Affinage

APOC3

Apolipoprotein C-III · UniProt P02656

Length
99 aa
Mass
10.9 kDa
Annotated
2026-06-09
100 papers in source corpus 37 papers cited in narrative 37 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 8/8 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

ApoC-III is a small exchangeable apolipoprotein that governs the catabolism of triglyceride-rich lipoproteins (TRLs), and its overexpression causes hypertriglyceridemia primarily by slowing tissue uptake of VLDL rather than by altering LPL substrate quality (PMID:1430212). Mechanistically it acts in two ways: an enriched apoC-III content displaces apoE from the lipoprotein surface and impairs receptor binding, a defect corrected by adding exogenous apoE or by co-expressing human apoE (PMID:8864964, PMID:15863838), and its inhibition of TRL clearance operates through a hepatic LDLR/LRP1 axis — apoC-III antisense oligonucleotide lowers triglyceride in mice lacking LPL, HSPG, LDLR alone, or LRP1 alone but fails when both LDLR and LRP1 are absent (PMID:27400128). When this receptor-mediated route is unavailable, as in apoE deficiency, apoC-III instead suppresses LPL activity, identifying it as a more specific LPL inhibitor than apoE (PMID:31092690, PMID:15863838). Human loss-of-function genetics confirm this model: reduced apoC-III accelerates VLDL-TG fractional clearance and remnant-to-LDL conversion without changing production rates (PMID:30580564, PMID:36040803). Beyond clearance, apoC-III contributes to hepatic VLDL1 assembly through its C-terminal lipid-binding domain, where the lipid-binding residue Lys58 and an intact positive charge are required to drive microsomal lumenal lipid droplet formation and VLDL1-TAG secretion (PMID:21676879), and the Ala23Thr variant blocks second-step VLDL1 maturation (PMID:20097930). Distinct sialylated glycoforms are differentially cleared by HSPG versus LDLR/LRP1, with O-glycosylation at Thr74 dispensable for secretion and lipid binding (PMID:31390883, PMID:3192519). APOC3 transcription is integrated at a promoter dominated by HNF-4 acting at the CIIIB/hormone response element, activated by SMAD3/4, ATF-2, SP1, RXR heterodimers, Foxo1, and PGC-1β/ERRα, and repressed by ARP-1/EAR-2/EAR-3, Rev-erbα, Jun family members, MAP kinase signaling, and insulin via Foxo1 (PMID:1639815, PMID:10995777, PMID:12454280, PMID:15546000, PMID:20889132, PMID:7868970). ApoC-III also exerts proinflammatory and tissue-injury effects, inducing endothelial dysfunction via TNF-α/JAM-1 (PMID:27619170) and macrophage NLRP3 pyroptosis via the SCIMP-SYK pathway (PMID:38232538).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 1984 High

    Establishing the APOC3 gene and protein sequence provided the molecular foundation for studying its regulation and function.

    Evidence Genomic clone sequencing of the APOA1-APOC3 locus and cDNA cloning defining the signal peptide and mature sequence

    PMID:2989400 PMID:6439535

    Open questions at the time
    • Does not address protein function or lipid interaction
    • Intergenic regulatory architecture only structurally noted
  2. 1979 Medium

    Biophysical study of apoC-III on bilayers showed it as a surface-bound, laterally mobile lipid-binding protein, characterizing the lipoprotein-surface behavior central to its later mechanistic roles.

    Evidence FRAP and light scattering of labeled apoC-III on phosphatidylcholine bilayers

    PMID:293667

    Open questions at the time
    • Model membranes, not native lipoproteins
    • No link to receptor binding or LPL at this stage
  3. 1988 High

    Resolving whether the Thr74 O-glycan was functionally required showed it is dispensable for secretion and lipid binding, redirecting attention from glycosylation as a determinant of basic function.

    Evidence Thr74Ala site-directed mutagenesis with secretion and density-gradient lipid-binding assays in stable cell lines, building on identification of the unglycosylated apoC-III-0 variant

    PMID:3123586 PMID:3192519

    Open questions at the time
    • Did not test glycoform-specific receptor clearance (resolved later)
    • No role for glycosylation in inflammation tested
  4. 1992 High

    The pivotal mechanistic question of whether apoC-III raises triglyceride by inhibiting LPL or by impairing clearance was answered in favor of reduced receptor-mediated hepatic uptake.

    Evidence Transgenic mouse VLDL turnover/FCR studies with radiolabeled VLDL, LPL activity assays, and hepatoma uptake assays

    PMID:1430212

    Open questions at the time
    • Did not identify the specific receptor(s) responsible
    • Mechanism of impaired uptake (apoE displacement) not yet defined
  5. 1996 High

    The defect in receptor-mediated uptake was traced to a reciprocal apoC-III/apoE relationship on the lipoprotein surface, defining apoE displacement as the proximal cause.

    Evidence ApoC-III/apoE transgenic crosses, fibroblast receptor-binding and heparin-Sepharose assays, apoE rescue

    PMID:8864964

    Open questions at the time
    • Did not distinguish LDLR from LRP1 contributions
    • Quantitative stoichiometry of displacement unresolved
  6. 2000 High

    Mapping the APOC3 promoter established HNF-4 acting at the CIIIB/hormone response element as the central integrator, with multiple activators and repressors converging on it.

    Evidence Footprinting, deletion/mutation and cotransfection assays defining HNF-4, ARP-1/EAR-2/EAR-3, SP1, NF-κB, RXR heterodimers, ATF-2/Jun, and SMAD3/4 inputs (Co-IP confirming SMAD-HNF-4 interaction)

    PMID:10995777 PMID:1639815 PMID:7640286 PMID:8036173 PMID:9760243 PMID:9893992

    Open questions at the time
    • Most binding/cotransfection data are single-lab in HepG2
    • In vivo relevance of several factors not tested
  7. 2004 High

    The longstanding observation that insulin lowers apoC-III was given a transcriptional mechanism: insulin acts through Foxo1 nuclear exclusion at an apoC-III insulin response element, explaining diabetic hypertriglyceridemia.

    Evidence Nuclear run-on insulin studies in diabetic mice and HepG2, plus Foxo1 promoter mutagenesis with adenoviral/transgenic in vivo validation

    PMID:15546000 PMID:7868970

    Open questions at the time
    • Upstream insulin signaling steps to Foxo1 not fully mapped here
    • Tissue specificity (liver vs intestine) of the response incompletely defined
  8. 2002 High

    Identification of Rev-erbα as a repressor and PGC-1β/ERRα as activators placed APOC3 transcription within circadian and energy-metabolism control, with PGC-1β knockdown rescuing hypertriglyceridemia.

