Component

Human L-type amino acid transporter 1 / LAT1 / SLC7A5

Human L-type amino acid transporter 1 / LAT1 / SLC7A5. Species, exposure and limitations are retained in each linked claim.

9 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. Human LAT1 with SLC3A2 transported large neutral amino acids and exchanged intracellular leucine or glutamine with extracellular substrates.

    Human L-type amino acid transporter 1 / LAT1 / SLC7A5 → Large neutral amino-acid exchange through human LAT1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human proteins expressed in Xenopus oocytes; large-neutral-amino-acid panel.
    limitations
    Accessed abstract does not resolve a separate isoleucine kinetic value. Shared transport is not proof that an ordinary mixed meal causes deficiency.
    nutrient_topic
    L-Isoleucine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Isoleucine
    plain_language
    Shared transport depends on amino acids on both sides of the membrane.
    primary_references
    Human L-type amino acid transporter 1 (LAT1): characterization of function and expression in tumor cell lines. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11557028/ · DOI 10.1016/s0005-2736(01)00384-4

    L-Isoleucine: transport, translation, catabolism and cross-nutrient mechanisms (2026-09-19) · lines 42–48

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human proteins expressed in Xenopus oocytes; large-neutral-amino-acid panel. · source_derived_draft · unverified_draft

    ## isoleucine-lat1-exchange Shared transport depends on amino acids on both sides of the membrane. Human LAT1 with SLC3A2 transported large neutral amino acids and exchanged intracellular leucine or glutamine with extracellular substrates. Model: Human proteins expressed in Xenopus oocytes; large-neutral-amino-acid panel. Limitations: Accessed abstract does not resolve a separate isoleucine kinetic value. Shared transport is not proof that an ordinary mixed meal causes deficiency. Evidence access: Primary abstract Human L-type amino acid transporter 1 (LAT1): characterization of function and expression in tumor cell lines. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11557028/ · DOI 10.1016/s0005-2736(01)00384-4
    Complete structured claim and evidence

  2. Human LAT1 with its SLC3A2 partner transported radiolabeled methionine with an apparent Km of 99 +/- 9 micromolar.

    Human L-type amino acid transporter 1 / LAT1 / SLC7A5 → L-Methionine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human LAT1/SLC3A2 expressed in Xenopus oocytes.
    limitations
    A transporter assay is not a human intestinal absorption threshold.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    A shared amino-acid carrier admits methionine.
    primary_references
    Transport of a neurotoxicant by molecular mimicry: the methylmercury-L-cysteine complex is a substrate for human L-type large neutral amino acid transporter (LAT) 1 and LAT2. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12117417/ · DOI 10.1042/BJ20020841
    transport_effect
    raises Radiolabelled methionine uptake with an apparent Km of 99 micromolar.
    transport_pool
    the expressing cell Radiolabelled methionine uptake with an apparent Km of 99 micromolar.

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 20–26

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human LAT1/SLC3A2 expressed in Xenopus oocytes. · source_derived_draft · unverified_draft

    ## methionine-lat1-transport A shared amino-acid carrier admits methionine. Human LAT1 with its SLC3A2 partner transported radiolabeled methionine with an apparent Km of 99 +/- 9 micromolar. Model: Human LAT1/SLC3A2 expressed in Xenopus oocytes. Limitations: A transporter assay is not a human intestinal absorption threshold. Evidence access: Primary abstract Transport of a neurotoxicant by molecular mimicry: the methylmercury-L-cysteine complex is a substrate for human L-type large neutral amino acid transporter (LAT) 1 and LAT2. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12117417/ · DOI 10.1042/BJ20020841
    Complete structured claim and evidence

  3. Human LAT1 coexpressed with human SLC3A2/4F2hc in Xenopus oocytes transported large neutral amino acids; extracellular substrates exchanged intracellular leucine and glutamine.

