Component

Acetyl-L-carnitine

Acetyl-L-carnitine. Species, exposure and limitations are retained in each linked claim.

18 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

Read recorded mechanisms Open recursive mind map

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What it acts on

  1. Isotope-labeled acetylcarnitine supplied acetyl-CoA and fatty-acid carbon in glucose-limited human U87MG glioma cells.

    Acetyl-L-carnitine → Human U87MG acetyl-CoA labeling from acetylcarnitine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human U87MG culture, isotope tracing.
    limitations
    Does not show that oral acetylcarnitine causes or treats cancer.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    The acetylated form can deliver carbon for cellular synthesis.
    primary_references
    Carnitine octanoyltransferase is important for the assimilation of exogenous acetyl-L-carnitine into acetyl-CoA in mammalian cells. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36587768/ · DOI 10.1016/j.jbc.2022.102848

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 210–216

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human U87MG culture, isotope tracing. · source_derived_draft · unverified_draft

    ## l-carnitine-acetyl-carbon The acetylated form can deliver carbon for cellular synthesis. Isotope-labeled acetylcarnitine supplied acetyl-CoA and fatty-acid carbon in glucose-limited human U87MG glioma cells. Model: Human U87MG culture, isotope tracing. Limitations: Does not show that oral acetylcarnitine causes or treats cancer. Evidence access: Primary abstract Carnitine octanoyltransferase is important for the assimilation of exogenous acetyl-L-carnitine into acetyl-CoA in mammalian cells. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36587768/ · DOI 10.1016/j.jbc.2022.102848
    Complete structured claim and evidence

  2. At 24 weeks in the same taxane trial, the acetyl-L-carnitine arm had worse neuropathy scores and more severe neurotoxicity than placebo.

    Acetyl-L-carnitine → Human taxane-associated peripheral neuropathy severity source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Same randomized trial; prespecified secondary follow-up.
    limitations
    Not a demonstrated molecular explanation of the harm; keep the clinical outcome visible.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    Longer follow-up revealed harm in that setting.
    primary_references
    Randomized double-blind placebo-controlled trial of acetyl-L-carnitine for the prevention of taxane-induced neuropathy in women undergoing adjuvant breast cancer therapy. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23733756/ · DOI 10.1200/JCO.2012.44.8738

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 338–344

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Same randomized trial; prespecified secondary follow-up. · source_derived_draft · unverified_draft

    ## l-carnitine-alc-neuropathy-harm Longer follow-up revealed harm in that setting. At 24 weeks in the same taxane trial, the acetyl-L-carnitine arm had worse neuropathy scores and more severe neurotoxicity than placebo. Model: Same randomized trial; prespecified secondary follow-up. Limitations: Not a demonstrated molecular explanation of the harm; keep the clinical outcome visible. Evidence access: Primary abstract Randomized double-blind placebo-controlled trial of acetyl-L-carnitine for the prevention of taxane-induced neuropathy in women undergoing adjuvant breast cancer therapy. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23733756/ · DOI 10.1200/JCO.2012.44.8738
    Complete structured claim and evidence

  3. In a 409-patient randomized trial during adjuvant taxane chemotherapy, acetyl-L-carnitine did not significantly improve the primary 12-week neuropathy endpoint.

    Acetyl-L-carnitine → Human taxane-associated peripheral neuropathy severity source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Women with breast cancer; 3 g/day acetyl-L-carnitine versus placebo.
    limitations
    A finding for this derivative and treatment context, not every carnitine use.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    A plausible nerve-protection idea failed its main clinical test.
    primary_references
    Randomized double-blind placebo-controlled trial of acetyl-L-carnitine for the prevention of taxane-induced neuropathy in women undergoing adjuvant breast cancer therapy. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23733756/ · DOI 10.1200/JCO.2012.44.8738

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 330–336

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Women with breast cancer; 3 g/day acetyl-L-carnitine versus placebo. · source_derived_draft · unverified_draft

