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Apolipoprotein A5 ‐ enriched HDL is Poor Acceptor for Cholesterol in in vitro Efflux Study
Author(s) -
Ray Assaf,
Shaish Aviv,
Harats Dror,
Grosskopf Itamar
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.791.1
Subject(s) - chemistry , very low density lipoprotein , reverse cholesterol transport , cholesterol , apolipoprotein b , efflux , high density lipoprotein , lipoprotein , triglyceride , endocrinology , medicine , lecithin , biochemistry , biology
High density lipoprotein (HDL) plays central role in reverse cholesterol (CH) transport (RCT). Although apolipoprotein A5, a modulator of triglyceride‐rich lipoprotein metabolism, is abundant on HDL its effect on HDL‐driven RCT has not been elucidated. To test this macrophages loaded with 3 H‐ CH were incubated with whole plasma, total HDL (d=1.063–1.21), HDL 3 (d=1.063–1.09), preβ‐HDL (d=1.15–1.21) from apoA5 transgenic (A5tg) and from background mice. Lipoproteins from A5tg mice were associated with significantly (p<0.05) lower CH efflux (expressed as % of medium/medium + cells cpm): 54.0 ± 4.0 vs. 35 ± 2.0 in the presence of whole plasma, 19.9 ± 4.0 vs. 12.2 ± 2.0 in the presence of total HDL, 28 ± 5.0 vs. 16.0 ± 3.0 in the presence of HDL 3 , 8.2 ± 2.0 vs. 4.2 ± 1.0 in the presence of preβ‐HDL. When we use HDL 2 (d=1.09–1.15) as acceptor, CH efflux for A5tg mice was comparable to background FVB mice. Additionally, no difference in CH efflux between the two mice strains was demonstrated in experiments that used as acceptor very low density lipoprotein (VLDL) ‐ a lipoprotein that does not involve lecithin‐cholesterol acyltransferase (LCAT) activity. While potential underlying case include differences between the groups in both lipid and apoprotein content of HDL, the lack of difference between the groups in the VLDL experiments supports the possibility that interference of apoA5 with the activity of LCAT is a likely mechanism.