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

التفاصيل البيبلوغرافية
العنوان: HDL-associated paraoxonase-1 can redistribute to cell membranes and influence sensitivity to oxidative stress
المؤلفون: Richard W. James, Marie-Luce Bochaton-Piallat, Sara Deakin, Silvana Bioletto
المصدر: Free Radical Biology and Medicine, Vol. 50, No 1 (2011) pp. 102-9
Free radical biology & medicine
سنة النشر: 2009
مصطلحات موضوعية: 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
الوصف: 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.
تدمد: 1873-4596
0891-5849
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6643d07be7160be0680b8d6c0a77f79e
https://pubmed.ncbi.nlm.nih.gov/20850524
حقوق: OPEN
رقم الأكسشن: edsair.doi.dedup.....6643d07be7160be0680b8d6c0a77f79e
قاعدة البيانات: OpenAIRE