    ## l-carnitine-alc-neuropathy-null A plausible nerve-protection idea failed its main clinical test. In a 409-patient randomized trial during adjuvant taxane chemotherapy, acetyl-L-carnitine did not significantly improve the primary 12-week neuropathy endpoint. Model: Women with breast cancer; 3 g/day acetyl-L-carnitine versus placebo. Limitations: A finding for this derivative and treatment context, not every carnitine use. Evidence access: Primary abstract Randomized double-blind placebo-controlled trial of acetyl-L-carnitine for the prevention of taxane-induced neuropathy in women undergoing adjuvant breast cancer therapy. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23733756/ · DOI 10.1200/JCO.2012.44.8738
    Complete structured claim and evidence

  4. Acetyl-L-carnitine treatment increased Grm2-associated H3K27 acetylation and mGlu2 expression in Flinders Sensitive Line rats.

    Acetyl-L-carnitine → Rat hippocampal and prefrontal Grm2-associated acetylation source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Rat depression-model hippocampus and prefrontal cortex.
    limitations
    Histone acetylation differs from DNA methylation; this is not proof of human antidepressant efficacy.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    The acetylated form altered a glutamate-signaling pathway in a rodent model.
    primary_references
    L-acetylcarnitine causes rapid antidepressant effects through the epigenetic induction of mGlu2 receptors. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23382250/ · DOI 10.1073/pnas.1216100110

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 314–320

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Rat depression-model hippocampus and prefrontal cortex. · source_derived_draft · unverified_draft

    ## l-carnitine-brain-acetylation The acetylated form altered a glutamate-signaling pathway in a rodent model. Acetyl-L-carnitine treatment increased Grm2-associated H3K27 acetylation and mGlu2 expression in Flinders Sensitive Line rats. Model: Rat depression-model hippocampus and prefrontal cortex. Limitations: Histone acetylation differs from DNA methylation; this is not proof of human antidepressant efficacy. Evidence access: Primary abstract L-acetylcarnitine causes rapid antidepressant effects through the epigenetic induction of mGlu2 receptors. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23382250/ · DOI 10.1073/pnas.1216100110
    Complete structured claim and evidence

  5. Adding acetylcarnitine increased histone acetylation in lipid-depleted mouse HCC cells lacking both ACLY and ACSS2.

    Acetyl-L-carnitine → Mouse HCC-cell histone acetylation source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full-text Figure 6 and cell-line methods
    experimental_model
    Mouse hepatocellular carcinoma double-knockout cells; supplementation and isotope tracing.
    limitations
    An engineered cancer-cell bypass is not a general epigenetic benefit.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    Acetyl-group transport can connect energy metabolism to chromatin chemistry.
    primary_references
    Acetylcarnitine shuttling links mitochondrial metabolism to histone acetylation and lipogenesis. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37134161/ · DOI 10.1126/sciadv.adf0115

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 234–240

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Mouse hepatocellular carcinoma double-knockout cells; supplementation and isotope tracing. · source_derived_draft · unverified_draft

    ## l-carnitine-histone-carbon Acetyl-group transport can connect energy metabolism to chromatin chemistry. Adding acetylcarnitine increased histone acetylation in lipid-depleted mouse HCC cells lacking both ACLY and ACSS2. Model: Mouse hepatocellular carcinoma double-knockout cells; supplementation and isotope tracing. Limitations: An engineered cancer-cell bypass is not a general epigenetic benefit. Evidence access: Primary full-text Figure 6 and cell-line methods Acetylcarnitine shuttling links mitochondrial metabolism to histone acetylation and lipogenesis. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37134161/ · DOI 10.1126/sciadv.adf0115
    Complete structured claim and evidence

What acts on it

  1. Muscle Crat deletion reduced short-chain acyltransferase activity and acetylcarnitine pools, supporting transfer of acetyl groups from acetyl-CoA to carnitine.

