| First Author | Sontag TJ | Year | 2014 |
| Journal | PLoS One | Volume | 9 |
| Issue | 2 | Pages | e88705 |
| PubMed ID | 24520415 | Mgi Jnum | J:212949 |
| Mgi Id | MGI:5582564 | Doi | 10.1371/journal.pone.0088705 |
| Citation | Sontag TJ, et al. (2014) Polymorphisms of mouse apolipoprotein A-II alter its physical and functional nature. PLoS One 9(2):e88705 |
| abstractText | ApoA-II is the second most abundant protein on HDL making up approximately 20% of the total protein but its functions have still only been partially characterized. Recent methodological improvements have allowed for the recombinant expression and characterization of human apoA-II which shares only 55% sequence homology with murine apoA-II. Here we describe the purification of the two most common polymorphic variants of apoA-II found in inbred mouse strains, differing at 3 amino acid sites. C57BL/6 mice having variant apoA-II(a) have lower plasma HDL levels than FVB/N mice that have variant apoA-II(b). Characterization of the helical structure of these two variants reveals a more alpha-helical structure for the FVB/N apoA-II. These changes do not alter the lipid or HDL binding of the two apoA-II variants, but significantly increase the ability of the FVB/N variant to promote both ABCA1 and ABCG1 mediated cellular cholesterol efflux. These differences may be differentially altering plasma HDL apoA-II levels. In vivo, neither C57 nor FVB apoA-II protein levels are affected by the absence of apoE, while an apoE/apoA-I double deficiency results in a 50% decrease of plasma FVB apoA-II but results in undetectable levels of C57 apoA-II in the plasma. FVB apoA-II is able to form an HDL particle in the absence of apoE or apoA-I. |