    Human L-type amino acid transporter 1 / LAT1 / SLC7A5 → Human LAT1 neutral amino acid exchange source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human transporter proteins in frog oocytes; human T24-cell disulfide-linked complex also detected.
    limitations
    This is an exchange assay, not a direct human brain-uptake trial.
    nutrient_topic
    Tryptophan collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Tryptophan
    plain_language
    Transport depends on a partner protein and amino acids on both sides of the membrane.
    primary_references
    Human L-type amino acid transporter 1 (LAT1): characterization of function and expression in tumor cell lines. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11557028/ · DOI 10.1016/s0005-2736(01)00384-4

    Tryptophan: transport, protein synthesis, neuroactive metabolites, NAD and microbial pathways (2026-09-19) · lines 42–48

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Human transporter proteins in frog oocytes; human T24-cell disulfide-linked complex also detected. · source_derived_draft · unverified_draft

    ## tryptophan-lat1-partner Transport depends on a partner protein and amino acids on both sides of the membrane. Human LAT1 coexpressed with human SLC3A2/4F2hc in Xenopus oocytes transported large neutral amino acids; extracellular substrates exchanged intracellular leucine and glutamine. Model: Human transporter proteins in frog oocytes; human T24-cell disulfide-linked complex also detected. Limitations: This is an exchange assay, not a direct human brain-uptake trial. Evidence access: Primary abstract Human L-type amino acid transporter 1 (LAT1): characterization of function and expression in tumor cell lines. · 2001 · https://pubmed.ncbi.nlm.nih.gov/11557028/ · DOI 10.1016/s0005-2736(01)00384-4
    Complete structured claim and evidence

  4. Human LAT1 mediated theanine uptake in stably transfected S2 cells.

    Human L-type amino acid transporter 1 / LAT1 / SLC7A5 → L-Theanine source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/theanine-research/23221699.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0f79abd668759eccd12f86ec895af75dadf94f6412c29d51a2b6cfde712f9372", "start_char": 0, "end_char": 1143, "text_sha256": "0f79abd668759eccd12f86ec895af75dadf94f6412c29d51a2b6cfde712f9372"}
    experimental_model
    Cell uptake and stable human-transporter expression
    exposure
    Radiolabeled theanine with leucine/BCH competition and sodium replacement
    limitations
    Human transporter identity confirmed in the public primary PDF methods. Engineered cells do not prove which transporter dominates human blood-brain-barrier flux or a clinical meal interaction.
    nutrient_topic
    L-Theanine research collection; topical membership is not evidence of a direct dietary effect. · L-Theanine
    organism
    Mammalian cell lines; human LAT1 and LAT2 expressed in mouse S2 cells
    plain_language
    The same amino acid has more than one identified transport route.
    primary_references
    [theanine-p23221699] The involvement of L-type amino acid transporters in theanine transport. (2012). https://pubmed.ncbi.nlm.nih.gov/23221699/ DOI: 10.1271/bbb.120519
    tissue_or_cell_type
    System L amino acid transport
    transport_effect
    raises Recorded as theanine uptake in stably transfected S2 cells.
    transport_pool
    the expressing cell Recorded as theanine uptake in stably transfected S2 cells.

    L-Theanine: metabolism, neural signaling, nutrient connections and human outcomes (2026-09-17) · lines 172–183

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Cell uptake and stable human-transporter expression · source_derived_draft · unverified_draft

    ### theanine-lat1-transport Human LAT1 mediated theanine uptake in stably transfected S2 cells. Condition category: normal nutrient_topic: L-Theanine research collection; topical membership is not evidence of a direct dietary effect. plain_language: The same amino acid has more than one identified transport route. organism: Mammalian cell lines; human LAT1 and LAT2 expressed in mouse S2 cells tissue_or_cell_type: System L amino acid transport experimental_model: Cell uptake and stable human-transporter expression limitations: Human transporter identity confirmed in the public primary PDF methods. Engineered cells do not prove which transporter dominates human blood-brain-barrier flux or a clinical meal interaction. exposure: Radiolabeled theanine with leucine/BCH competition and sodium replacement evidence_span: {"source_cache": "artifacts/theanine-research/23221699.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0f79abd668759eccd12f86ec895af75dadf94f6412c29d51a2b6cfde712f9372", "start_char": 0, "end_char": 1143, "text_sha256": "0f79abd668759eccd12f86ec895af75dadf94f6412c29d51a2b6cfde712f9372"} [theanine-p23221699] The involvement of L-type amino acid transporters in theanine transport. (2012). https://pubmed.ncbi.nlm.nih.gov/23221699/ DOI: 10.1271/bbb.120519
    Complete structured claim and evidence

  5. Purified human LAT1 transported Cu(His)2 without the internal counter-substrate required for ordinary amino-acid antiport.