    Mouse carnitine acetyltransferase / Crat → Acetyl-L-carnitine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract and full-text Figures 1-4
    experimental_model
    Muscle-specific mouse knockout, enzyme assays and metabolomics.
    limitations
    Crat buffer function depends on tissue and substrate conditions.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    Carnitine can carry excess acetyl groups as well as long fatty-acid groups.
    primary_references
    Muscle-specific deletion of carnitine acetyltransferase compromises glucose tolerance and metabolic flexibility. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22560225/ · DOI 10.1016/j.cmet.2012.04.005

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 154–160

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Muscle-specific mouse knockout, enzyme assays and metabolomics. · source_derived_draft · unverified_draft

    ## l-carnitine-crat-buffer Carnitine can carry excess acetyl groups as well as long fatty-acid groups. Muscle Crat deletion reduced short-chain acyltransferase activity and acetylcarnitine pools, supporting transfer of acetyl groups from acetyl-CoA to carnitine. Model: Muscle-specific mouse knockout, enzyme assays and metabolomics. Limitations: Crat buffer function depends on tissue and substrate conditions. Evidence access: Primary abstract and full-text Figures 1-4 Muscle-specific deletion of carnitine acetyltransferase compromises glucose tolerance and metabolic flexibility. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22560225/ · DOI 10.1016/j.cmet.2012.04.005
    Complete structured claim and evidence

  2. Purified recombinant human CRAT transferred short-chain acyl groups including acetyl from acyl-CoA substrates to carnitine in enzyme assays.

    Human carnitine acetyltransferase / CRAT → Acetyl-L-carnitine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full-text Table 1 and recombinant enzyme methods
    experimental_model
    Human CRAT expressed in E. coli; steady-state kinetic substrate panel.
    limitations
    Purified-enzyme capacity does not identify the dominant flux in every compartment.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    The human enzyme directly connects carnitine and the CoA pool.
    primary_references
    Carnitine octanoyltransferase is important for the assimilation of exogenous acetyl-L-carnitine into acetyl-CoA in mammalian cells. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36587768/ · DOI 10.1016/j.jbc.2022.102848

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 498–504

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human CRAT expressed in E. coli; steady-state kinetic substrate panel. · source_derived_draft · unverified_draft

    ## l-carnitine-human-crat-reaction The human enzyme directly connects carnitine and the CoA pool. Purified recombinant human CRAT transferred short-chain acyl groups including acetyl from acyl-CoA substrates to carnitine in enzyme assays. Model: Human CRAT expressed in E. coli; steady-state kinetic substrate panel. Limitations: Purified-enzyme capacity does not identify the dominant flux in every compartment. Evidence access: Primary full-text Table 1 and recombinant enzyme methods Carnitine octanoyltransferase is important for the assimilation of exogenous acetyl-L-carnitine into acetyl-CoA in mammalian cells. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36587768/ · DOI 10.1016/j.jbc.2022.102848
    Complete structured claim and evidence

  3. Expressed human OCTN2 transported acetyl-L-carnitine in a sodium-dependent manner with a measured Km of 8.5 micromolar.

    Human carnitine transporter OCTN2 / SLC22A5 → Acetyl-L-carnitine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human OCTN2 in HEK293 cells.
    limitations
    A kinetic constant is not a treatment target.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    The transporter also carries the acetylated form.
    primary_references
    Na(+)-dependent carnitine transport by organic cation transporter (OCTN2): its pharmacological and toxicological relevance. · 1999 · https://pubmed.ncbi.nlm.nih.gov/10525100/
    transport_effect
    raises Sodium-dependent acetylcarnitine transport with a measured Km of 8.5 micromolar.
    transport_pool
    the expressing cell Sodium-dependent acetylcarnitine transport with a measured Km of 8.5 micromolar.