    Evidence Rev-erbα promoter mapping and knockout mice; PGC-1β proteomic complex analysis with liver-specific RNAi and nicotinic acid studies

    PMID:12454280 PMID:20889132

    Open questions at the time
    • Chromatin cofactor identities for PGC-1β/ERRα only partly defined
    • Crosstalk between circadian and insulin inputs not resolved
  9. 2011 High

    A second, intracellular function emerged: the C-terminal lipid-binding domain drives hepatic VLDL1 assembly via lumenal lipid droplet formation, with disease-associated mutations dissecting the step.

    Evidence Ala23Thr and Lys58 (K58E) mutant expression in McA-RH7777 cells and apoc3-null mice, metabolic labeling, Fat Western lipid-binding, charge-substitution mutagenesis

    PMID:20097930 PMID:21676879

    Open questions at the time
    • Molecular partners mediating droplet-VLDL fusion not identified
    • Structural basis of lipid binding at K58 not solved
  10. 2016 High

    Genetic epistasis pinned the clearance-inhibition mechanism to the hepatic LDLR/LRP1 axis and showed it is independent of VLDL secretion and muscle uptake.

    Evidence ApoC-III ASO across LPL-, HSPG-, LDLR-, LRP1-, and double LDLR/LRP1-knockout mice with clearance and injection studies

    PMID:27400128

    Open questions at the time
    • Did not explain residual LPL-dependent effects in receptor-null settings (later resolved)
    • Relative contribution of LDLR vs LRP1 not separated
  11. 2019 High

    Resolving the apparent dual mechanism, apoE was shown to be required for the LDLR/LRP1 route, and apoC-III reverts to LPL inhibition when hepatic clearance is absent; glycoforms were further shown to partition between receptors.

    Evidence ApoC-III ASO in Apoe-/-Ndst1f/f double-deficient mice with adipose LPL measurement; glycoform-specific clearance in KO mice with patient mass spectrometry

    PMID:15863838 PMID:31092690 PMID:31390883

    Open questions at the time
    • Molecular basis of glycoform-receptor selectivity unresolved
    • Quantitative balance of the two mechanisms in humans not defined
  12. 2022 High

    Human loss-of-function kinetics validated the clearance model in vivo, showing reduced apoC-III accelerates lipolysis and remnant clearance without altering lipoprotein production.

    Evidence Stable-isotope turnover studies of VLDL-TG, apoB48/apoB100 fractions in R19X and other LOF carriers vs non-carriers

    PMID:30580564 PMID:36040803

    Open questions at the time
    • Tissue site of accelerated lipolysis not directly measured in humans
    • Effect on inflammatory endpoints not assessed
  13. 2024 Medium

    Beyond lipid handling, apoC-III was shown to act as a proinflammatory and tissue-injury effector across endothelium, macrophages, valve cells, and CKD, broadening its pathological scope.

    Evidence HUVEC TNF-α/JAM-1 siRNA rescue; macrophage NLRP3/SCIMP-SYK pyroptosis with Co-IP and inhibitor rescue; valve cell calcification proteomics/IHC; CKD guanidinylation mass spectrometry with mouse models

    PMID:27619170 PMID:33334888 PMID:34588185 PMID:38232538

    Open questions at the time
    • Receptor mediating apoC-III proinflammatory signaling not identified
    • Most pathways are single-lab and partially characterized
    • Link between lipid and inflammatory functions mechanistically unconnected

Open questions

Synthesis pass · forward-looking unresolved questions
  • The receptor(s) and signal-transduction machinery by which extracellular apoC-III triggers cellular inflammation and the precise stoichiometry by which it balances apoE displacement against direct LPL inhibition in human physiology remain undefined.
  • No defined cell-surface receptor for apoC-III signaling
  • Unified structural model linking lipid-binding, receptor-displacement, and LPL-inhibition functions absent

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0008289 lipid binding 3 GO:0098772 molecular function regulator activity 3
Localization
GO:0005576 extracellular region 3 GO:0005783 endoplasmic reticulum 2
Pathway
R-HSA-1430728 Metabolism 3 R-HSA-74160 Gene expression (Transcription) 3 R-HSA-8953854 Metabolism of RNA 3
Partners
APOEHNF4ALDLRLRP1SMAD3SMAD4