    Human L-type amino acid transporter 1 / LAT1 / SLC7A5 → Copper(II) bis(L-histidinate) / Cu(His)2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Reconstituted human LAT1; radiotracer uptake, copper mass spectrometry and mutagenesis; representative assay 40 micromolar histidine plus 20 micromolar copper sulfate.
    limitations
    This in-vitro uniport finding does not establish human copper delivery, safety or treatment efficacy.
    nutrient_topic
    L-Histidine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Histidine
    plain_language
    Binding copper changed how the histidine-containing species crossed this transporter.
    primary_references
    LAT1 (SLC7A5) catalyzes copper(histidinate) transport switching from antiport to uniport mechanism. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37692288/ · DOI 10.1016/j.isci.2023.107738
    transport_effect
    raises Transported without the internal counter-substrate ordinary antiport needs, so this record is a uniport measurement.
    transport_pool
    the proteoliposome interior Transported without the internal counter-substrate ordinary antiport needs, so this record is a uniport measurement.

    L-Histidine: supply, catabolism, histamine, receptors and cross-nutrient mechanisms (2026-09-19) · lines 82–88

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Reconstituted human LAT1; radiotracer uptake, copper mass spectrometry and mutagenesis; representative assay 40 micromolar histidine plus 20 micromolar copper sulfate. · source_derived_draft · unverified_draft

    ## histidine-lat1-copper-complex Binding copper changed how the histidine-containing species crossed this transporter. Purified human LAT1 transported Cu(His)2 without the internal counter-substrate required for ordinary amino-acid antiport. Model: Reconstituted human LAT1; radiotracer uptake, copper mass spectrometry and mutagenesis; representative assay 40 micromolar histidine plus 20 micromolar copper sulfate. Limitations: This in-vitro uniport finding does not establish human copper delivery, safety or treatment efficacy. Evidence access: Primary full text LAT1 (SLC7A5) catalyzes copper(histidinate) transport switching from antiport to uniport mechanism. · 2023 · https://pubmed.ncbi.nlm.nih.gov/37692288/ · DOI 10.1016/j.isci.2023.107738
    Complete structured claim and evidence

  6. Reconstituted human LAT1 supported histidine antiport, including exchange with internal cysteine, tyrosine or glutamine; external histidine affinity exceeded internal affinity.

    Human L-type amino acid transporter 1 / LAT1 / SLC7A5 → L-Histidine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human SiHa extracts and purified recombinant human LAT1 in proteoliposomes.
    limitations
    In-vitro exchange does not establish whole-body competition or supplement ratios.
    nutrient_topic
    L-Histidine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Histidine
    plain_language
    The transporter exchanges substrates, so both sides of the membrane matter.
    primary_references
    LAT1 is the transport competent unit of the LAT1/CD98 heterodimeric amino acid transporter. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26256001/ · DOI 10.1016/j.biocel.2015.08.004
    transport_effect
    depends Recorded as antiport, including exchange with internal cysteine, tyrosine or glutamine.
    transport_pool
    the cytosol across the plasma membrane Recorded as antiport, including exchange with internal cysteine, tyrosine or glutamine.

    L-Histidine: supply, catabolism, histamine, receptors and cross-nutrient mechanisms (2026-09-19) · lines 58–64

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human SiHa extracts and purified recombinant human LAT1 in proteoliposomes. · source_derived_draft · unverified_draft

    ## histidine-lat1-exchange The transporter exchanges substrates, so both sides of the membrane matter. Reconstituted human LAT1 supported histidine antiport, including exchange with internal cysteine, tyrosine or glutamine; external histidine affinity exceeded internal affinity. Model: Human SiHa extracts and purified recombinant human LAT1 in proteoliposomes. Limitations: In-vitro exchange does not establish whole-body competition or supplement ratios. Evidence access: Primary abstract LAT1 is the transport competent unit of the LAT1/CD98 heterodimeric amino acid transporter. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26256001/ · DOI 10.1016/j.biocel.2015.08.004
    Complete structured claim and evidence

  7. Purified human LAT1 alone transported histidine in proteoliposomes; purified CD98 alone did not.

    Human L-type amino acid transporter 1 / LAT1 / SLC7A5 → Transport competence of reconstituted human LAT1 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Recombinant human LAT1 and CD98 reconstitution.
    limitations
    CD98 dispensability for this assay does not mean dispensability for membrane targeting in intact tissues.
    nutrient_topic
    L-Histidine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Histidine
    plain_language
    The transport pore and its partnering protein have distinct roles.
    primary_references
    LAT1 is the transport competent unit of the LAT1/CD98 heterodimeric amino acid transporter. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26256001/ · DOI 10.1016/j.biocel.2015.08.004

