HDL-apoA-I exchange: rapid detection and association with atherosclerosis.
High density lipoprotein (HDL) cholesterol levels are associated with decreased risk of cardiovascular disease, but not all HDL are functionally equivalent. A primary determinant of HDL functional status is the conformational adaptability of its main protein component, apoA-I, an exchangeable apolip...
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doaj-1e58836a5d004ecdb31766e8e2e6b96a2021-03-03T20:20:37ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0188e7154110.1371/journal.pone.0071541HDL-apoA-I exchange: rapid detection and association with atherosclerosis.Mark S BorjaLei ZhaoBradley HammersonChongren TangRichard YangNancy CarsonGayani FernandoXiaoqin LiuMadhu S BudamaguntaJacques GenestGregory C ShearerFranck DuclosMichael N OdaHigh density lipoprotein (HDL) cholesterol levels are associated with decreased risk of cardiovascular disease, but not all HDL are functionally equivalent. A primary determinant of HDL functional status is the conformational adaptability of its main protein component, apoA-I, an exchangeable apolipoprotein. Chemical modification of apoA-I, as may occur under conditions of inflammation or diabetes, can severely impair HDL function and is associated with the presence of cardiovascular disease. Chemical modification of apoA-I also impairs its ability to exchange on and off HDL, a critical process in reverse cholesterol transport. In this study, we developed a method using electron paramagnetic resonance spectroscopy (EPR) to quantify HDL-apoA-I exchange. Using this approach, we measured the degree of HDL-apoA-I exchange for HDL isolated from rabbits fed a high fat, high cholesterol diet, as well as human subjects with acute coronary syndrome and metabolic syndrome. We observed that HDL-apoA-I exchange was markedly reduced when atherosclerosis was present, or when the subject carries at least one risk factor of cardiovascular disease. These results show that HDL-apoA-I exchange is a clinically relevant measure of HDL function pertinent to cardiovascular disease.https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24015188/?tool=EBI |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Mark S Borja Lei Zhao Bradley Hammerson Chongren Tang Richard Yang Nancy Carson Gayani Fernando Xiaoqin Liu Madhu S Budamagunta Jacques Genest Gregory C Shearer Franck Duclos Michael N Oda |
spellingShingle |
Mark S Borja Lei Zhao Bradley Hammerson Chongren Tang Richard Yang Nancy Carson Gayani Fernando Xiaoqin Liu Madhu S Budamagunta Jacques Genest Gregory C Shearer Franck Duclos Michael N Oda HDL-apoA-I exchange: rapid detection and association with atherosclerosis. PLoS ONE |
author_facet |
Mark S Borja Lei Zhao Bradley Hammerson Chongren Tang Richard Yang Nancy Carson Gayani Fernando Xiaoqin Liu Madhu S Budamagunta Jacques Genest Gregory C Shearer Franck Duclos Michael N Oda |
author_sort |
Mark S Borja |
title |
HDL-apoA-I exchange: rapid detection and association with atherosclerosis. |
title_short |
HDL-apoA-I exchange: rapid detection and association with atherosclerosis. |
title_full |
HDL-apoA-I exchange: rapid detection and association with atherosclerosis. |
title_fullStr |
HDL-apoA-I exchange: rapid detection and association with atherosclerosis. |
title_full_unstemmed |
HDL-apoA-I exchange: rapid detection and association with atherosclerosis. |
title_sort |
hdl-apoa-i exchange: rapid detection and association with atherosclerosis. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2013-01-01 |
description |
High density lipoprotein (HDL) cholesterol levels are associated with decreased risk of cardiovascular disease, but not all HDL are functionally equivalent. A primary determinant of HDL functional status is the conformational adaptability of its main protein component, apoA-I, an exchangeable apolipoprotein. Chemical modification of apoA-I, as may occur under conditions of inflammation or diabetes, can severely impair HDL function and is associated with the presence of cardiovascular disease. Chemical modification of apoA-I also impairs its ability to exchange on and off HDL, a critical process in reverse cholesterol transport. In this study, we developed a method using electron paramagnetic resonance spectroscopy (EPR) to quantify HDL-apoA-I exchange. Using this approach, we measured the degree of HDL-apoA-I exchange for HDL isolated from rabbits fed a high fat, high cholesterol diet, as well as human subjects with acute coronary syndrome and metabolic syndrome. We observed that HDL-apoA-I exchange was markedly reduced when atherosclerosis was present, or when the subject carries at least one risk factor of cardiovascular disease. These results show that HDL-apoA-I exchange is a clinically relevant measure of HDL function pertinent to cardiovascular disease. |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24015188/?tool=EBI |
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