Component

Mitochondria

Organelles containing respiratory and metabolic machinery.

8 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 acts on it

  1. G125S carrier constructs retained mitochondrial targeting despite impaired uptake.

    Human SLC25A19 G125S variant → Mitochondria source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence-scope
    HepG2 cells
    evidence_locator
    Abstract
    evidence_spans
    [{"source_document": "artifacts/thiamine_transport_sources/subramanian-2013-mitochondrial-uptake-source-record.json", "source_field": "resultList.result[0].abstractText", "start_char": 0, "end_char": 1750}]
    experimental_model
    Mouse liver mitochondria and human SLC25A19 constructs in HepG2 cells.
    limitations
    Imaging identifies organellar targeting; carrier is in the inner membrane, not soluble matrix.
    nutrient_topic
    Thiamine research collection; topical membership is not evidence of a direct dietary effect. · Thiamine (vitamin B1)
    organism
    Homo sapiens
    plain_language
    Reaching the correct organelle does not guarantee carrier function.
    primary_references
    [subramanian-2013-mitochondrial-uptake] Mitochondrial Uptake of Thiamin Pyrophosphate: Physiological and Cell Biological Aspects (2013). https://pmc.ncbi.nlm.nih.gov/articles/PMC3758298/ DOI: 10.1371/journal.pone.0073503
    spatial_context
    Mitochondrial localization of membrane carrier.
    tissue_or_cell_type
    HepG2 cells
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Thiamine: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 473–486

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Mouse liver mitochondria and human SLC25A19 constructs in HepG2 cells. · source_derived_draft · unverified_draft

    ### b1-slc25a19-g125s-targeting G125S carrier constructs retained mitochondrial targeting despite impaired uptake. Condition category: machinery_impairment nutrient_topic: Thiamine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Reaching the correct organelle does not guarantee carrier function. organism: Homo sapiens tissue_or_cell_type: HepG2 cells experimental_model: Mouse liver mitochondria and human SLC25A19 constructs in HepG2 cells. limitations: Imaging identifies organellar targeting; carrier is in the inner membrane, not soluble matrix. spatial_context: Mitochondrial localization of membrane carrier. evidence_spans: [{"source_document": "artifacts/thiamine_transport_sources/subramanian-2013-mitochondrial-uptake-source-record.json", "source_field": "resultList.result[0].abstractText", "start_char": 0, "end_char": 1750}] evidence_locator: Abstract evidence-scope: HepG2 cells [subramanian-2013-mitochondrial-uptake] Mitochondrial Uptake of Thiamin Pyrophosphate: Physiological and Cell Biological Aspects (2013). https://pmc.ncbi.nlm.nih.gov/articles/PMC3758298/ DOI: 10.1371/journal.pone.0073503
    Complete structured claim and evidence

  2. In vitro synthesized human FADS1 entered isolated rat liver mitochondria and was processed; transfected-cell imaging also localized it to mitochondria.

    Human FAD synthetase isoform 1 → Mitochondria source_derived_draftungraded
    Experimental context and source evidence
    evidence_location
    Abstract; mitochondrial import and confocal imaging
    experimental_model
    Import into purified rat liver mitochondria; BHK-21/Caco-2 confocal imaging
    exposure
    In vitro synthesized and transiently expressed human FADS1.
    limitations
    Construct/import evidence does not establish its abundance in every human tissue.
    nutrient_topic
    Riboflavin research collection; topical membership is not evidence of a direct dietary effect. · Riboflavin (vitamin B2)
    organism
    Human protein; rat mitochondria; hamster and human cells
    plain_language
    One FLAD1 isoform can provide FAD-synthesis machinery inside mitochondria.
    primary_references
    [transport-fads-localization-2010] Mitochondrial localization of human FAD synthetase isoform 1. (2010). https://pubmed.ncbi.nlm.nih.gov/20060505/ DOI: 10.1016/j.mito.2009.12.149
    tissue_or_cell_type
    Liver mitochondria and cultured epithelial cells

    Riboflavin: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 347–358

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Import into purified rat liver mitochondria; BHK-21/Caco-2 confocal imaging · source_derived_draft · unverified_draft

    ### transport-flad1-isoform1-mitochondria In vitro synthesized human FADS1 entered isolated rat liver mitochondria and was processed; transfected-cell imaging also localized it to mitochondria. Condition category: normal nutrient_topic: Riboflavin research collection; topical membership is not evidence of a direct dietary effect. plain_language: One FLAD1 isoform can provide FAD-synthesis machinery inside mitochondria. organism: Human protein; rat mitochondria; hamster and human cells tissue_or_cell_type: Liver mitochondria and cultured epithelial cells experimental_model: Import into purified rat liver mitochondria; BHK-21/Caco-2 confocal imaging limitations: Construct/import evidence does not establish its abundance in every human tissue. exposure: In vitro synthesized and transiently expressed human FADS1. evidence_location: Abstract; mitochondrial import and confocal imaging [transport-fads-localization-2010] Mitochondrial localization of human FAD synthetase isoform 1. (2010). https://pubmed.ncbi.nlm.nih.gov/20060505/ DOI: 10.1016/j.mito.2009.12.149
    Complete structured claim and evidence

  3. Full-length human NADK2 localized to mitochondria in HEK293A cells; deletion of its first 62 residues disrupted that localization.