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 50–56

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human OCTN2 in HEK293 cells. · source_derived_draft · unverified_draft

    ## l-carnitine-octn2-acetyl The transporter also carries the acetylated form. Expressed human OCTN2 transported acetyl-L-carnitine in a sodium-dependent manner with a measured Km of 8.5 micromolar. Model: Human OCTN2 in HEK293 cells. Limitations: A kinetic constant is not a treatment target. Evidence access: Primary abstract Na(+)-dependent carnitine transport by organic cation transporter (OCTN2): its pharmacological and toxicological relevance. · 1999 · https://pubmed.ncbi.nlm.nih.gov/10525100/
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Carnitine repletion of doubly deficient HepG2 cells increased acetylcarnitine, propionylcarnitine and 3-hydroxyisovalerylcarnitine each by more than 50-fold.

    L-Carnitine → HepG2 acylcarnitine response to carnitine repletion source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    nutrient_deficiency Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/biotin-research/25527659.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4a368eb2fa2020bb1cabc99b31a3420870a8256886d5934d3d834c90b078238f", "start_char": 0, "end_char": 2372, "text_sha256": "4a368eb2fa2020bb1cabc99b31a3420870a8256886d5934d3d834c90b078238f"}
    experimental_model
    Two-factor biotin/carnitine depletion and carnitine repletion in human HepG2 cells
    exposure
    Separate and combined biotin and carnitine depletion
    limitations
    This is a cell-culture demonstration of marker masking; it does not validate a diagnostic correction formula in pregnancy or the general population.
    nutrient_topic
    Biotin research collection; topical membership is not evidence of a direct dietary effect. · Biotin
    organism
    Homo sapiens
    plain_language
    Restoring carnitine exposed the unresolved biotin-related bottleneck.
    primary_references
    [b7-p25527659] In HepG2 cells, coexisting carnitine deficiency masks important indicators of marginal biotin deficiency. (2015). https://pubmed.ncbi.nlm.nih.gov/25527659/ DOI: 10.3945/jn.114.201343
    tissue_or_cell_type
    HepG2 hepatoma cells
    trigger_kind
    nutrient_deficiency Imported condition classification; unverified.

    Biotin: carboxylases, recycling, deficiency and nutrient interactions (2026-09-17) · lines 975–986

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Two-factor biotin/carnitine depletion and carnitine repletion in human HepG2 cells · source_derived_draft · unverified_draft

    ### b7-carnitine-unmasking Carnitine repletion of doubly deficient HepG2 cells increased acetylcarnitine, propionylcarnitine and 3-hydroxyisovalerylcarnitine each by more than 50-fold. Condition category: nutrient_deficiency nutrient_topic: Biotin research collection; topical membership is not evidence of a direct dietary effect. plain_language: Restoring carnitine exposed the unresolved biotin-related bottleneck. organism: Homo sapiens tissue_or_cell_type: HepG2 hepatoma cells experimental_model: Two-factor biotin/carnitine depletion and carnitine repletion in human HepG2 cells limitations: This is a cell-culture demonstration of marker masking; it does not validate a diagnostic correction formula in pregnancy or the general population. exposure: Separate and combined biotin and carnitine depletion evidence_span: {"source_cache": "artifacts/biotin-research/25527659.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "4a368eb2fa2020bb1cabc99b31a3420870a8256886d5934d3d834c90b078238f", "start_char": 0, "end_char": 2372, "text_sha256": "4a368eb2fa2020bb1cabc99b31a3420870a8256886d5934d3d834c90b078238f"} [b7-p25527659] In HepG2 cells, coexisting carnitine deficiency masks important indicators of marginal biotin deficiency. (2015). https://pubmed.ncbi.nlm.nih.gov/25527659/ DOI: 10.3945/jn.114.201343
    Complete structured claim and evidence

  2. Acetyl-L-carnitine did not produce the reported behavioral benefit in mGlu2-knockout mice exposed to chronic unpredictable stress.