Evidence

Reading pass · 37 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1992 Hypertriglyceridemia in human APOC3 transgenic mice results primarily from decreased tissue uptake (reduced fractional catabolic rate) of triglyceride-rich VLDL particles, associated with increased apoC-III and decreased apoE content on VLDL particles, impairing receptor-mediated hepatic uptake rather than reducing LPL activity or substrate quality for LPL. Transgenic mouse models (low and high expressors), in vivo VLDL turnover/FCR studies with radiolabeled VLDL, tissue LPL activity assays, hepatoma cell uptake assays, primary hepatocyte secretion studies, electron microscopy The Journal of clinical investigation High 1430212
1996 ApoC-III and apoE exert a functionally significant reciprocal relationship on triglyceride-rich lipoprotein surfaces: excess apoC-III displaces apoE, impairing lipoprotein receptor binding; adding exogenous apoE corrects the defect, and crossing apoC-III transgenic mice with human apoE transgenic mice normalizes hypertriglyceridemia. Additionally, apoC-III-enriched VLDL shows decreased heparin-Sepharose binding, suggesting impaired HSPG-mediated LPL interaction. ApoC-III transgenic and mouse apoC-III transgenic mouse models, vitamin A fat tolerance test, fibroblast lipoprotein receptor binding assays, cross-breeding with apoE transgenic mice, heparin-Sepharose binding assays Journal of lipid research High 8864964
1984 The human APOC3 gene structure was determined: the coding sequence is interrupted by three introns located in the 5' noncoding region, in the signal sequence-encoding region, and in the mature protein-coding region. The intergenic region between APOA1 and APOC3 was characterized. Genomic DNA isolation, complete DNA sequence determination, structural analysis DNA (Mary Ann Liebert, Inc.) High 6439535
1985 ApoC-III primary translational product contains a 20 amino acid N-terminal signal peptide. cDNA cloning corrected the amino acid sequence at four positions. The SacI polymorphism in the 3' noncoding region does not alter the apoC-III amino acid sequence despite three nucleotide differences between Sac+ and Sac- alleles. cDNA cloning, nucleotide sequencing, comparison of two allelic cDNA clones Journal of lipid research High 2989400
1987 A Thr74→Ala74 substitution in apoC-III abolishes O-linked glycosylation at position 74, the site where a carbohydrate chain (galactosamine, galactose, sialic acid) is normally attached. This variant produces unglycosylated apoC-III (apoC-III-0). ApoC-III gene cloning from a subject with elevated apoC-III-0, DNA sequencing, identification of A→G transition creating AluI site Journal of lipid research High 3123586
1988 O-linked glycosylation at Thr74 of apoC-III is not required for intracellular transport, secretion, or lipid (lipoprotein) binding; cells expressing the Thr74→Ala74 mutant secrete unmodified apoC-III with similar flotation properties and relative affinities for VLDL and HDL as the glycosylated form. Site-directed mutagenesis of Thr74→Ala74, stable cell line transfection (BPV vector), pulse-chase labeling, density gradient ultracentrifugation The Journal of biological chemistry High 3192519
1989 A 13-nucleotide promoter element (C3P, located in the apoCIII promoter) is required for high-level hepatic apoCIII expression and is sufficient to confer hepatic-specific expression on a heterologous promoter. A hepatic nuclear protein (AF-1) binds this element. Cell-type-specific activity is not due to absence of binding proteins in non-expressing cells but to qualitative differences in C3P-binding proteins across cell types. Reporter gene transfection assays, nuclear extract binding assays, identification of AF-1 protein The Journal of biological chemistry Medium 2777781
1990 The human apoCIII promoter contains 10 nuclear protein footprints between -792 and -25. The region -890 to -686 contains factors promoting both hepatic and intestinal transcription; -686 to -553 contains hepatic-specific factors. The -86 to -74 region (CIIIB) is recognized by two mutually exclusive factors: CIIIB1 (associated with reduced transcription) and CIIIB2 (associated with normal transcription). Promoter deletion analysis, nucleotide substitution, DNase I footprinting with rat liver nuclear extracts, DNA binding and methylation interference assays, transfection of HepG2 and Caco-2 cells The Journal of biological chemistry High 2161843
1991 Nuclear factor CIIIB1 was purified from rat liver nuclear extracts. It is a ~41 kDa polypeptide that binds the octameric motif CAGGTGAC in the apoCIII promoter (-86 to -74) and also the apoA-II promoter region containing the same motif, suggesting shared regulatory function. Nucleotide substitutions within this octamer abolish CIIIB1 binding. Protein purification (anion/cation exchange chromatography, sequence-specific affinity chromatography, heat treatment), SDS-PAGE, photoaffinity cross-linking, DNase I footprinting, methylation interference The Journal of biological chemistry High 2033057
1992 Four members of the steroid hormone receptor superfamily — HNF-4, ARP-1, EAR-2, and EAR-3 — bind specifically to regulatory elements (BA1 in APOB, CIIIB in APOC3, AIIJ in APOAII) with dissociation constants of 1-3 nM. ARP-1, EAR-2, and EAR-3 repress APOC3 promoter activity; HNF-4 activates transcription and reverses ARP-1-mediated repression through competition for the same regulatory element CIIIB. DNA binding assays (Kd measurements), cotransfection in HepG2 cells, reporter gene assays with homopolymeric promoters, site-directed mutagenesis of HNF-4 binding sites The Journal of biological chemistry High 1639815
1994 Insulin transcriptionally downregulates apoC-III gene expression. In streptozotocin-diabetic mice, hepatic apoC-III mRNA increases 1.4-1.5-fold; insulin treatment normalizes it. Nuclear run-on assays confirm transcriptional regulation. Insulin causes dose-dependent repression of apoC-III transcriptional activity in transfected HepG2 cells. Streptozotocin-diabetic mouse model, Northern analysis, quantitative RNase protection assay, nuclear run-on transcription assay, reporter gene transfection in HepG2 cells with insulin treatment Journal of lipid research High 7868970
1994 The apoCIII promoter contains a functional NF-κB binding element at approximately -150 bp upstream of the transcriptional start site. Purified NF-κB and the p50/p65 subunits in HepG2 nuclear extracts bind this element specifically. The element confers PMA- and IL-1β-inducible transcriptional activity. Upstream enhancer sequences (~-500 bp) suppress this NF-κB-mediated inducibility. EMSA with purified NF-κB, HepG2 nuclear extracts, antibody supershift (p50, p65), reporter gene transfection, deletion analysis Nucleic acids research High 8036173
1995 Transcriptional activation of apoCIII requires complex interactions: SP1 binds distal regulatory elements F, H, and I; orphan receptors ARP-1 and EAR-3 bind element G (a specialized HRE that HNF-4 does not bind); HNF-4 binds proximal element B and distal element I4. Distal SP1 sites enhance proximal HNF-4-driven transcription approximately 10-fold, requiring an intact hormone response element on the proximal promoter. DNA binding assays, competition assays, supershift assays, transient transfection in HepG2 cells, synthetic promoter constructs Biochemistry Medium 7640286
