Definition and research guide
This page combines a MeSH definition, publication statistics and selected research abstracts. It is a starting point for reading the literature, not a medical textbook or a systematic evidence review.
Content available: 4 complete abstracts (701 words), 10 references. Full article text is not stored or reproduced here; follow the PMID, DOI or PMC links to read the original sources and their access terms.
Definition
The most abundant protein component of high density lipoproteins or HDL. This protein serves as an acceptor for cholesterol released from cells thus promoting efflux of cholesterol to HDL then to the liver for excretion from the body (reverse cholesterol transport). It also acts as a cofactor for lecithin cholesterol acyltransferase that forms cholesterol esters on the HDL particles. Mutations of this gene apoa1 cause HDL deficiency, such as in familial alpha lipoprotein deficiency disease and in some patients with tangier disease.
Definition: NLM Medical Subject Headings (MeSH) scope note (Public domain (U.S. National Library of Medicine); attribution requested). View the MeSH record.
Also known as: Apolipoprotein A I; Apo A-I; Apo A1; Apo AI; ApoA-1; ApoA-I; Apolipoprotein A-1; Apolipoprotein A 1.
Where it fits in the MeSH classification
- Broader topics
- Apolipoproteins A
Related concepts
- High Density Lipoproteins
- Cholesterol
- Liver
- Lecithin Cholesterol Acyltransferase
- Cholesterol Esters
- Apoa1
- Familial Alpha Lipoprotein Deficiency Disease
- Tangier Disease
Research landscape
PubMed indexes 9,538 records tagged with the MeSH heading “Apolipoprotein A-I” (counts retrieved 2026-10-31). 1,031 of them (10.8%) were published from 2020 onward, and the busiest period so far is through 1999 with 3,371 records.
Reviews account for 696 records (7.3%) and meta-analyses for 49. Randomized controlled trials number 478 (5.0%) as a share of all records on the topic.
Show the data
| Period | Records |
|---|---|
| through 1999 | 3,371 |
| 2000-2009 | 2,521 |
| 2010-2019 | 2,615 |
| 2020 onward | 1,031 |
Publication-type chart data
| Type | Records | Share |
|---|---|---|
| Reviews | 696 | 7.3% |
| Meta-analyses | 49 | 0.5% |
| Randomized controlled trials | 478 | 5.0% |
Method: PubMed query "Apolipoprotein A-I"[MeSH Terms] with publication-type and date filters, retrieved 2026-10-31.
Reading the evidence in drugs and chemicals
Studies of a chemical or drug can answer very different questions: what it is and how it behaves in cells and animals, how the body handles it, and whether it changes outcomes in people. Laboratory and animal findings often do not carry over to patients, and observational studies of exposures are confounded by who uses a substance and why. Nothing on this page is a recommendation to use, avoid, start or stop any substance or medicine; talk to a qualified clinician or pharmacist about your own situation. Check the dose, the species, the comparison group and whether a patient-relevant outcome was measured.
Evidence from open-access studies
These open-access studies come from PubMed’s best-match results for this heading (papers whose main topic it is), ranked here by citation count, with one recent addition. Each abstract is reproduced in full under its recorded open licence so that you can read the authors’ own words. They illustrate the literature; they are not a systematic summary of it. Citation counts measure attention, not reliability or clinical benefit.
| Study / authors | Year | Source label / design | Europe PMC citations | Licence / source |
|---|---|---|---|---|
| Apolipoprotein AI prevents regulatory to follicular helper T cell switching during atherosclerosis | 2018 | Research article Design not recorded in structured metadata | 155 | cc by PMID 29545616 · DOI · PMC5854619 |
| Acute exposure to apolipoprotein A1 inhibits macrophage chemotaxis in vitro and monocyte recruitment in vivo | 2016 | Research article Design not recorded in structured metadata | 63 | cc by PMID 27572261 · DOI · PMC5030090 |
| Apolipoprotein A-I enhances insulin-dependent and insulin-independent glucose uptake by skeletal muscle | 2019 | Research article Design not recorded in structured metadata | 56 | cc by PMID 30718702 · DOI · PMC6362284 |
| Apolipoprotein A-I (CSL112) and Cardiovascular Outcomes in Atherosclerotic Cardiovascular Disease: A Scoping Review | 2026 | Research article Design not recorded in structured metadata | 1 | cc by PMID 42047024 · DOI · PMC13122269 |
Apolipoprotein AI prevents regulatory to follicular helper T cell switching during atherosclerosis [1]
Abstract reading summary — source excerpts
- Opening excerpt
- Regulatory T (Treg) cells contribute to the anti-inflammatory response during atherogenesis.