    Mouse metabotropic glutamate receptor 2 / Grm2 → Mouse stress-model behavioral response to acetylcarnitine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Mouse knockout and stress-behavior experiments.
    limitations
    Behavioral tests are not human depression outcomes.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    Removing the receptor tested whether the rodent effect depended on it.
    primary_references
    L-acetylcarnitine causes rapid antidepressant effects through the epigenetic induction of mGlu2 receptors. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23382250/ · DOI 10.1073/pnas.1216100110

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 322–328

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Mouse knockout and stress-behavior experiments. · source_derived_draft · unverified_draft

    ## l-carnitine-brain-receptor-required Removing the receptor tested whether the rodent effect depended on it. Acetyl-L-carnitine did not produce the reported behavioral benefit in mGlu2-knockout mice exposed to chronic unpredictable stress. Model: Mouse knockout and stress-behavior experiments. Limitations: Behavioral tests are not human depression outcomes. Evidence access: Primary abstract L-acetylcarnitine causes rapid antidepressant effects through the epigenetic induction of mGlu2 receptors. · 2013 · https://pubmed.ncbi.nlm.nih.gov/23382250/ · DOI 10.1073/pnas.1216100110
    Complete structured claim and evidence

  3. Purified rat mitochondrial CACT reconstituted into liposomes exchanged carnitine and transported acylcarnitines of several chain lengths.

    Rat carnitine-acylcarnitine translocase / Slc25a20 → L-Carnitine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Recombinant rat carrier and proteoliposomes.
    limitations
    Transport reconstitution is not a human flux measurement.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    A separate carrier moves the loaded molecule across the inner membrane.
    primary_references
    Bacterial overexpression, purification, and reconstitution of the carnitine/acylcarnitine carrier from rat liver mitochondria. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9731180/ · DOI 10.1006/bbrc.1998.9197

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 98–104

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Recombinant rat carrier and proteoliposomes. · source_derived_draft · unverified_draft

    ## l-carnitine-cact-exchange A separate carrier moves the loaded molecule across the inner membrane. Purified rat mitochondrial CACT reconstituted into liposomes exchanged carnitine and transported acylcarnitines of several chain lengths. Model: Recombinant rat carrier and proteoliposomes. Limitations: Transport reconstitution is not a human flux measurement. Evidence access: Primary abstract Bacterial overexpression, purification, and reconstitution of the carnitine/acylcarnitine carrier from rat liver mitochondria. · 1998 · https://pubmed.ncbi.nlm.nih.gov/9731180/ · DOI 10.1006/bbrc.1998.9197
    Complete structured claim and evidence

  4. Human CPT2 had activity with C8-C18 acyl-CoAs but virtually none with short-chain acyl-CoAs or branched-chain amino-acid oxidation intermediates.

    Human carnitine palmitoyltransferase 2 / CPT2 → Propionyl-CoA source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Recombinant human CPT2 substrate panel.
    limitations
    No claim that every acylcarnitine originates from CPT2.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    The long-chain shuttle is not the same enzyme system as short-chain buffering.
    primary_references
    Carnitine palmitoyltransferase 2: New insights on the substrate specificity and implications for acylcarnitine profiling. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20538056/ · DOI 10.1016/j.bbadis.2010.06.002

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 114–120

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human CPT2 substrate panel. · source_derived_draft · unverified_draft

    ## l-carnitine-cpt2-specificity The long-chain shuttle is not the same enzyme system as short-chain buffering. Human CPT2 had activity with C8-C18 acyl-CoAs but virtually none with short-chain acyl-CoAs or branched-chain amino-acid oxidation intermediates. Model: Recombinant human CPT2 substrate panel. Limitations: No claim that every acylcarnitine originates from CPT2. Evidence access: Primary abstract Carnitine palmitoyltransferase 2: New insights on the substrate specificity and implications for acylcarnitine profiling. · 2010 · https://pubmed.ncbi.nlm.nih.gov/20538056/ · DOI 10.1016/j.bbadis.2010.06.002
    Complete structured claim and evidence