    L-Histidine: supply, catabolism, histamine, receptors and cross-nutrient mechanisms (2026-09-19) · lines 66–72

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Recombinant human LAT1 and CD98 reconstitution. · source_derived_draft · unverified_draft

    ## histidine-lat1-subunit The transport pore and its partnering protein have distinct roles. Purified human LAT1 alone transported histidine in proteoliposomes; purified CD98 alone did not. Model: Recombinant human LAT1 and CD98 reconstitution. Limitations: CD98 dispensability for this assay does not mean dispensability for membrane targeting in intact tissues. Evidence access: Primary abstract LAT1 is the transport competent unit of the LAT1/CD98 heterodimeric amino acid transporter. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26256001/ · DOI 10.1016/j.biocel.2015.08.004
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Methylmercury-L-cysteine used human LAT1/LAT2 in oocyte assays, with substrate exchange characteristics resembling methionine.

    Methylmercury-L-cysteine complex → Substrate transport through human LAT1/LAT2 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human carrier expression in Xenopus oocytes.
    limitations
    Complex identity and chirality matter; this does not demonstrate protection from methionine supplementation.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    A toxicant complex can exploit nutrient transport machinery.
    primary_references
    Transport of a neurotoxicant by molecular mimicry: the methylmercury-L-cysteine complex is a substrate for human L-type large neutral amino acid transporter (LAT) 1 and LAT2. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12117417/ · DOI 10.1042/BJ20020841

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 36–42

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human carrier expression in Xenopus oocytes. · source_derived_draft · unverified_draft

    ## methionine-toxicant-mimicry A toxicant complex can exploit nutrient transport machinery. Methylmercury-L-cysteine used human LAT1/LAT2 in oocyte assays, with substrate exchange characteristics resembling methionine. Model: Human carrier expression in Xenopus oocytes. Limitations: Complex identity and chirality matter; this does not demonstrate protection from methionine supplementation. Evidence access: Primary abstract Transport of a neurotoxicant by molecular mimicry: the methylmercury-L-cysteine complex is a substrate for human L-type large neutral amino acid transporter (LAT) 1 and LAT2. · 2002 · https://pubmed.ncbi.nlm.nih.gov/12117417/ · DOI 10.1042/BJ20020841
    Complete structured claim and evidence

  2. After 100 mg/kg oral phenylalanine in six healthy men, plasma phenylalanine rose about elevenfold and brain uptake of the artificial large-neutral-amino-acid tracer carbon-11 ACHC fell from 0.036 to 0.019 mL/g/min.

    L-Phenylalanine → Human brain influx of carbon-11 ACHC tracer source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    biomarker_context Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human PET loading study in six men.
    limitations
    ACHC is a transport tracer; each individual natural amino acid was not directly measured. This is not a normal-meal threshold.
    nutrient_topic
    L-Phenylalanine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Phenylalanine
    plain_language
    A large phenylalanine load can compete with other molecules for brain entry.
    primary_references
    Inhibition of neutral amino acid transport across the human blood-brain barrier by phenylalanine. · 1995 · https://pubmed.ncbi.nlm.nih.gov/7861158/ · DOI 10.1046/j.1471-4159.1995.64031252.x
    trigger_kind
    biomarker_context Imported condition classification; unverified.

    L-Phenylalanine: transport, protein synthesis, cofactor recycling and cross-nutrient mechanisms (2026-09-19) · lines 190–196

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human PET loading study in six men. · source_derived_draft · unverified_draft

    ## l-phenylalanine-brain-competition A large phenylalanine load can compete with other molecules for brain entry. After 100 mg/kg oral phenylalanine in six healthy men, plasma phenylalanine rose about elevenfold and brain uptake of the artificial large-neutral-amino-acid tracer carbon-11 ACHC fell from 0.036 to 0.019 mL/g/min. Model: Human PET loading study in six men. Limitations: ACHC is a transport tracer; each individual natural amino acid was not directly measured. This is not a normal-meal threshold. Evidence access: Primary abstract Inhibition of neutral amino acid transport across the human blood-brain barrier by phenylalanine. · 1995 · https://pubmed.ncbi.nlm.nih.gov/7861158/ · DOI 10.1046/j.1471-4159.1995.64031252.x
    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