Spectral imaging of red blood cells in experimental anemia of Cyprinus carpio

Rothmann, Chana; Levinshal, T.; Timan, Bracha; Avtalion, Ramy R.; Malik, Zvi

doi:10.1016/s1095-6433(99)00157-9

Cited by 30 publications

(23 citation statements)

References 33 publications

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“…The cytochrome c release and ROS generation may be related to mitochondrion in fish erythrocytes. Rothmann et al reported that fish erythrocytes contain mitochondrial organelles [34]. Studies indicated that mitochondria is the source of cytochrome c release and ROS generation in mammal cells [79].…”

Section: • Oh-induced Apoptosis In Fish Erythrocytesmentioning

confidence: 99%

“…Moreover, as the mammal erythrocytes, fish erythrocytes contain the high concentrations of Hb that transports O 2 and CO 2 for respiration and continuously produce ROS [24,30]. Fish erythrocytes retain nucleus, mitochondria and other organelles, which are most like the mammal nucleated cells in structure [32,34]. In our experience, fish erythrocytes are easy to harvest and culture in vitro [30].…”

Section: • Oh-induced Apoptosis In Fish Erythrocytesmentioning

confidence: 99%

“…ROS can induce the influx of Ca 2 þ that activates scramblase with subsequent phosphatidylserine (PS) externalization at the cell surface (a biomarker of apoptosis) in mammal erythrocytes [33]. Fish erythrocytes retain nucleus, mitochondria and other organelles, which are most like the mammal nucleated cells in structure [32,34]. Studies have indicated that oxidative stress can initiate the aggregation of death receptors (e.g.…”

Section: Introductionmentioning

confidence: 99%

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The metabolites of glutamine prevent hydroxyl radical-induced apoptosis through inhibiting mitochondria and calcium ion involved pathways in fish erythrocytes

Jiang

Liu

et al. 2016

Free Radical Biology and Medicine

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a b s t r a c tThe present study explored the apoptosis pathways in hydroxyl radicals ( • OH)-induced carp erythrocytes. Carp erythrocytes were treated with the caspase inhibitors in physiological carp saline (PCS) or Ca 2 þ -free PCS in the presence of 40 μM FeSO 4 /20 μM H 2 O 2 . The results showed that the generation of reactive oxygen species (ROS), the release of cytochrome c and DNA fragmentation were caspase-dependent, and Ca 2 þ was involved in calpain activation and phosphatidylserine (PS) exposure in • OH-induced carp erythrocytes. Moreover, the results suggested that caspases were involved in PS exposure, and Ca 2 þ was involved in DNA fragmentation in • OH-induced fish erythrocytes. These results demonstrated that there might be two apoptosis pathways in fish erythrocytes, one is the caspase and cytochrome c-dependent apoptosis that is similar to that in mammal nucleated cells, the other is the Ca 2 þ -involved apoptosis that was similar to that in mammal non-nucleated erythrocytes. So, fish erythrocytes may be used as a model for studying oxidative stress and apoptosis in mammal cells. Furthermore, the present study investigated the effects of glutamine (Gln)'s metabolites [alanine (Ala), citrulline (Cit), proline (Pro) and their combination (Ala 10 Pro 4 Cit 1 )] on the pathways of apoptosis in fish erythrocytes. The results displayed that Ala, Cit, Pro and Ala 10 Pro 4 Cit 1 effectively suppressed ROS generation, cytochrome c release, activation of caspase-3, caspase-8 and caspase-9 at the physiological concentrations, prevented Ca 2 þ influx, calpain activation, PS exposure, DNA fragmentation and the degradation of the cytoskeleton and oxidation of membrane and hemoglobin (Hb) and increased activity of anti-hydroxyl radical (AHR) in • OH-induced carp erythrocytes. Ala 10 Pro 4 Cit 1 produced a synergistic effect of inhibited oxidative stress and apoptosis in fish erythrocytes. These results demonstrated that Ala, Cit, Pro and their combination can protect mammal erythrocytes and nucleated cells against oxidative stress and apoptosis. The studies supported the use of Gln, Ala, Cit and Pro as oxidative stress and apoptosis inhibitors in mammal cells and the hypothesis that the inhibited effects of Gln on oxidative stress and apoptosis are at least partly dependent on that of its metabolites in mammalian.