  5. Silencing CRAT in primary human myotubes reduced acetylcarnitine export by 47%.

    Human carnitine acetyltransferase / CRAT → Human primary myotube acetylcarnitine export source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full-text Figure 6 and methods
    experimental_model
    Human myotubes; adenoviral silencing, approximately 60% lower enzyme activity.
    limitations
    Cell culture, not human supplementation.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    An independent enzyme controls acetyl-group export from muscle cells.
    primary_references
    Muscle-specific deletion of carnitine acetyltransferase compromises glucose tolerance and metabolic flexibility. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22560225/ · DOI 10.1016/j.cmet.2012.04.005

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 170–176

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human myotubes; adenoviral silencing, approximately 60% lower enzyme activity. · source_derived_draft · unverified_draft

    ## l-carnitine-crat-knockdown-export An independent enzyme controls acetyl-group export from muscle cells. Silencing CRAT in primary human myotubes reduced acetylcarnitine export by 47%. Model: Human myotubes; adenoviral silencing, approximately 60% lower enzyme activity. Limitations: Cell culture, not human supplementation. Evidence access: Primary full-text Figure 6 and methods Muscle-specific deletion of carnitine acetyltransferase compromises glucose tolerance and metabolic flexibility. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22560225/ · DOI 10.1016/j.cmet.2012.04.005
    Complete structured claim and evidence

  6. Silencing CRAT in human myotubes reduced glucose uptake by 13% while increasing oleate oxidation.

    Human carnitine acetyltransferase / CRAT → Human primary myotube glucose uptake source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full-text Figure 6
    experimental_model
    Primary human myotube loss-of-function experiment.
    limitations
    No universal reciprocal rule for all tissues.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    More fat oxidation did not mean better glucose handling in this experiment.
    primary_references
    Muscle-specific deletion of carnitine acetyltransferase compromises glucose tolerance and metabolic flexibility. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22560225/ · DOI 10.1016/j.cmet.2012.04.005

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 178–184

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Primary human myotube loss-of-function experiment. · source_derived_draft · unverified_draft

    ## l-carnitine-crat-knockdown-glucose More fat oxidation did not mean better glucose handling in this experiment. Silencing CRAT in human myotubes reduced glucose uptake by 13% while increasing oleate oxidation. Model: Primary human myotube loss-of-function experiment. Limitations: No universal reciprocal rule for all tissues. Evidence access: Primary full-text Figure 6 Muscle-specific deletion of carnitine acetyltransferase compromises glucose tolerance and metabolic flexibility. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22560225/ · DOI 10.1016/j.cmet.2012.04.005
    Complete structured claim and evidence

  7. Removing Crat impaired glucose-derived lipid synthesis in ACLY-deficient mouse HCC cells.

    Mouse carnitine acetyltransferase / Crat → Mouse HCC-cell glucose-derived lipid synthesis source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text and cell-line methods
    experimental_model
    Mouse HCC cell genetic perturbation and carbon tracing.
    limitations
    Dependence arises in the specified metabolic background.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    The acetyl shuttle can supply lipid synthesis when a usual route is missing.
    primary_references
    Acetylcarnitine shuttling links mitochondrial metabolism to histone acetylation and lipogenesis. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37134161/ · DOI 10.1126/sciadv.adf0115

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 242–248

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Mouse HCC cell genetic perturbation and carbon tracing. · source_derived_draft · unverified_draft

    ## l-carnitine-crat-lipogenesis The acetyl shuttle can supply lipid synthesis when a usual route is missing. Removing Crat impaired glucose-derived lipid synthesis in ACLY-deficient mouse HCC cells. Model: Mouse HCC cell genetic perturbation and carbon tracing. Limitations: Dependence arises in the specified metabolic background. Evidence access: Primary full text and cell-line methods Acetylcarnitine shuttling links mitochondrial metabolism to histone acetylation and lipogenesis. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37134161/ · DOI 10.1126/sciadv.adf0115
    Complete structured claim and evidence