    NADK2 → Mitochondria source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/niacin-redox-sources/nadk2-2012.fulltext.txt", "locator": "Results", "start_char": 12522, "end_char": 13722, "file_sha256": "65209c0b4ea7220bc95afdd182e40910f2445345172956e85552d5c6db649648", "text_sha256": "bdd61af93db3bf8e573fc599daf7a38da7f5b844d9b5da00d86e955657611875"}
    experimental_model
    FLAG-tagged proteins and endogenous-protein fractionation
    exposure
    Full-length versus Δ62 construct
    limitations
    Evidence resolves mitochondrial localization, not precise submitochondrial position.
    nutrient_topic
    Niacin research collection; topical membership is not evidence of a direct dietary effect. · Niacin (vitamin B3)
    organism
    Homo sapiens
    plain_language
    The N-terminal targeting region directs this kinase into mitochondria.
    primary_references
    [nadk2-2012] Identification and characterization of a human mitochondrial NAD kinase. (2012). https://pubmed.ncbi.nlm.nih.gov/23212377/ DOI: 10.1038/ncomms2262
    tissue_or_cell_type
    HEK293A cells

    Niacin: NAD metabolism, deficiency and nutrient interactions (2026-09-17) · lines 912–923

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · FLAG-tagged proteins and endogenous-protein fractionation · source_derived_draft · unverified_draft

    ### b3-redox-nadk2-localization Full-length human NADK2 localized to mitochondria in HEK293A cells; deletion of its first 62 residues disrupted that localization. Condition category: normal nutrient_topic: Niacin research collection; topical membership is not evidence of a direct dietary effect. plain_language: The N-terminal targeting region directs this kinase into mitochondria. organism: Homo sapiens tissue_or_cell_type: HEK293A cells experimental_model: FLAG-tagged proteins and endogenous-protein fractionation limitations: Evidence resolves mitochondrial localization, not precise submitochondrial position. exposure: Full-length versus Δ62 construct evidence_span: {"source_cache": "artifacts/niacin-redox-sources/nadk2-2012.fulltext.txt", "locator": "Results", "start_char": 12522, "end_char": 13722, "file_sha256": "65209c0b4ea7220bc95afdd182e40910f2445345172956e85552d5c6db649648", "text_sha256": "bdd61af93db3bf8e573fc599daf7a38da7f5b844d9b5da00d86e955657611875"} [nadk2-2012] Identification and characterization of a human mitochondrial NAD kinase. (2012). https://pubmed.ncbi.nlm.nih.gov/23212377/ DOI: 10.1038/ncomms2262
    Complete structured claim and evidence

  4. The BCO2a targeting sequence directed a reporter to mitochondria in ARPE-19 cells; this experiment establishes mitochondrial import, not precise membrane topology.

    Human BCO2a precursor isoform → Mitochondria source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/lutein-research/32873706.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1555914c4a5090c968595f2aba72ce276054594a66423916be600a600a28349f", "start_char": 0, "end_char": 1517, "text_sha256": "1555914c4a5090c968595f2aba72ce276054594a66423916be600a600a28349f"}
    experimental_model
    Isoform targeting, recombinant expression and enzyme assays
    exposure
    Removal of N-terminal mitochondrial targeting sequence; expression optimization
    limitations
    Activity of processed recombinant protein does not quantify retinal flux; mouse chimeric substrate results remain mouse-specific.
    nutrient_topic
    Lutein research collection; topical membership is not evidence of a direct dietary effect. · Lutein
    organism
    Human BCO2 isoforms and engineered mouse protein
    plain_language
    An amino-terminal address directs the protein into mitochondria.
    primary_references
    [lutein-p32873706] The human mitochondrial enzyme BCO2 exhibits catalytic activity toward carotenoids and apocarotenoids. (2020). https://pubmed.ncbi.nlm.nih.gov/32873706/ DOI: 10.1074/jbc.ra120.015515
    tissue_or_cell_type
    ARPE-19 cells and bacterial expression

    Lutein: metabolism, signaling and nutrient connections (2026-09-17) · lines 294–305

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Isoform targeting, recombinant expression and enzyme assays · source_derived_draft · unverified_draft