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Section: • Oh-induced Apoptosis In Fish Erythrocytesmentioning

confidence: 99%

Section: • Oh-induced Apoptosis In Fish Erythrocytesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The metabolites of glutamine prevent hydroxyl radical-induced apoptosis through inhibiting mitochondria and calcium ion involved pathways in fish erythrocytes

Jiang

Liu

et al. 2016

Free Radical Biology and Medicine

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“…Scanning Electron MicroscopyCells were washed with phosphate-buffered saline, mounted on glass coverslips, and subsequently fixed in glutaraldehyde/paraformaldehyde solution, 2% OsO 4 , 2% tannic acid/guanidine hydrochloride (35). After dehydration, the cells were air-dried and gold-coated using a Polaron sputter coater (Fisons).…”

Section: In Vivo Labeling and Immunoprecipitation-procyclicmentioning

confidence: 99%

Role of Protein Translocation Pathways across the Endoplasmic Reticulum in Trypanosoma brucei

Goldshmidt

Sheiner

Bütikofer

et al. 2008

Journal of Biological Chemistry

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The translocation of secretory and membrane proteins across the endoplasmic reticulum (ER) membrane is mediated by co-translational (via the signal recognition particle (SRP)) and post-translational mechanisms. In this study, we investigated the relative contributions of these two pathways in trypanosomes. A homologue of SEC71, which functions in the post-translocation chaperone pathway in yeast, was identified and silenced by RNA interference. This factor is essential for parasite viability. In SEC71-silenced cells, signal peptide (SP)-containing proteins traversed the ER, but several were mislocalized, whereas polytopic membrane protein biogenesis was unaffected. Surprisingly trypanosomes can interchangeably utilize two of the pathways to translocate SPcontaining proteins except for glycosylphosphatidylinositol-anchored proteins, whose level was reduced in SEC71-silenced cells but not in cells depleted for SRP68, an SRP-binding protein. Entry of SP-containing proteins to the ER was significantly blocked only in cells co-silenced for the two translocation pathways (SEC71 and SRP68). SEC63, a factor essential for both translocation pathways in yeast, was identified and silenced by RNA interference. SEC63 silencing affected entry to the ER of both SP-containing proteins and polytopic membrane proteins, suggesting that, as in yeast, this factor is essential for both translocation pathways in vivo. This study suggests that, unlike bacteria or other eukaryotes, trypanosomes are generally promiscuous in their choice of mechanism for translocating SPcontaining proteins to the ER, although the SRP-independent pathway is favored for glycosylphosphatidylinositol-anchored proteins, which are the most abundant surface proteins in these parasites.

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“…However, the pathway of apoptosis still remains unknown in fish erythrocytes. According to the developmental stages, erythroid lineage includes early erythroblasts, intermediate cells and matured cells in the peripheral blood of fish (Rothmann et al 2000). The early erythroblasts are poorly differentiated cells and contain various organelles.…”

Section: Introductionmentioning

confidence: 99%

Ca2+ and caspases are involved in hydroxyl radical-induced apoptosis in erythrocytes of Jian carp (Cyprinus carpio var. Jian)

Feng

Jiang

et al. 2015

Fish Physiol Biochem

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Spectral imaging of red blood cells in experimental anemia of Cyprinus carpio

Cited by 30 publications

References 33 publications

The metabolites of glutamine prevent hydroxyl radical-induced apoptosis through inhibiting mitochondria and calcium ion involved pathways in fish erythrocytes

The metabolites of glutamine prevent hydroxyl radical-induced apoptosis through inhibiting mitochondria and calcium ion involved pathways in fish erythrocytes

Role of Protein Translocation Pathways across the Endoplasmic Reticulum in Trypanosoma brucei

Ca2+ and caspases are involved in hydroxyl radical-induced apoptosis in erythrocytes of Jian carp (Cyprinus carpio var. Jian)

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