Phospholipid rearrangement of apoptotic membrane does not depend on nuclear activity

Renò, Filippo; Burattini, Sabrina; Rossi, Stefano; Luchetti, Francesca; Columbaro, Marta; Santi, Spartaco; Papa, Stefano; Falcieri, Elisabetta

doi:10.1007/s004180050308

Cited by 37 publications

(35 citation statements)

References 31 publications

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“…The increased oxidative stress has been shown to result in the selective phosphatidylserine oxidation that precedes phosphatidylserine externalization in oxidant-induced 2 ). After incubation for 4 or 18 h, the cells were harvested to determine the binding of annexin V to the externalized PS on the cell surface (55,60). Results are the mean Ϯ S.E.…”

Section: Discussionmentioning

confidence: 99%

Role of Reduced Glutathione Efflux in Apoptosis of Immortalized Human Keratinocytes Induced by UVA

Huang

Ramirez

et al. 2003

Journal of Biological Chemistry

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We have investigated the role played by GSH efflux in apoptosis of human HaCaT keratinocytes induced by UVA irradiation. UVA irradiation of HaCaT cells caused a rapid rise in GSH efflux across the intact cell membrane, followed by an increase in apoptosis. GSH efflux was stimulated by glucose and was reduced by the addition of exogenous GSH and intracellular GSH depletion by buthionine sulfoximine, suggesting that GSH transport is active and is influenced by the GSH concentration gradient across the cell membrane. Verapamil and cyclosporin A, blockers of the multidrug resistanceassociated protein, decreased UVA-induced GSH efflux. GSH efflux occurred within 2 h of UVA irradiation, suggesting that the stimulation of GSH efflux is due to an increase in the activity of pre-existing multidrug resistance-associated protein transporter carrier. Although inhibition of GSH efflux did not affect caspase activation and DNA fragmentation, it delayed the gradual increase in plasma membrane permeability and reduced phosphatidylserine translocation in HaCaT cells. It is therefore likely that upon UVA irradiation, GSH efflux increased the intracellular oxidative stress without intervention of reactive oxygen species, thus resulting in more phosphatidylserine externalization and membrane rearrangement. These provide targets for macrophage recognition and phagocytosis and thus minimize the potential to invoke inflammation or neoplastic transformation.

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Section: Discussionmentioning

confidence: 99%

Role of Reduced Glutathione Efflux in Apoptosis of Immortalized Human Keratinocytes Induced by UVA

Huang

Ramirez

et al. 2003

Journal of Biological Chemistry

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“…Apoptotic and necrotic cells were quantitatively evaluated by flow cytometry (Martin et al, 1995;Reno et al, 1998). After irradiation, the cells were harvested by trypsinization and collected by centrifugation at 140 g for 6 min at 22°C.…”

Section: Measurement Of Apoptotic and Necrotic Cellsmentioning

confidence: 99%

Phototoxicity and cytotoxicity of fullerol in human lens epithelial cells

Roberts

Wielgus

Boyes

et al. 2008

Toxicology and Applied Pharmacology

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The water-soluble, hydroxylated fullerene [fullerol, nano-C 60 (OH) [22][23][24][25][26] ] has several clinical applications including use as a drug carrier to bypass the blood ocular barriers. We have assessed fullerol's potential ocular toxicity by measuring its cytotoxicity and phototoxicity induced by UVA and visible light in vitro with human lens epithelial cells (HLE B-3). Accumulation of nano-C 60 (OH) [22][23][24][25][26] in the cells was confirmed spectrophotometrically at 405 nm and cell viability estimated using MTS and LDH assays. Fullerol was cytotoxic to HLE B-3 cells maintained in the dark at concentrations higher than 20 µM. Exposure to either UVA or visible light in the presence of >5 µM fullerol induced phototoxic damage. When cells were pretreated with non-toxic antioxidants: 20 µM lutein, 1 mM N-acetyl cysteine, or 1 mM L-ascorbic acid prior to irradiation, only the singlet oxygen quencher lutein significantly protected against fullerol photodamage. Apoptosis was observed in lens cells treated with fullerol whether or not the cells were irradiated, in the order UVA > visible light > dark. Dynamic light scattering (DLS) showed that in the presence of the endogenous lens protein α-crystallin, large aggregates of fullerol were reduced. In conclusion, fullerol is both cytotoxic and phototoxic to human lens epithelial cells. Although the acute toxicity of water soluble nano-C 60 (OH) 22-26 is low, these compounds are retained in the body for long periods, raising concern for their chronic toxic effect. Before fullerols are used to deliver drugs to the eye, they should be tested for photo-and cytotoxicity in vivo.

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“…After commitment of cells to apoptosis, characteristic morphological changes are observed in the execution phase of cell death. These alterations include cytoplasmic condensation and plasma membrane blebbing, cell shrinkage, condensation of chromatin that marginates towards the inner nuclear membrane forming cap-shaped, compact areas, and, ultimately, fragmentation of residual nuclear structures into apoptotic bodies that are phagocytosed by neighboring cells and macrophages [Hale et al, 1996;Vaux and Strasser, 1996;Falcieri et al, 1994;Earnshaw, 1995;Kroemer et al, 1995;Dini et al, 1995;Martelli et al, 1997;Renò et al, 1998]. Most likely, these changes reflect proteolysis of several nuclear and cytoplasmic polypeptides, and DNA degradation by endogenous nucleases into at first large and then finally nucleosomal-size fragments [e.g., Collins et al, 1997].…”

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confidence: 98%

Behavior of nucleolar proteins during the course of apoptosis in camptothecin-treated HL60 cells

Martelli

Robuffo²,

Bortul

et al. 2000

J. Cell. Biochem.

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By means of immunofluorescence and immunoelectron microscopy we have studied the fate of different nucleolar components during the apoptotic process in camptothecin-treated HL60 cells. We have found that RNA polymerase I disappeared while UBF was associated with previously described fibrogranular threaded bodies. In contrast, fibrillarin, C23/nucleolin, and B23/nucleophosmin remained detectable in granular material present amid micronuclei of late apoptotic cells. Double immunolabeling experiments showed colocalization of both C23 and B23 with fibrillarin. Immunoblotting analysis showed that UBF was proteolytically degraded, whereas fibrillarin, C23/nucleolin, and B23/nucleophosmin were not. These results may help explain the presence of anti-nucleolar antibodies seen in various pathological disorders.

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Phospholipid rearrangement of apoptotic membrane does not depend on nuclear activity

Cited by 37 publications

References 31 publications

Role of Reduced Glutathione Efflux in Apoptosis of Immortalized Human Keratinocytes Induced by UVA

Role of Reduced Glutathione Efflux in Apoptosis of Immortalized Human Keratinocytes Induced by UVA

Phototoxicity and cytotoxicity of fullerol in human lens epithelial cells

Behavior of nucleolar proteins during the course of apoptosis in camptothecin-treated HL60 cells

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