Component

Human L-type amino acid transporter 2 / LAT2 / SLC7A8

Human L-type amino acid transporter 2 / LAT2 / SLC7A8. Species, exposure and limitations are retained in each linked claim.

3 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 LAT2/SLC3A2 transported methionine; leucine and phenylalanine stimulated methionine efflux even against an inward methionine gradient.

    Human L-type amino acid transporter 2 / LAT2 / SLC7A8 → L-Methionine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human transporter in Xenopus oocytes; tracer influx and efflux.
    limitations
    Does not show that ordinary mixed meals deplete methionine.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    Transport depends on substrates on both sides of the membrane.
    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 28–34

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

    ## methionine-lat2-exchange Transport depends on substrates on both sides of the membrane. Human LAT2/SLC3A2 transported methionine; leucine and phenylalanine stimulated methionine efflux even against an inward methionine gradient. Model: Human transporter in Xenopus oocytes; tracer influx and efflux. Limitations: Does not show that ordinary mixed meals deplete methionine. 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. Human LAT2 mediated theanine uptake in stably transfected S2 cells.

    Human L-type amino acid transporter 2 / LAT2 / SLC7A8 → 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 185–196

    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-lat2-transport Human LAT2 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

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

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