- Closing excerpt
- Together our results suggest that ApoAI, the main protein in high-density lipoprotein particles, modulates the cellular fate of Treg cells and thus influences the immune response during atherosclerosis.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (145 words)
Regulatory T (Treg) cells contribute to the anti-inflammatory response during atherogenesis. Here we show that during atherogenesis Treg cells lose Foxp3 expression and their immunosuppressive function, leading to the conversion of a fraction of these cells into T follicular helper (Tfh) cells. We show that Tfh cells are pro-atherogenic and that their depletion reduces atherosclerosis. Mechanistically, the conversion of Treg cells to Tfh cells correlates with reduced expression of IL-2Rα and pSTAT5 levels and increased expression of IL-6Rα. In vitro, incubation of naive T cells with oxLDL prevents their differentiation into Treg cells. Furthermore, injection of lipid-free Apolipoprotein AI (ApoAI) into ApoE-/- mice reduces intracellular cholesterol levels in Treg cells and prevents their conversion into Tfh cells. Together our results suggest that ApoAI, the main protein in high-density lipoprotein particles, modulates the cellular fate of Treg cells and thus influences the immune response during atherosclerosis.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 29545616 · DOI · PMC5854619
Acute exposure to apolipoprotein A1 inhibits macrophage chemotaxis in vitro and monocyte recruitment in vivo [2]
Abstract reading summary — source excerpts
- Opening excerpt
- Apolipoprotein A1 (apoA1) is the major protein component of high-density lipoprotein (HDL) and has well documented anti-inflammatory properties.
- Closing excerpt
- Our data strengthen the evidence base for therapeutic apoA1 infusions in situations where reduced monocyte recruitment to sites of inflammation could have beneficial outcomes.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (146 words)
Apolipoprotein A1 (apoA1) is the major protein component of high-density lipoprotein (HDL) and has well documented anti-inflammatory properties. To better understand the cellular and molecular basis of the anti-inflammatory actions of apoA1, we explored the effect of acute human apoA1 exposure on the migratory capacity of monocyte-derived cells in vitro and in vivo. Acute (20-60 min) apoA1 treatment induced a substantial (50-90%) reduction in macrophage chemotaxis to a range of chemoattractants. This acute treatment was anti-inflammatory in vivo as shown by pre-treatment of monocytes prior to adoptive transfer into an on-going murine peritonitis model. We find that apoA1 rapidly disrupts membrane lipid rafts, and as a consequence, dampens the PI3K/Akt signalling pathway that coordinates reorganization of the actin cytoskeleton and cell migration. Our data strengthen the evidence base for therapeutic apoA1 infusions in situations where reduced monocyte recruitment to sites of inflammation could have beneficial outcomes.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 27572261 · DOI · PMC5030090
Apolipoprotein A-I enhances insulin-dependent and insulin-independent glucose uptake by skeletal muscle [3]
Abstract reading summary — source excerpts
- Opening excerpt
- Therapeutic interventions that increase plasma high density lipoprotein (HDL) and apolipoprotein (apo) A-I levels have been reported to reduce plasma glucose levels and attenuate insulin resistance.
- Closing excerpt
- The findings suggest that therapeutic agents that increase apoA-I levels may improve glycemic control in people with type 2 diabetes.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (176 words)
Therapeutic interventions that increase plasma high density lipoprotein (HDL) and apolipoprotein (apo) A-I levels have been reported to reduce plasma glucose levels and attenuate insulin resistance. The present study asks if this is a direct effect of increased glucose uptake by skeletal muscle. Incubation of primary human skeletal muscle cells (HSKMCs) with apoA-I increased insulin-dependent and insulin-independent glucose uptake in a time- and concentration-dependent manner. The increased glucose uptake was accompanied by enhanced phosphorylation of the insulin receptor (IR), insulin receptor substrate-1 (IRS-1), the serine/threonine kinase Akt and Akt substrate of 160 kDa (AS160). Cell surface levels of the glucose transporter type 4, GLUT4, were also increased. The apoA-I-mediated increase in glucose uptake by HSKMCs was dependent on phosphatidylinositol-4,5-bisphosphate 3-kinase (PI3K)/Akt, the ATP binding cassette transporter A1 (ABCA1) and scavenger receptor class B type I (SR-B1). Taken together, these results establish that apoA-I increases glucose disposal in skeletal muscle by activating the IR/IRS-1/PI3K/Akt/AS160 signal transduction pathway. The findings suggest that therapeutic agents that increase apoA-I levels may improve glycemic control in people with type 2 diabetes.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 30718702 · DOI · PMC6362284
Apolipoprotein A-I (CSL112) and Cardiovascular Outcomes in Atherosclerotic Cardiovascular Disease: A Scoping Review [4]
Abstract reading summary — source excerpts
- Opening excerpt
- BackgroundApolipoprotein A-I (ApoA-I), the principal protein component of high-density lipoproteins (HDL), plays a pivotal role in cardiovascular physiology and has gained increasing attention in atherosclerotic cardiovascular disease (ASCVD).
