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Phospholipid signaling in apoptosis: peroxidation and externalization of phosphatidylserine
Phospholipid signaling in apoptosis: peroxidation and externalization of phosphatidylserine
- Source :
- Toxicology. 148(2-3)
- Publication Year :
- 2000
-
Abstract
- The role of phospholipids in apoptosis signaling and the relationship between oxidation of phosphatidylserine and its redistribution in the plasma membrane were studied. A novel method for detection of site-specific phospholipid peroxidation based on the use of cis-parinaric acid as a reporter molecule metabolically integrated into membrane phospholipids in living cells was employed. When several tissue culture cell lines and different exogenous oxidants were used, the relationship between the oxidation of phosphatidylserine and apoptosis has been revealed. The plasma membrane was the preferred site of phosphatidylserine oxidation in cells. It was shown that selective oxidation of phosphatidylserine precedes its translocation from the inside to the outside surface of the plasma membrane during apoptosis. A model is proposed in which cytochrome c released from mitochondria by oxidative stress binds to phosphatidylserine located at the cytoplasmic surface of the plasma membrane and induces its oxidation. Interaction of peroxidized phosphatidylserine with aminophospholipid translocase causes inhibition of the enzyme relevant to phosphatidylserine externalization.
- Subjects :
- Keratinocytes
Programmed cell death
Phospholipid
Apoptosis
HL-60 Cells
Phosphatidylserines
Biology
Mitochondrion
Toxicology
PC12 Cells
chemistry.chemical_compound
Nitriles
Translocase
Animals
Humans
Phospholipids
Phenol
Cytochrome c
Biological Transport
Phosphatidylserine
Cell biology
Rats
chemistry
Gene Expression Regulation
Proto-Oncogene Proteins c-bcl-2
biology.protein
Lipid Peroxidation
Signal transduction
Azo Compounds
Signal Transduction
Subjects
Details
- ISSN :
- 0300483X
- Volume :
- 148
- Issue :
- 2-3
- Database :
- OpenAIRE
- Journal :
- Toxicology
- Accession number :
- edsair.doi.dedup.....ba1d13a99007987a063c55fcd9c5757d