1999 The MAP kinase signaling pathway regulates apoCIII gene transcription. Inhibition of MAP kinase (PD98059) increases apoCIII transcription 5-8-fold; activation by phorbol ester reduces it 3-5-fold. The MAP kinase-responsive element maps to a 6-bp element at -740, bound predominantly by HNF4. MAP kinase regulates apoCIII at least in part by modulating HNF4 mRNA and protein levels. HepG2 cell transfection, MAP kinase inhibitor (PD98059) and activator (phorbol ester) treatment, promoter deletion mapping, EMSA, HNF4 mRNA/protein quantification The Journal of biological chemistry Medium 10551874
1999 Ligand-dependent nuclear receptors modulate apoCIII promoter activity: RXRα/RARα heterodimers bind elements B and G and activate apoCIII promoter ~2-fold in the presence of 9-cis or all-trans RA; RXRα/T3Rβ heterodimers activate with 9-cis RA but repress in the presence of T3. Binding sites (DR-1 for RXRα/RARα, DR-5 for RXRα/T3Rβ) were mapped by methylation interference. DNA binding assays, methylation interference, cotransfection in HepG2 cells, ligand treatment (RA, T3), promoter mutation analysis Biochemistry Medium 9893992
1998 ATF-2 is a positive transcriptional regulator of apoCIII: it binds three regions in the apoCIII promoter (at -747/-726, -219/-199, and -102/-75), and cotransfection activates the promoter ~1.6-fold. Jun family members (c-Jun, JunB, JunD) dose-dependently repress the apoCIII promoter by interfering with the apoCIII enhancer; Jun repression can be reversed by ATF-2 and HNF-4. DNase I footprinting, cotransfection in HepG2 cells, reporter gene assays, promoter deletion and mutation analysis Biochemistry Medium 9760243
2000 SMAD3 and SMAD3-SMAD4 transactivate the apoCIII promoter 15-70-fold; dominant-negative SMAD4 represses it by 50%. SMAD-mediated transactivation requires an intact hormone response element and depends on HNF-4: antisense ribozyme knockdown of HNF-4 reduces constitutive apoCIII promoter activity to 10% and abolishes SMAD-mediated transactivation. SMAD3, SMAD4, and HNF-4 physically interact as shown by Co-IP and GST pull-down. HepG2 cotransfection with SMAD expression constructs, dominant-negative SMAD4, antisense HNF-4 ribozyme, Co-immunoprecipitation, GST pull-down, reporter gene assays The Journal of biological chemistry High 10995777
2000 A hormone response element within the apoCIII enhancer (located ~0.8 kb upstream of the apoCIII cap site) is essential for intestinal and renal expression of the linked apoA-I gene and contributes to hepatic expression of both apoA-I and apoCIII. Mutations in this element abolish intestinal and renal apoA-I expression and reduce hepatic expression by 80%. Transgenic mice carrying wild-type or HRE-mutated apoA-I/apoCIII gene cluster, tissue-specific reporter (CAT) expression analysis The Journal of biological chemistry High 10893424
2002 Rev-erbα is a physiological repressor of apoCIII gene transcription: it decreases basal and HNF-4-stimulated apoCIII promoter activity in transfected rat hepatocytes and RK13 cells. A Rev-erbα response element (AGGTCA half-site) was mapped to position -23/-18 in the apoCIII promoter by deletion/mutation analysis and gel-shift assays. Rev-erbα-deficient mice display elevated serum and hepatic apoC-III mRNA levels with increased serum VLDL-TG. Cotransfection in rat primary hepatocytes and RK13 cells, promoter deletion and mutation analysis, gel-shift (EMSA), Rev-erbα knockout mice (serum and liver mRNA analysis) Journal of lipid research High 12454280
2004 Foxo1 mediates insulin action on apoC-III expression: Foxo1 stimulates hepatic apoC-III transcription by binding its consensus site in the apoC-III promoter. Deletion or mutation of this binding site abolishes the insulin response element and Foxo1-stimulated transcription. Adenoviral overexpression of Foxo1 in mouse liver elevates apoC-III mRNA, increases plasma TG, and impairs fat tolerance. In diabetic NOD and db/db mice, Foxo1 is elevated and skewed toward nuclear distribution, correlating with elevated apoC-III. Adenovirus-mediated gene transfer of Foxo1 to hepatocytes, Foxo1 binding site deletion and mutation in apoC-III promoter, reporter gene assays in enterocytes and hepatocytes, transgenic mice with constitutively active Foxo1, diabetic mouse models (NOD, db/db) The Journal of clinical investigation High 15546000
2010 PGC-1β transcriptionally regulates APOC3 expression by coactivating the orphan nuclear receptor ERRα and recruiting chromatin-remodeling cofactors to stimulate APOC3 gene transcription. Liver-specific knockdown of APOC3 significantly ameliorates PGC-1β-induced hypertriglyceridemia. Nicotinic acid reduces hepatic PGC-1β and APOC3 expression; adenoviral knockdown of either PGC-1β or APOC3 recapitulates nicotinic acid's hypolipidemic effect. Adenoviral RNAi knockdown (liver-specific), proteomic analysis of PGC-1β transcriptional complex, mouse models with adenoviral PGC-1β overexpression, nicotinic acid treatment Cell metabolism High 20889132
2010 The Ala23Thr hypotriglyceridemia-associated missense mutation in apoC-III abolishes VLDL1 assembly: C3AT cells have markedly decreased TAG secretion and fail to assemble VLDL1. Microsomal lumenal [3H]TAG in C3AT cells accumulates 60% higher than wild-type cells, primarily in IDL/LDL-like lumenal particles, suggesting that Ala23Thr blocks the second-step VLDL1 maturation (lipid droplet-VLDL precursor fusion), not microsomal triglyceride transfer protein activity. Transfected McA-RH7777 cells expressing wild-type or Ala23Thr mutant apoC-III, metabolic labeling with [3H]glycerol and [35S], density gradient fractionation of lumenal lipoproteins, brefeldin A comparison, MTP activity assay Journal of lipid research High 20097930
2011 The C-terminal lipid-binding domain of apoC-III (residue Lys58) is critical for VLDL assembly and secretion: the K58E missense mutation (found in hypotriglyceridemic humans) abolishes apoC-III binding to lipids (Fat Western assay) and eliminates its ability to stimulate VLDL1-TAG secretion and lumenal lipid droplet (LLD) accumulation. The positive charge at position 58 (not just Lys) is required. ApoC-III plays a role in forming microsomal lumenal lipid droplets as precursors for VLDL assembly. Transfected McA-RH7777 cells and apoc3-null mice injected with adenovirus expressing C3wt or C3KE, metabolic labeling, Fat Western lipid-protein overlay assay, charge substitution mutagenesis (K58R, K58E/K60E) The Journal of biological chemistry High 21676879
2016 ApoC-III inhibits clearance of triglyceride-rich lipoproteins primarily through a hepatic mechanism dependent on the LDL receptor (LDLR) and LRP1 axis. ApoC-III ASO lowers plasma TG in mice lacking LPL, HSPG receptors, LDLR alone, or LRP1 alone, but fails to lower TG in mice lacking both LDLR and LRP1. ApoC-III ASO has no effect on VLDL secretion or tissue (heart/skeletal muscle) lipid uptake. ApoC-III antisense oligonucleotide treatment in multiple mouse knockout lines (LPL-deficient, HSPG-deficient, LDLR-KO, LRP1-KO, double LDLR/LRP1-KO), postprandial clearance studies, lipoprotein injection experiments The Journal of clinical investigation High 27400128
2017 The APOC3 A43T missense variant causes reduced apoC-III levels due to impaired binding of A43T apoC-III to lipoproteins and accelerated renal catabolism of free apoC-III. The reduced apoC-III content on TRLs results in accelerated TRL clearance in vivo. A monoclonal antibody targeting lipoprotein-bound human apoC-III promotes its clearance and enhances TRL catabolism. Human APOC3 A43T heterozygote characterization, mice expressing human APOC3 A43T, lipoprotein-binding assays, in vivo catabolism studies, monoclonal antibody development and testing in humanized mice Nature medicine High 28825717
