented auto-necrosis, and augmented lipid fluidity that initiates a chain of inflammatory reactions that cause endothelial dysfunction [18,19]. Low levels of hemoglobin which is the main intracellular protein for RBCs is resulted from losing blood or rapid destruction of blood cells, leading to anemia [20].…”

Section: Resultsmentioning

confidence: 99%