  8. Deleting CRAT did not diminish acetyl-CoA labeling from supplied acetylcarnitine in U87MG cells.

    Human carnitine acetyltransferase / CRAT → Human U87MG acetyl-CoA labeling from acetylcarnitine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full-text Figure 4
    experimental_model
    Human U87MG knockout and tracer experiment.
    limitations
    Incoming acetylcarnitine utilization differs from mitochondrial production; not a conflict with muscle export.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    The enzyme needed to make acetylcarnitine need not be the one that uses it.
    primary_references
    Carnitine octanoyltransferase is important for the assimilation of exogenous acetyl-L-carnitine into acetyl-CoA in mammalian cells. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36587768/ · DOI 10.1016/j.jbc.2022.102848

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 226–232

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human U87MG knockout and tracer experiment. · source_derived_draft · unverified_draft

    ## l-carnitine-crat-null-assimilation The enzyme needed to make acetylcarnitine need not be the one that uses it. Deleting CRAT did not diminish acetyl-CoA labeling from supplied acetylcarnitine in U87MG cells. Model: Human U87MG knockout and tracer experiment. Limitations: Incoming acetylcarnitine utilization differs from mitochondrial production; not a conflict with muscle export. Evidence access: Primary full-text Figure 4 Carnitine octanoyltransferase is important for the assimilation of exogenous acetyl-L-carnitine into acetyl-CoA in mammalian cells. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36587768/ · DOI 10.1016/j.jbc.2022.102848
    Complete structured claim and evidence

  9. Deleting CROT reduced labeling of acetyl-CoA and palmitate from exogenous acetylcarnitine; CROT cDNA rescue restored acetyl-CoA labeling.

    Human carnitine octanoyltransferase / CROT → Human U87MG acetyl-CoA labeling from acetylcarnitine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full-text Figure 5 and enzyme assays
    experimental_model
    Human U87MG cells, CROT knockout and rescue; 1 mM tracer under glucose limitation.
    limitations
    Compartment and substrate supply may explain why this enzyme dominates in these cells.
    nutrient_topic
    L-Carnitine collection; isomer, preparation, species, exposure and manipulation remain explicit. · L-Carnitine
    plain_language
    Another carnitine enzyme provided this carbon route.
    primary_references
    Carnitine octanoyltransferase is important for the assimilation of exogenous acetyl-L-carnitine into acetyl-CoA in mammalian cells. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36587768/ · DOI 10.1016/j.jbc.2022.102848

    L-Carnitine: synthesis, acyl-group transport, fuel selection and nutrient interactions (2026-09-19) · lines 218–224

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human U87MG cells, CROT knockout and rescue; 1 mM tracer under glucose limitation. · source_derived_draft · unverified_draft

    ## l-carnitine-crot-knockout Another carnitine enzyme provided this carbon route. Deleting CROT reduced labeling of acetyl-CoA and palmitate from exogenous acetylcarnitine; CROT cDNA rescue restored acetyl-CoA labeling. Model: Human U87MG cells, CROT knockout and rescue; 1 mM tracer under glucose limitation. Limitations: Compartment and substrate supply may explain why this enzyme dominates in these cells. Evidence access: Primary full-text Figure 5 and enzyme assays Carnitine octanoyltransferase is important for the assimilation of exogenous acetyl-L-carnitine into acetyl-CoA in mammalian cells. · 2023 · https://pubmed.ncbi.nlm.nih.gov/36587768/ · DOI 10.1016/j.jbc.2022.102848
    Complete structured claim and evidence

  10. Acetate infusion increased muscle acetyl-CoA, citrate and acetylcarnitine, and resting active-form pyruvate dehydrogenase declined during 20 minutes of acetate infusion from 0.37 to 0.16 mmol per minute per kg wet weight, coinciding with an elevation in the acetyl-CoA to free CoA ratio from 0.28 to 0.73, whereas after the bicarbonate control infusion resting activity was similar to that before acetate.