2019 ApoE is essential for apoC-III-mediated inhibition of TRL clearance via LDLR/LRP1. In apoE-deficient mice also lacking HSPG (Apoe-/-Ndst1f/fAlb-Cre+), apoC-III ASO reduces plasma TG without improving hepatic TRL clearance; instead, TG reduction is associated with increased LPL activity in white adipose tissue. Thus, when hepatic receptor-mediated clearance is absent, apoC-III inhibits LPL activity as the alternative mechanism. ApoC-III ASO treatment in Apoe-/-Ndst1f/fAlb-Cre+ double-deficient mice, LPL activity measurement in adipose tissue, hepatic VLDL production assays, clinical data correlation with APOE isoform genotype Journal of lipid research High 31092690
2019 ApoC-III glycoforms are differentially cleared by distinct hepatic TRL receptors: HSPG preferentially clears the disialylated glycoform (apoC-III2), while LDLR/LRP1 more effectively clears the monosialylated glycoform (apoC-III1). ApoC-III2 is cleared more rapidly in HSPG-deficient mice; the relative abundance of apoC-III2 versus apoC-III1 shifts after volanesorsen treatment, and the decrease in apoC-III1 correlates with improved TG levels. Human TRL injection into wild-type, HSPG-deficient, and LDLR/LRP1-double-deficient mice; pharmacokinetic analysis; mass spectrometry of apoC-III glycoforms in patient plasma before and after volanesorsen Arteriosclerosis, thrombosis, and vascular biology High 31390883
2019 In APOC3 R19X null mutation heterozygotes, reduced apoC-III (49% lower) leads to higher fractional clearance rates of VLDL-TG and VLDL-apoB100 (not lower production rates), and accelerated conversion of VLDL remnants to LDL. Direct hepatic removal of VLDL remnants does not differ from non-carriers. apoC-III production rate is lower in carriers, and both apoC-III and apoC-II FCRs are higher. Stable isotope kinetic studies (VLDL-TG, apoB100, apoC-III, apoC-II turnover) in R19X heterozygotes vs. unaffected siblings Arteriosclerosis, thrombosis, and vascular biology High 30580564
2021 ApoC-III induces calcification in human aortic valve cells via a mitochondrial dysfunction/inflammation-mediated pathway. ApoC-III protein is enriched in fibrotic and calcific valve tissue, localizes in the calcification-prone fibrosa layer, and directly promotes calcification of primary human valvular interstitial cells in culture. Proteomics and immunohistochemistry of human aortic valve tissues (calcific vs. non-calcific), primary human valvular cell culture with recombinant apoC-III, calcification assays The Journal of biological chemistry Medium 33334888
2021 Guanidinylation of ApoC3 (gApoC3) is a post-translational modification occurring in CKD patients, driven by guanidine and urea. gApoC3 augments the proinflammatory effects of ApoC3 in monocytes in vitro, promotes kidney fibrosis, and impedes vascular regeneration in humanized mouse models of kidney injury and vascular injury. Mass spectrometry of ApoC3 from CKD patients vs. healthy individuals, in vitro guanidinylation, monocyte culture assays, humanized mouse models (UUO kidney fibrosis and vascular injury), 2D-proteomic analysis in adenine-diet CKD mice Journal of the American Society of Nephrology Medium 34588185
2022 Genetic reduction of apoC-III via loss-of-function mutations accelerates lipolysis of TG-rich lipoproteins and increases removal of VLDL remnants without altering production rates of chylomicrons (apoB48), VLDL1, VLDL2, or LDL-apoB100 in the postprandial state. Concentrations of VLDL1, VLDL2, and IDL particles are substantially reduced. Stable isotope kinetic studies of apoB48 and apoB100 in chylomicrons, VLDL1, VLDL2, IDL, and LDL in APOC3 LOF mutation carriers vs. non-carriers in the postprandial state JCI insight High 36040803
2019 ApoC-III inhibits intestinal basolateral lipid substrate transport (BLST): primary murine enteroids can take up TAG from TRLs on their basolateral surface, and excess apoC-III on TRLs inhibits this uptake. When apoC-III is high or basolateral substrates are absent, dietary TAG is diverted from cytosolic lipid droplets toward mitochondrial fatty acid oxidation, reducing chylomicron secretion. Primary murine enteroid cultures, basolateral TRL uptake assays, Seahorse mitochondrial respiration analysis, apoC-III transgenic mice (in vivo) Journal of lipid research Medium 31152000
2024 ApoC3 promotes NLRP3 inflammasome-mediated pyroptosis of macrophages in acute lung injury via mitochondrial damage, calcium-dependent ROS production, and activation of the SCIMP-SYK pathway. ApoC3 increases SCIMP expression and facilitates the SCIMP-SYK interaction; inhibition of pyroptosis or ROS mitigates the effects. METTL3 mediates m6A mRNA modification of ApoC3. LPS/ATP macrophage ALI models (in vitro and in vivo), ApoC3 knockdown and overexpression, recombinant ApoC3 protein treatment, NLRP3 inflammasome readouts, pyroptosis/ROS inhibitors, Co-IP for SCIMP-SYK interaction, METTL3 m6A analysis International immunopharmacology Medium 38232538
1979 ApoC-III binds to phosphatidylcholine bilayers in the head-group region and exhibits lateral mobility dependent on bilayer lipid phase state. The lateral diffusion coefficient transitions at ~30-35°C in DPPC bilayers consistent with the gel-to-liquid crystalline transition. ApoC-III binding mediates reversible vesicle aggregation at ~33°C but does not affect the gel-to-liquid phase transition itself. Fluorescence recovery after photobleaching (FRAP) of fluorescein-labeled ApoC-III in multilamellar bilayers (DPPC, egg PC, egg PC/cholesterol), light scattering, fluorescence polarization Proceedings of the National Academy of Sciences of the United States of America Medium 293667
2009 Increasing the apoC-III content in reconstituted HDL (rHDL) produces smaller particles with fewer apoA-I molecules, enhances surfactant-like properties, and reduces LCAT activation ability; however, CE transfer ability is not decreased. ApoC-III-containing rHDL aggravates MDA production in cell culture and increases LDL uptake by cells. Reconstitution of HDL particles with varying apoA-I:apoC-III molar ratios, particle size analysis, LCAT activation assay, CE transfer assay, MDA production assay, cellular LDL uptake assay Molecules and cells Medium 19326075
2005 Apoc3 deficiency prevents apoE4-induced hyperlipidemia in a gene-dose-dependent manner: complete Apoc3 knockout normalizes TG and TC in apoE4-overexpressing mice (TG from 57.2 to 1.5 mM), while heterozygous knockout provides intermediate protection. The mechanism involves alleviating apoE-induced inhibition of VLDL-TG hydrolysis: apoC-III is shown to be a more specific LPL inhibitor than apoE. ApoC-III deficiency increases fatty acid uptake from VLDL-like particles by white adipose tissue (enhanced LPL activity), despite a 10-fold increase in hepatic VLDL-TG production. Adenoviral apoE4 overexpression in Apoe-/-, Apoe-/-.Apoc3+/-, Apoe-/-.Apoc3-/- mice; TG production rate (Triton WR-1339), fatty acid uptake in adipose tissue, in vitro LPL inhibition assays with purified apoC-III and apoE Journal of lipid research High 15863838
2016 APOC3 induces endothelial dysfunction through upregulation of TNF-α, which increases JAM-1 expression, disrupting tight junctions between HUVECs. This promotes platelet assembly, leukocyte exudation, and THP-1 cell adhesion to endothelial cells. siRNA knockdown of TNF-α or JAM-1 mitigates these APOC3-induced effects. HUVEC culture with recombinant APOC3, ELISA, qRT-PCR, immunofluorescence, flow cytometry, transwell assays, siRNA knockdown of TNF-α and JAM-1 Lipids in health and disease Medium 27619170