- Closing excerpt
- Integrating ApoA-I into personalized treatment strategies could improve cardiovascular outcomes and reduce disease burden.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (234 words)
BackgroundApolipoprotein A-I (ApoA-I), the principal protein component of high-density lipoproteins (HDL), plays a pivotal role in cardiovascular physiology and has gained increasing attention in atherosclerotic cardiovascular disease (ASCVD). Its involvement extends beyond lipid transport to include anti-inflammatory and antioxidant mechanisms.ObjectiveTo comprehensively evaluate the role of ApoA-I in ASCVD, including its biological functions, clinical relevance as a biomarker, and potential as a therapeutic target.MethodsA scoping review of the literature was conducted to examine current evidence on ApoA-I in cardiovascular health and disease. Studies assessing its role in reverse cholesterol transport (RCT), association with cardiovascular outcomes, and emerging therapeutic strategies were included.ResultsApoA-I contributes significantly to reverse cholesterol transport and exhibits antioxidant and anti-inflammatory properties that protect against atherosclerosis. Elevated ApoA-I levels are consistently associated with reduced risk of major adverse cardiovascular events, supporting its utility as a biomarker for cardiovascular risk assessment. However, variability in HDL particle composition and the influence of confounding factors such as comorbidities and lifestyle limit its interpretability. Therapeutic approaches targeting ApoA-I, including infusion therapies and mimetic peptides, have shown mixed results in clinical trials, highlighting ongoing challenges.ConclusionApoA-I remains a promising biomarker and therapeutic target in ASCVD, though its clinical application is complicated by biological and methodological variability. Future research focusing on gene therapies, small molecule modulators, and ApoA-I mimetics may enhance its functional properties and clinical utility. Integrating ApoA-I into personalized treatment strategies could improve cardiovascular outcomes and reduce disease burden.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 42047024 · DOI · PMC13122269
Key reviews and meta-analyses
The most cited review-type papers among PubMed’s best-match results for this heading, listed with bibliographic details only. Follow the links for the full text and access terms.
- Research article The apoB/apoA-I ratio: a strong, new risk factor for cardiovascular disease and a target for lipid-lowering therapy--a review of the evidence [5]
- Research article Role of apoA-I, ABCA1, LCAT, and SR-BI in the biogenesis of HDL [6]
- Research article Apolipoprotein B and apolipoprotein A-I: risk indicators of coronary heart disease and targets for lipid-modifying therapy [7]
- Research article Formation and metabolism of prebeta-migrating, lipid-poor apolipoprotein A-I [8]
- Research article Apolipoprotein A-I mimetic peptides [9]
- Research article Apolipoprotein A-I: structure-function relationships [10]
References
- Gaddis DE, Padgett LE, Wu R, McSkimming C, Romines V, Taylor AM, et al.. Apolipoprotein AI prevents regulatory to follicular helper T cell switching during atherosclerosis. . 2018. PMID 29545616 · DOI · PMC5854619
- Iqbal AJ, Barrett TJ, Taylor L, McNeill E, Manmadhan A, Recio C, et al.. Acute exposure to apolipoprotein A1 inhibits macrophage chemotaxis in vitro and monocyte recruitment in vivo. . 2016. PMID 27572261 · DOI · PMC5030090
- Tang S, Tabet F, Cochran BJ, Cuesta Torres LF, Wu BJ, Barter PJ, et al.. Apolipoprotein A-I enhances insulin-dependent and insulin-independent glucose uptake by skeletal muscle. . 2019. PMID 30718702 · DOI · PMC6362284
- Habib A, Khan MSM, Aneeq A, Tahir HMT, Mehmoodi A, Malik J, et al.. Apolipoprotein A-I (CSL112) and Cardiovascular Outcomes in Atherosclerotic Cardiovascular Disease: A Scoping Review. . 2026. PMID 42047024 · DOI · PMC13122269
- Walldius G, Jungner I. The apoB/apoA-I ratio: a strong, new risk factor for cardiovascular disease and a target for lipid-lowering therapy--a review of the evidence. J Intern Med. 2006. PMID 16629855 · DOI
- Zannis VI, Chroni A, Krieger M. Role of apoA-I, ABCA1, LCAT, and SR-BI in the biogenesis of HDL. J Mol Med (Berl). 2006. PMID 16501936 · DOI
- Walldius G, Jungner I. Apolipoprotein B and apolipoprotein A-I: risk indicators of coronary heart disease and targets for lipid-modifying therapy. J Intern Med. 2004. PMID 14746556 · DOI
- Rye KA, Barter PJ. Formation and metabolism of prebeta-migrating, lipid-poor apolipoprotein A-I. Arterioscler Thromb Vasc Biol. 2004. PMID 14592845 · DOI
- Navab M, Anantharamaiah GM, Reddy ST, Hama S, Hough G, Grijalva VR, et al.. Apolipoprotein A-I mimetic peptides. Arterioscler Thromb Vasc Biol. 2005. PMID 15831812 · DOI
- Frank PG, Marcel YL. Apolipoprotein A-I: structure-function relationships. J Lipid Res. 2000. PMID 10828078 · DOI
About this article
- Sources
- NLM Medical Subject Headings (definition, synonyms); NCBI PubMed (counts, identifiers); Europe PMC (open-access abstracts and citation counts).
- Verification
- Every reference was resolved against PubMed on 2026-10-31; title, year and DOI matched.
- Review state
- automated source verified; no human expert review has been recorded yet.
- Version
- 1, last updated 2026-10-31.
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Evidence strength
EvidenceHelix's computed view of the study designs behind this topic: how common meta-analyses, randomized trials and reviews are, how recent the literature is, and a plain-language reading. It describes the design mix of the literature. It is not a quality appraisal of any study, and it is not medical advice.