ArticleBiochimica et biophysica acta2010
The role of hydrophobic and negatively charged surface patches of lipid-free apolipoprotein A-I in lipid binding and ABCA1-mediated cholesterol efflux.
Article in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Reducing Complexity in Lipid Nanoparticles: Three-Component Zwitterionic Amino Lipids for Targeted Extrahepatic mRNA Delivery.ACS biomaterials science & engineering · 2025Article
- A thumbwheel mechanism for APOA1 activation of LCAT activity in HDL.Journal of lipid research · 2018Article
- Apolipoprotein A-II alters the proteome of human lipoproteins and enhances cholesterol efflux from ABCA1.Journal of lipid research · 2017Article
- Binding of human apoA-I[K107del] variant to TG-rich particles: implications for mechanisms underlying hypertriglyceridemia.Journal of lipid research · 2014Article
- Article
- Imaging apolipoprotein AI in vivo.NMR in biomedicine · 2011Article
- Update on HDL receptors and cellular cholesterol transport.Current atherosclerosis reports · 2011Review
- Structure of apolipoprotein A-I N terminus on nascent high density lipoproteins.The Journal of biological chemistry · 2011Article
- DmCatD, a cathepsin D-like peptidase of the hematophagous insect Dipetalogaster maxima (Hemiptera: Reduviidae): Purification, bioinformatic analyses and the significance of its interaction with lipophorin in the internalization by developing oocytes.Journal of insect physiologyArticle
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2 authors.
Funding
Abstract
Recent models of lipid-free apolipoprotein A-I, including a cross-link/homology model and an X-ray crystal structure have identified two potential functionally relevant "patches" on the protein surface. The first is a hydrophobic surface patch composed of leucine residues 42, 44, 46, and 47 and the second a negatively charged patch composed of glutamic acid residues 179, 191, and 198. To determine if these domains play a functional role, these surface patches were disrupted by site-directed mutagenesis and the bacterially expressed mutants were compared with respect to their ability to bind lipid and stimulate ABCA1-mediated cholesterol efflux. It was found that neither patch plays a significant functional role in the ability of apoA-I to accept cholesterol in an ABCA1-dependent manner, but that the hydrophobic patch did affect the ability of apoA-I to clear DMPC liposomes. Interestingly, contrary to previous predictions, disruption of the hydrophobic surface patch enhanced the lipid binding ability of apoA-I. The hydrophobic surface patch may be important to the structural stability of lipid-free apoA-I or may be a necessary permissive structural element for lipid binding.
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