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2014 Loss-of-function mutations in APOC3, triglycerides, and coronary disease. The New England journal of medicine 898 24941081
2014 Loss-of-function mutations in APOC3 and risk of ischemic vascular disease. The New England journal of medicine 788 24941082
2008 A null mutation in human APOC3 confers a favorable plasma lipid profile and apparent cardioprotection. Science (New York, N.Y.) 575 19074352
1992 Mechanism of hypertriglyceridemia in human apolipoprotein (apo) CIII transgenic mice. Diminished very low density lipoprotein fractional catabolic rate associated with increased apo CIII and reduced apo E on the particles. The Journal of clinical investigation 428 1430212
2014 Targeting APOC3 in the familial chylomicronemia syndrome. The New England journal of medicine 399 25470695
1992 Transcriptional regulation of human apolipoprotein genes ApoB, ApoCIII, and ApoAII by members of the steroid hormone receptor superfamily HNF-4, ARP-1, EAR-2, and EAR-3. The Journal of biological chemistry 285 1639815
2004 Foxo1 mediates insulin action on apoC-III and triglyceride metabolism. The Journal of clinical investigation 241 15546000
2016 ApoC-III inhibits clearance of triglyceride-rich lipoproteins through LDL family receptors. The Journal of clinical investigation 214 27400128
2019 N-acetyl galactosamine-conjugated antisense drug to APOC3 mRNA, triglycerides and atherogenic lipoprotein levels. European heart journal 200 31329855
2024 Plozasiran, an RNA Interference Agent Targeting APOC3, for Mixed Hyperlipidemia. The New England journal of medicine 171 38804517
2002 Identification of Rev-erbalpha as a physiological repressor of apoC-III gene transcription. Journal of lipid research 151 12454280
1994 Transcriptional regulation of the apoC-III gene by insulin in diabetic mice: correlation with changes in plasma triglyceride levels. Journal of lipid research 145 7868970
2020 The Roles of ApoC-III on the Metabolism of Triglyceride-Rich Lipoproteins in Humans. Frontiers in endocrinology 142 32849270
2024 Plozasiran (ARO-APOC3) for Severe Hypertriglyceridemia: The SHASTA-2 Randomized Clinical Trial. JAMA cardiology 138 38583092
2001 Association of the Sst-I polymorphism at the APOC3 gene locus with variations in lipid levels, lipoprotein subclass profiles and coronary heart disease risk: the Framingham offspring study. Atherosclerosis 103 11500189
1984 Isolation and sequence analysis of the human apolipoprotein CIII gene and the intergenic region between the apo AI and apo CIII genes. DNA (Mary Ann Liebert, Inc.) 101 6439535
1990 Promoter elements and factors required for hepatic and intestinal transcription of the human ApoCIII gene. The Journal of biological chemistry 95 2161843
2017 A human APOC3 missense variant and monoclonal antibody accelerate apoC-III clearance and lower triglyceride-rich lipoprotein levels. Nature medicine 93 28825717
2004 ApoC-I and ApoC-III as potential plasmatic markers to distinguish between ischemic and hemorrhagic stroke. Proteomics 92 15274118
1992 Polymorphisms in the apolipoprotein (apo) AI-CIII-AIV gene cluster: detection of genetic variation determining plasma apo AI, apo CIII and apo AIV concentrations. Human genetics 92 1740321
2011 Missense mutation in APOC3 within the C-terminal lipid binding domain of human ApoC-III results in impaired assembly and secretion of triacylglycerol-rich very low density lipoproteins: evidence that ApoC-III plays a major role in the formation of lipid precursors within the microsomal lumen. The Journal of biological chemistry 90 21676879
1991 Variation at the apo AI/CIII/AIV gene complex is associated with elevated plasma levels of apo CIII. Atherosclerosis 89 1906714
1996 Further characterization of the metabolic properties of triglyceride-rich lipoproteins from human and mouse apoC-III transgenic mice. Journal of lipid research 85 8864964
1999 ApoCIII gene variants modulate postprandial response to both glucose and fat tolerance tests. Circulation 82 10199885
2019 Effects of APOC3 Heterozygous Deficiency on Plasma Lipid and Lipoprotein Metabolism. Arteriosclerosis, thrombosis, and vascular biology 79 30580564
2019 Emerging Evidence that ApoC-III Inhibitors Provide Novel Options to Reduce the Residual CVD. Current atherosclerosis reports 77 31111320
2002 Associations of LPL and APOC3 gene polymorphisms on plasma lipids in a Mediterranean population: interaction with tobacco smoking and the APOE locus. Journal of lipid research 71 11893778
1997 Common genomic variation in the APOC3 promoter associated with variation in plasma lipoproteins. Arteriosclerosis, thrombosis, and vascular biology 70 9409252
1988 DNA polymorphism haplotypes of the human apolipoprotein APOA1-APOC3-APOA4 gene cluster. Human genetics 70 2903847
1985 Isolation and characterization of cDNA clones corresponding to two different human apoC-III alleles. Journal of lipid research 70 2989400
2006 Associations among race/ethnicity, ApoC-III genotypes, and lipids in HIV-1-infected individuals on antiretroviral therapy. PLoS medicine 67 16417409
2022 Broadening the Scope of Dyslipidemia Therapy by Targeting APOC3 (Apolipoprotein C3) and ANGPTL3 (Angiopoietin-Like Protein 3). Arteriosclerosis, thrombosis, and vascular biology 66 36579649
2011 The APOC3 T-455C and C-482T promoter region polymorphisms are not associated with the severity of liver damage independently of PNPLA3 I148M genotype in patients with nonalcoholic fatty liver. Journal of hepatology 66 21777557