    ### lutein-bco2-targeting The BCO2a targeting sequence directed a reporter to mitochondria in ARPE-19 cells; this experiment establishes mitochondrial import, not precise membrane topology. Condition category: normal nutrient_topic: Lutein research collection; topical membership is not evidence of a direct dietary effect. plain_language: An amino-terminal address directs the protein into mitochondria. organism: Human BCO2 isoforms and engineered mouse protein tissue_or_cell_type: ARPE-19 cells and bacterial expression experimental_model: Isoform targeting, recombinant expression and enzyme assays limitations: Activity of processed recombinant protein does not quantify retinal flux; mouse chimeric substrate results remain mouse-specific. exposure: Removal of N-terminal mitochondrial targeting sequence; expression optimization evidence_span: {"source_cache": "artifacts/lutein-research/32873706.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "1555914c4a5090c968595f2aba72ce276054594a66423916be600a600a28349f", "start_char": 0, "end_char": 1517, "text_sha256": "1555914c4a5090c968595f2aba72ce276054594a66423916be600a600a28349f"} [lutein-p32873706] The human mitochondrial enzyme BCO2 exhibits catalytic activity toward carotenoids and apocarotenoids. (2020). https://pubmed.ncbi.nlm.nih.gov/32873706/ DOI: 10.1074/jbc.ra120.015515
    Complete structured claim and evidence

  5. A human ALDH1L2 construct carrying its N-terminal targeting region localized to mitochondria in transfected cells.

    Human ALDH1L2 → Mitochondria source_derived_draftungraded
    Experimental context and source evidence
    experimental_model
    Fluorescent protein localization
    exposure
    Assay conditions described in the linked primary study.
    limitations
    Localization alone does not measure carbon-disposal flux.
    nutrient_topic
    Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. · Folate (vitamin B9)
    organism
    Homo sapiens
    plain_language
    ALDH1L2 is the mitochondrial counterpart of cytosolic ALDH1L1.
    primary_references
    [krupenko-2010] ALDH1L2 is the mitochondrial homolog of 10-formyltetrahydrofolate dehydrogenase (2010). https://pubmed.ncbi.nlm.nih.gov/20498374/ DOI: 10.1074/jbc.m110.128843
    tissue_or_cell_type
    A549 cells; corroborating COS-7 host experiments

    Folate and folic acid: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1034–1044

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Fluorescent protein localization · source_derived_draft · unverified_draft

    ### aldh1l2-targeting A human ALDH1L2 construct carrying its N-terminal targeting region localized to mitochondria in transfected cells. Condition category: normal nutrient_topic: Folate and folic acid research collection; topical membership is not evidence of a direct dietary effect. plain_language: ALDH1L2 is the mitochondrial counterpart of cytosolic ALDH1L1. organism: Homo sapiens tissue_or_cell_type: A549 cells; corroborating COS-7 host experiments experimental_model: Fluorescent protein localization limitations: Localization alone does not measure carbon-disposal flux. exposure: Assay conditions described in the linked primary study. [krupenko-2010] ALDH1L2 is the mitochondrial homolog of 10-formyltetrahydrofolate dehydrogenase (2010). https://pubmed.ncbi.nlm.nih.gov/20498374/ DOI: 10.1074/jbc.m110.128843
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Ppif-null hepatocytes and fibroblasts resist calcium-overload-induced death relative to wild type.

    Mitochondrial cyclophilin D / PPIF → Calcium overload-induced cell death source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    compartment_description
    Mitochondrial permeability-transition pathway
    experimental_model
    Ppif-null and cyclophilin-D-overexpressing mice; isolated mitochondria, hepatocytes and fibroblasts
    limitations
    Protection does not extend to all classical apoptotic stimuli; calcium nutrition was not manipulated.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Mus musculus
    plain_language
    Removing cyclophilin D protects these cells against calcium-overload injury.
    primary_references
    [ca-baines2005] Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death (2005). https://pubmed.ncbi.nlm.nih.gov/15800627/ DOI: 10.1038/nature03434
    research_relationship_category
    loss_of_function
    tissue_or_cell_type
    Primary hepatocytes and fibroblasts
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Calcium: mechanism-first literature curation (2026-09-17) · lines 849–860

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Ppif-null and cyclophilin-D-overexpressing mice; isolated mitochondria, hepatocytes and fibroblasts · source_derived_draft · unverified_draft

    ### ca-ppif-loss-calcium-death-resistance Ppif-null hepatocytes and fibroblasts resist calcium-overload-induced death relative to wild type. Condition category: machinery_impairment nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Removing cyclophilin D protects these cells against calcium-overload injury. organism: Mus musculus tissue_or_cell_type: Primary hepatocytes and fibroblasts experimental_model: Ppif-null and cyclophilin-D-overexpressing mice; isolated mitochondria, hepatocytes and fibroblasts limitations: Protection does not extend to all classical apoptotic stimuli; calcium nutrition was not manipulated. research_relationship_category: loss_of_function compartment_description: Mitochondrial permeability-transition pathway [ca-baines2005] Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death (2005). https://pubmed.ncbi.nlm.nih.gov/15800627/ DOI: 10.1038/nature03434
    Complete structured claim and evidence

  2. In cblD-MMA/HC fibroblasts, an MMADHC construct with improved mitochondrial targeting increased adenosylcobalamin formation relative to the targeting comparator.

