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Phospholipid signaling in apoptosis: peroxidation and externalization of phosphatidylserine.

Authors
Tyurina-YY; Shvedova-AA; Kawai-K; Tyurin-VA; Kommineni-C; Quinn-PJ; Schor-NF; Fabisiak-JP; Kagan-VE
Source
Toxicology 2000 Aug; 148(2-3):93-101
NIOSHTIC No.
20020837
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.
Keywords
Phospholipids; Peroxides; Oxidation; Tissue-culture; Oxides; Antioxidants; Antioxidation
Contact
Department of Environmental and Occupational Health, University of Pittsburgh, 260 Kappa Drive, RIDC Park, Pittsburgh, PA 15238, USA
CODEN
TXCYAC
Publication Date
20000807
Document Type
Journal Article
Email Address
kagan@pitt.edu
Fiscal Year
2000
NTIS Accession No.
NTIS Price
Issue of Publication
2-3
ISSN
0300-483X
NIOSH Division
HELD
Source Name
Toxicology
State
WV; PA
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