    Intravenous sodium acetate infusion → Active-form pyruvate dehydrogenase in skeletal muscle source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/acetate-research/7762627.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "343ba052925b754982d178cee1a1c2e3e0a3d1e940e6dd349989c7d6c2704f76", "start_char": 0, "end_char": 1730, "text_sha256": "343ba052925b754982d178cee1a1c2e3e0a3d1e940e6dd349989c7d6c2704f76"}
    experimental_model
    Eight human subjects infused with sodium acetate at rest and during cycling, with muscle biopsies
    exposure
    400 mmol sodium acetate infused over 20 min rest, 5 min cycling at 40% and 15 min at 80% of maximal oxygen uptake, against a 400 mmol sodium bicarbonate control two weeks later
    limitations
    A direct human measurement with a matched sodium control. The effect was present at rest and absent during exercise, so it is not a general property of raised acetate.
    nutrient_topic
    Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. · Acetic acid
    organism
    Human
    plain_language
    Raising blood acetate in people switched down the enzyme that commits glucose to being burned.
    primary_references
    [acetate-p7762627] Skeletal muscle pyruvate dehydrogenase activity during acetate infusion in humans. (1995). https://pubmed.ncbi.nlm.nih.gov/7762627/ DOI: 10.1152/ajpendo.1995.268.5.e1007
    tissue_or_cell_type
    Skeletal muscle

    Acetic acid: the ingested acid, the receptors acetate binds, the acetyl-CoA it becomes, and the acetyl groups that reach histones (2026-09-21) · lines 485–496

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Eight human subjects infused with sodium acetate at rest and during cycling, with muscle biopsies · source_derived_draft · unverified_draft

    ### acetate-acetate-suppresses-pdh Acetate infusion increased muscle acetyl-CoA, citrate and acetylcarnitine, and resting active-form pyruvate dehydrogenase declined during 20 minutes of acetate infusion from 0.37 to 0.16 mmol per minute per kg wet weight, coinciding with an elevation in the acetyl-CoA to free CoA ratio from 0.28 to 0.73, whereas after the bicarbonate control infusion resting activity was similar to that before acetate. Condition category: normal nutrient_topic: Acetic acid research collection; topical membership is not evidence of a direct clinical effect, and the ingested acid is recorded separately from the circulating acetate anion. plain_language: Raising blood acetate in people switched down the enzyme that commits glucose to being burned. organism: Human tissue_or_cell_type: Skeletal muscle experimental_model: Eight human subjects infused with sodium acetate at rest and during cycling, with muscle biopsies limitations: A direct human measurement with a matched sodium control. The effect was present at rest and absent during exercise, so it is not a general property of raised acetate. exposure: 400 mmol sodium acetate infused over 20 min rest, 5 min cycling at 40% and 15 min at 80% of maximal oxygen uptake, against a 400 mmol sodium bicarbonate control two weeks later evidence_span: {"source_cache": "artifacts/acetate-research/7762627.abstract.txt", "locator": "Indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "343ba052925b754982d178cee1a1c2e3e0a3d1e940e6dd349989c7d6c2704f76", "start_char": 0, "end_char": 1730, "text_sha256": "343ba052925b754982d178cee1a1c2e3e0a3d1e940e6dd349989c7d6c2704f76"} [acetate-p7762627] Skeletal muscle pyruvate dehydrogenase activity during acetate infusion in humans. (1995). https://pubmed.ncbi.nlm.nih.gov/7762627/ DOI: 10.1152/ajpendo.1995.268.5.e1007
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards