High-Density Lipoprotein Biogenesis: Defining the Domains Involved in Human Apolipoprotein A-I Lipidation

Pollard, Ricquita D.; Fulp, Brian; Sorci-Thomas, Mary G.; Thomas, Michael J.

doi:10.1021/acs.biochem.6b00347

Cited by 19Cholesterol and Lipid MetabolismLipoproteins and Cardiovascular HealthLipid Membrane Structure and Behavior

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High-Density Lipoprotein Biogenesis: Defining the Domains Involved in Human Apolipoprotein A-I Lipidation

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Pollard, Ricquita D., Fulp, Brian, Sorci-Thomas, Mary G., Thomas, Michael J.·2016·Biochemistry

DOI 10.1021/acs.biochem.6b00347PMC PMC5356376

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Abstract

The first step in removing cholesterol from a cell is the ATP-binding cassette transporter 1 (ABCA1)-driven transfer of cholesterol to lipid-free or lipid-poor apolipoprotein A-I (apoA-I), which yields cholesterol-rich nascent high-density lipoprotein (nHDL) that then matures in plasma to spherical, cholesteryl ester-rich HDL. However, lipid-free apoA-I has a three-dimensional (3D) conformation that is significantly different from that of lipidated apoA-I on nHDL. By comparing the lipid-free apoA-I 3D conformation of apoA-I to that of 9-14 nm diameter nHDL, we formulated the hypothetical helical domain transitions that might drive particle formation. To test the hypothesis, ten apoA-I mutants were prepared that contained two strategically placed cysteines several of which could form intramolecular disulfide bonds and others that could not form these bonds. Mass spectrometry was used to identify amino acid sequence and intramolecular disulfide bond formation. Recombinant HDL (rHDL) formation was assessed with this group of apoA-I mutants. ABCA1-driven nHDL formation was measured in four mutants and wild-type apoA-I. The mutants contained cysteine substitutions in one of three regions: the N-terminus, amino acids 34 and 55 (E34C to S55C), central domain amino acids 104 and 162 (F104C to H162C), and the C-terminus, amino acids 200 and 233 (L200C to L233C). Mutants were studied in the locked form, with an intramolecular disulfide bond present, or unlocked form, with the cysteine thiol blocked by alkylation. Only small amounts of rHDL or nHDL were formed upon locking the central domain. We conclude that both the N- and C-terminal ends assist in the initial steps in lipid acquisition, but that opening of the central domain was essential for particle formation.

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In vitro models express human apolipoproteins, lipoprotein receptors, and lipid transport proteins, providing a metabolically relevant context for studying lipid accumulation pathways relevant to MASLD.
“In contrast, in vitro models express human apolipoproteins, lipoprotein receptors, and lipid transport proteins [43,44,45,46], providing a metabolically relevant context for studying lipid accumulation pathways relevant to MASLD.”
From The HepG2 Cell Line as a Model for Studying Metabolic Dysfunction-Associated Steatotic Liver Disease (2026) · cites this paper as [46]
The Materials and Methods section ('Cell Culture and Purification of Nascent HDL'; page unavailable) describes an in vitro model using HEK293 cells expressing the lipid transporter ABCA1, incubated with human apoA-I. The paper does not show those cells expressing apolipoproteins or lipoprotein receptors, and it studies HDL formation rather than lipid accumulation pathways in MASLD. (LLM, conf=0.86)
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Authors: Pollard, R. D., Fulp, B., Sorci-Thomas, M. G., & Thomas, M. J.
Affiliations: Wake Forest University Health Sciences (US)
Departments of Medicine, Division of Endocrinology, Pharmacology and Toxicology, and Blood Research Institute, BloodCenter of Wisconsin, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, United States
Medical College of Wisconsin (US)
Corresponding author: Thomas, Michael J.
ORCID: Thomas, Michael J.
Venue: Biochemistry
Publisher: American Chemical Society (ACS)
Published: 2016-08-23
Volume: 55
Issue: 35
Pages: 4971-4981
ISSN: 0006-2960 (ISSN-L)
1520-4995
DOI: 10.1021/acs.biochem.6b00347
PMC: PMC5356376
OpenAlex: W2514134090
Cited by: 19
References: 87
Citations by year: 2026: 2 · 2024: 1 · 2023: 4 · 2021: 2 · 2020: 3 · 2018: 3 · 2017: 4
FWCI: 2.58
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Locations: Biochemistry (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: National Heart, Lung, and Blood Institute (HL-112270, HL-112270A1S1, HL-49373, HL-64163)
American Heart Association (09GRNT2280053, 14GRNT20500029)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Lipoproteins and Cardiovascular Health
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Keywords: apolipoprotein A-I, nascent HDL, ABCA1, cholesterol efflux, lipid modification, intramolecular disulfide bond, protein conformation, cysteine mutants, particle formation
MeSH terms: Protein Domains, Humans, Lipids, Lipoproteins, HDL, Mass Spectrometry, Apolipoprotein A-I, HEK293 Cells

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High-Density Lipoprotein Biogenesis: Defining the Domains Involved in Human Apolipoprotein A-I Lipidation

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