2010 Regulation of hepatic ApoC3 expression by PGC-1β mediates hypolipidemic effect of nicotinic acid. Cell metabolism 65 20889132
1989 A regulatory element in the ApoCIII promoter that directs hepatic specific transcription binds to proteins in expressing and nonexpressing cell types. The Journal of biological chemistry 60 2777781
2002 ApoC-III gene polymorphisms and risk of coronary artery disease. Journal of lipid research 58 12235176
2013 A gene variant of PNPLA3, but not of APOC3, is associated with histological parameters of NAFLD in an obese population. Obesity (Silver Spring, Md.) 57 23512881
2015 Aggravated restenosis and atherogenesis in ApoCIII transgenic mice but lack of protection in ApoCIII knockouts: the effect of authentic triglyceride-rich lipoproteins with and without ApoCIII. Cardiovascular research 56 26160324
2017 The impact of APOA5, APOB, APOC3 and ABCA1 gene polymorphisms on ischemic stroke: Evidence from a meta-analysis. Atherosclerosis 55 28865324
2010 Functional analysis of the missense APOC3 mutation Ala23Thr associated with human hypotriglyceridemia. Journal of lipid research 54 20097930
2009 Synthesis of reconstituted high density lipoprotein (rHDL) containing apoA-I and apoC-III: the functional role of apoC-III in rHDL. Molecules and cells 54 19326075
2017 Lycopene amends LPS induced oxidative stress and hypertriglyceridemia via modulating PCSK-9 expression and Apo-CIII mediated lipoprotein lipase activity. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie 51 29174038
1990 Intracellular modification of human apolipoprotein AII (apoAII) and sites of apoAII mRNA synthesis: comparison of apoAII with apoCII and apoCIII isoproteins. Biochemistry 51 2108716
2019 ApoC-III ASO promotes tissue LPL activity in the absence of apoE-mediated TRL clearance. Journal of lipid research 49 31092690
2005 APOC3/A5 haplotypes, lipid levels, and risk of myocardial infarction in the Central Valley of Costa Rica. Journal of lipid research 49 16192625
1995 Complex interactions between SP1 bound to multiple distal regulatory sites and HNF-4 bound to the proximal promoter lead to transcriptional activation of liver-specific human APOCIII gene. Biochemistry 49 7640286
2006 Evidence for a complex relationship between apoA-V and apoC-III in patients with severe hypertriglyceridemia. Journal of lipid research 48 16861622
1999 Binding specificity and modulation of the human ApoCIII promoter activity by heterodimers of ligand-dependent nuclear receptors. Biochemistry 48 9893992
2021 Pharmacological Inhibition of CETP (Cholesteryl Ester Transfer Protein) Increases HDL (High-Density Lipoprotein) That Contains ApoC3 and Other HDL Subspecies Associated With Higher Risk of Coronary Heart Disease. Arteriosclerosis, thrombosis, and vascular biology 45 34937388
2015 Decreased expression of the APOA1-APOC3-APOA4 gene cluster is associated with risk of Alzheimer's disease. Drug design, development and therapy 45 26491253
2012 Genetic variation in PNPLA3 but not APOC3 influences liver fat in non-alcoholic fatty liver disease. Journal of gastroenterology and hepatology 44 22141340
2020 ApoCIII: A multifaceted protein in cardiometabolic disease. Metabolism: clinical and experimental 42 33058850
2003 The study of APOA1, APOC3 and APOA4 variability in healthy ageing people reveals another paradox in the oldest old subjects. Annals of human genetics 42 12556235
1999 Mitogen-activated protein kinase regulates transcription of the ApoCIII gene. Involvement of the orphan nuclear receptor HNF4. The Journal of biological chemistry 42 10551874
2024 Apolipoprotein C3 (ApoC3) facilitates NLRP3 mediated pyroptosis of macrophages through mitochondrial damage by accelerating of the interaction between SCIMP and SYK pathway in acute lung injury. International immunopharmacology 41 38232538
2021 ApoC-III is a novel inducer of calcification in human aortic valves. The Journal of biological chemistry 41 33334888
2017 ApoCIII as a Cardiovascular Risk Factor and Modulation by the Novel Lipid-Lowering Agent Volanesorsen. Current atherosclerosis reports 41 29124482
2000 SMAD proteins transactivate the human ApoCIII promoter by interacting physically and functionally with hepatocyte nuclear factor 4. The Journal of biological chemistry 38 10995777
1987 Molecular cloning of a human apoC-III variant: Thr 74----Ala 74 mutation prevents O-glycosylation. Journal of lipid research 38 3123586
1997 The apolipoprotein A-I/C-III/A-IV gene cluster: ApoC-III and ApoA-IV expression is regulated by two common enhancers. Biochimica et biophysica acta 37 9366246
1979 Lateral mobility of an amphipathic apolipoprotein, ApoC-III, bound to phosphatidylcholine bilayers with and without cholesterol. Proceedings of the National Academy of Sciences of the United States of America 37 293667
2008 ApoE epsilon2/epsilon3/epsilon4 polymorphism, ApoC-III/ApoE ratio and metabolic syndrome. Clinical and experimental medicine 36 18188530
2007 Association between the -455T>C promoter polymorphism of the APOC3 gene and the metabolic syndrome in a multi-ethnic sample. BMC medical genetics 36 18096054
2000 Gender related association between genetic variations of APOC-III gene and lipid and lipoprotein variables in northern France. Atherosclerosis 36 10781646
1994 Apo CIII gene transcription is regulated by a cytokine inducible NF-kappa B element. Nucleic acids research 36 8036173
1988 Mutagenesis of the glycosylation site of human ApoCIII. O-linked glycosylation is not required for ApoCIII secretion and lipid binding. The Journal of biological chemistry 36 3192519
