HDL-associated paraoxonase-1 can redistribute to cell membranes and influence sensitivity to oxidative stress

Autor: Richard W. James, Marie-Luce Bochaton-Piallat, Sara Deakin, Silvana Bioletto
Rok vydání: 2009
Předmět:
Cytoprotection/physiology
Very low-density lipoprotein
Aryldialkylphosphatase/metabolism/physiology
Oxidative Stress/physiology
CHO Cells
ddc:616.07
030204 cardiovascular system & hematology
Biology
medicine.disease_cause
Cyclodextrins/metabolism
Biochemistry
Protein Transport/physiology
03 medical and health sciences
0302 clinical medicine
Cricetulus
Physiology (medical)
Cricetinae
medicine
Animals
Humans
Secretion
Tissue Distribution
Scavenger Receptors
Class B/metabolism
Cells
Cultured
030304 developmental biology
ddc:616
0303 health sciences
Cyclodextrins
Aryldialkylphosphatase
Cell Membrane/metabolism
Chinese hamster ovary cell
Cell Membrane
Paraoxonase
Scavenger Receptors
Class B
PON1
Oxidative Stress
Protein Transport
Membrane
Cytoprotection
Lipoproteins
HDL/metabolism
biology.protein
Lipoproteins
HDL
Oxidative stress
Lipoprotein
Zdroj: Free Radical Biology and Medicine, Vol. 50, No 1 (2011) pp. 102-9
Free radical biology & medicine
ISSN: 1873-4596
0891-5849
Popis: Paraoxonase-1 (PON1) is a high-density lipoprotein (HDL)-associated serum enzyme thought to make a major contribution to the antioxidant capacity of the lipoprotein. In previous studies, we proposed that HDL promoted PON1 secretion by transfer of the enzyme from its plasma membrane location to HDL transiently anchored to the hepatocyte. This study examined whether PON1 can be transferred into cell membranes and retain its enzymatic activities and functions. Using Chinese hamster ovary and human endothelial cells, we found that recombinant PON1 as well as PON1 associated with purified human HDL was freely exchanged between the external medium and the cell membranes. Transferred PON1 was located in the external face of the plasma membrane of the cells in an enzymatically active form. The transfer of PON1 led to a gain of function by the target cells, as revealed by significantly reduced susceptibility to oxidative stress and significantly increased ability to neutralize the bacterial virulence agent 3-oxo-C(12)-homoserine lactone. The data demonstrate that PON1 is not a fixed component of HDL and suggest that the enzyme could also exert its protective functions outside the lipoprotein environment. The observations may be of relevance to tissues exposed to oxidative stress and/or bacterial infection.
Databáze: OpenAIRE
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