    MMADHC with enhanced mitochondrial targeting sequence → 5'-Deoxyadenosylcobalamin source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    false
    evidence_location
    Abstract
    experimental_model
    Human cblD-MMA/HC fibroblast transfection
    exposure
    Engineered mitochondrial leader sequence
    limitations
    Abstract-level construct experiment; effect in isolated cblD-MMA lines depended on mutation and endogenous expression.
    nutrient_topic
    Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B12 (cobalamins)
    organism
    Homo sapiens
    plain_language
    Redirecting MMADHC toward mitochondria increased production of this B12 cofactor.
    primary_references
    [stucki-2012-mmad-routing] Molecular mechanisms leading to three different phenotypes in the cblD defect of intracellular cobalamin metabolism (2012). https://pubmed.ncbi.nlm.nih.gov/22156578/ DOI: 10.1093/hmg/ddr579
    tissue_or_cell_type
    Patient fibroblasts
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Vitamin B12: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 823–835

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human cblD-MMA/HC fibroblast transfection · source_derived_draft · unverified_draft

    ### b12-mmad-mito-target-adenosylcobalamin In cblD-MMA/HC fibroblasts, an MMADHC construct with improved mitochondrial targeting increased adenosylcobalamin formation relative to the targeting comparator. Condition category: machinery_impairment nutrient_topic: Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Redirecting MMADHC toward mitochondria increased production of this B12 cofactor. organism: Homo sapiens tissue_or_cell_type: Patient fibroblasts experimental_model: Human cblD-MMA/HC fibroblast transfection limitations: Abstract-level construct experiment; effect in isolated cblD-MMA lines depended on mutation and endogenous expression. exposure: Engineered mitochondrial leader sequence cross_nutrient: false evidence_location: Abstract [stucki-2012-mmad-routing] Molecular mechanisms leading to three different phenotypes in the cblD defect of intracellular cobalamin metabolism (2012). https://pubmed.ncbi.nlm.nih.gov/22156578/ DOI: 10.1093/hmg/ddr579
    Complete structured claim and evidence

  3. In cblD-MMA/HC fibroblasts, an MMADHC construct with improved mitochondrial targeting decreased methylcobalamin formation relative to the targeting comparator.

    MMADHC with enhanced mitochondrial targeting sequence → Methylcobalamin source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    cross_nutrient
    false
    evidence_location
    Abstract
    experimental_model
    Human cblD-MMA/HC fibroblast transfection
    exposure
    Engineered mitochondrial leader sequence
    limitations
    Abstract-level construct experiment; effect in isolated cblD-MMA lines depended on mutation and endogenous expression.
    nutrient_topic
    Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B12 (cobalamins)
    organism
    Homo sapiens
    plain_language
    Redirecting MMADHC toward mitochondria decreased production of this B12 cofactor.
    primary_references
    [stucki-2012-mmad-routing] Molecular mechanisms leading to three different phenotypes in the cblD defect of intracellular cobalamin metabolism (2012). https://pubmed.ncbi.nlm.nih.gov/22156578/ DOI: 10.1093/hmg/ddr579
    tissue_or_cell_type
    Patient fibroblasts
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Vitamin B12: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 837–849

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Human cblD-MMA/HC fibroblast transfection · source_derived_draft · unverified_draft

    ### b12-mmad-mito-target-methylcobalamin In cblD-MMA/HC fibroblasts, an MMADHC construct with improved mitochondrial targeting decreased methylcobalamin formation relative to the targeting comparator. Condition category: machinery_impairment nutrient_topic: Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. plain_language: Redirecting MMADHC toward mitochondria decreased production of this B12 cofactor. organism: Homo sapiens tissue_or_cell_type: Patient fibroblasts experimental_model: Human cblD-MMA/HC fibroblast transfection limitations: Abstract-level construct experiment; effect in isolated cblD-MMA lines depended on mutation and endogenous expression. exposure: Engineered mitochondrial leader sequence cross_nutrient: false evidence_location: Abstract [stucki-2012-mmad-routing] Molecular mechanisms leading to three different phenotypes in the cblD defect of intracellular cobalamin metabolism (2012). https://pubmed.ncbi.nlm.nih.gov/22156578/ DOI: 10.1093/hmg/ddr579
    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.

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