2025 Targeting APOC3 with Olezarsen in Moderate Hypertriglyceridemia. The New England journal of medicine 35 40888739
1992 Characterization of the mouse apolipoprotein Apoa-1/Apoc-3 gene locus: genomic, mRNA, and protein sequences with comparisons to other species. Genomics 35 1478650
2016 Interactions of Environmental Factors and APOA1-APOC3-APOA4-APOA5 Gene Cluster Gene Polymorphisms with Metabolic Syndrome. PloS one 34 26824674
2023 Advances in Dyslipidaemia Treatments: Focusing on ApoC3 and ANGPTL3 Inhibitors. Journal of lipid and atherosclerosis 33 38299167
2024 Drug-target Mendelian randomization analysis supports lowering plasma ANGPTL3, ANGPTL4, and APOC3 levels as strategies for reducing cardiovascular disease risk. European heart journal open 32 38895109
2018 APOC-III Antisense Oligonucleotides: A New Option for the Treatment of Hypertriglyceridemia. Current medicinal chemistry 32 28595549
2003 Plasma turnover of HDL apoC-I, apoC-III, and apoE in humans: in vivo evidence for a link between HDL apoC-III and apoA-I metabolism. Journal of lipid research 32 12867543
2003 Interaction between the APOC3 gene promoter polymorphisms, saturated fat intake and plasma lipoproteins. Atherosclerosis 32 14612212
2024 APOC3 siRNA and ASO therapy for dyslipidemia. Current opinion in endocrinology, diabetes, and obesity 31 38334488
2006 Longitudinal analysis of haplotypes and polymorphisms of the APOA5 and APOC3 genes associated with variation in serum triglyceride levels: the Bogalusa Heart Study. Metabolism: clinical and experimental 31 17142127
2019 ApoC-III Glycoforms Are Differentially Cleared by Hepatic TRL (Triglyceride-Rich Lipoprotein) Receptors. Arteriosclerosis, thrombosis, and vascular biology 30 31390883
2018 New medications targeting triglyceride-rich lipoproteins: Can inhibition of ANGPTL3 or apoC-III reduce the residual cardiovascular risk? Atherosclerosis 30 29544086
2016 Targeting ApoC-III to Reduce Coronary Disease Risk. Current atherosclerosis reports 30 27443326
2007 Allelic variation in ApoC3, ApoA5 and LPL genes and first and second generation antipsychotic effects on serum lipids in patients with schizophrenia. The pharmacogenomics journal 30 17726453
2015 Associations of the APOC3 rs5128 polymorphism with plasma APOC3 and lipid levels: a meta-analysis. Lipids in health and disease 29 25928461
2000 A hormone response element in the human apolipoprotein CIII (ApoCIII) enhancer is essential for intestinal expression of the ApoA-I and ApoCIII genes and contributes to the hepatic expression of the two linked genes in transgenic mice. The Journal of biological chemistry 29 10893424
2021 APOC3 genetic variation, serum triglycerides, and risk of coronary artery disease in Asian Indians, Europeans, and other ethnic groups. Lipids in health and disease 28 34548093
1991 Purification and characterization of a heat stable nuclear factor CIIIB1 involved in the regulation of the human ApoC-III gene. The Journal of biological chemistry 28 2033057
1994 Electrophoretic screening for genetic variation in apolipoprotein C-III: identification of a novel apoC-III variant, apoC-III(Asp45-->Asn), in a Turkish patient. Journal of lipid research 27 7989867
2006 Susceptibility to type 1 diabetes is associated with ApoCIII gene haplotypes. Diabetes 26 16505251
2022 Postprandial metabolism of apolipoproteins B48, B100, C-III, and E in humans with APOC3 loss-of-function mutations. JCI insight 25 36040803
2021 Guanidinylated Apolipoprotein C3 (ApoC3) Associates with Kidney and Vascular Injury. Journal of the American Society of Nephrology : JASN 25 34588185
2016 APOC3 induces endothelial dysfunction through TNF-α and JAM-1. Lipids in health and disease 24 27619170
2007 Association between plasma lipid parameters and APOC3 genotypes in Brazilian subjects: effect of gender, smoking and APOE genotypes. Clinica chimica acta; international journal of clinical chemistry 24 17367769
2019 Intestinal basolateral lipid substrate transport is linked to chylomicron secretion and is regulated by apoC-III. Journal of lipid research 23 31152000
2017 Increased hepatic mitochondrial FA oxidation reduces plasma and liver TG levels and is associated with regulation of UCPs and APOC-III in rats. Journal of lipid research 23 28473603
2016 Metabolic Characterization of a Rare Genetic Variation Within APOC3 and Its Lipoprotein Lipase-Independent Effects. Circulation. Cardiovascular genetics 23 27114411
2016 An APOC3 3'UTR variant associated with plasma triglycerides levels and coronary heart disease by creating a functional miR-4271 binding site. Scientific reports 23 27624799
2005 ApoC-III deficiency prevents hyperlipidemia induced by apoE overexpression. Journal of lipid research 23 15863838
2000 Severe hypertriglyceridaemia in Type II diabetes: involvement of apoC-III Sst-I polymorphism, LPL mutations and apo E3 deficiency. Diabetologia 23 11126401
1998 Transactivation of the ApoCIII promoter by ATF-2 and repression by members of the Jun family. Biochemistry 23 9760243
2008 Birth weight and blood lipid levels in Spanish adolescents: influence of selected APOE, APOC3 and PPARgamma2 gene polymorphisms. The AVENA Study. BMC medical genetics 22 19000312
2006 Use of Intralipid for kinetic analysis of HDL apoC-III: evidence for a homogeneous kinetic pool of apoC-III in plasma. Journal of lipid research 22 16556931
2016 Very low-depth sequencing in a founder population identifies a cardioprotective APOC3 signal missed by genome-wide imputation. Human molecular genetics 21 27146844

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