HDL Oxidation Compromises its Influence on Paraoxonase-1 Secretion and its Capacity to Modulate Enzyme Activity
| Autor: | Richard James, Xenia Moren, Sara Deakin |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
medicine.medical_specialty
Hypochlorite Enzyme-Linked Immunosorbent Assay medicine.disease_cause chemistry.chemical_compound Cricetinae Internal medicine medicine Animals Humans Cells Cultured Dose-Response Relationship Drug biology Aryldialkylphosphatase Chemistry Cholesterol Cholesterol HDL Paraoxonase nutritional and metabolic diseases Metabolism Atherosclerosis Oxidants Recombinant Proteins Enzyme assay Hypochlorous Acid Rats Endocrinology Biochemistry Myeloperoxidase Hepatocytes biology.protein Female lipids (amino acids peptides and proteins) Cardiology and Cardiovascular Medicine Oxidation-Reduction Oxidative stress |
| Zdroj: | Arteriosclerosis, Thrombosis, and Vascular Biology. 27:1146-1152 |
| ISSN: | 1524-4636 1079-5642 |
| DOI: | 10.1161/atvbaha.107.141747 |
| Popis: | Objective— The purpose of this study was to analyze the consequences of HDL oxidation for paraoxonase-1 metabolism and function. Methods and Results— HDL was oxidized with AAPH, copper ions, and hypochlorite. Secretion studies were performed using human paraoxonase-1–transfected cells lines and primary rat hepatocytes. Stability studies were performed with recombinant paraoxonase. Conditioned medium had significantly reduced paraoxonase-1 when Cu or AAPH-oxidized HDL was the acceptor complex ( P Conclusions— AAPH and copper, but not hypochlorite, oxidation of HDL compromises its ability to promote release of paraoxonase-1 and stabilize enzyme activity. HDL-associated paraoxonase-1 is highly sensitive to hypochlorite. Reducing paraoxonase-1 renders HDL susceptible to oxidation, which may compromise HDL function. It provides a novel example at the HDL level of the detrimental effects of oxidative stress, and underlines the need for further evaluation of the consequences of HDL oxidation. |
| Databáze: | OpenAIRE |
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