Component

Mouse B0AT1 / Slc6a19

Mouse B0AT1 / Slc6a19. Species, exposure and limitations are retained in each linked claim.

5 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. Ace2 loss removed intestinal B0AT1 expression in mice; kidney B0AT1 regulation differed and depended on collectrin.

    Mouse angiotensin-converting enzyme 2 / Ace2 → Mouse B0AT1 / Slc6a19 source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text, partner constructs and mouse tissue results
    experimental_model
    Mouse tissue expression and transporter-partner experiments.
    limitations
    Separate oocyte experiments combine human B0AT1 with mouse ACE2 or human collectrin; they are not an all-human ACE2 reconstruction.
    nutrient_topic
    Tryptophan collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Tryptophan
    plain_language
    The same amino-acid transporter needs different support in intestine and kidney.
    primary_references
    Tissue-specific amino acid transporter partners ACE2 and collectrin differentially interact with hartnup mutations. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19185582/ · DOI 10.1053/j.gastro.2008.10.055
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Tryptophan: transport, protein synthesis, neuroactive metabolites, NAD and microbial pathways (2026-09-19) · lines 66–72

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Mouse tissue expression and transporter-partner experiments. · source_derived_draft · unverified_draft

    ## tryptophan-ace2-transporter The same amino-acid transporter needs different support in intestine and kidney. Ace2 loss removed intestinal B0AT1 expression in mice; kidney B0AT1 regulation differed and depended on collectrin. Model: Mouse tissue expression and transporter-partner experiments. Limitations: Separate oocyte experiments combine human B0AT1 with mouse ACE2 or human collectrin; they are not an all-human ACE2 reconstruction. Evidence access: Primary full text, partner constructs and mouse tissue results Tissue-specific amino acid transporter partners ACE2 and collectrin differentially interact with hartnup mutations. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19185582/ · DOI 10.1053/j.gastro.2008.10.055
    Complete structured claim and evidence

  2. The study reported increased mRNA and protein expression of the mouse intestinal transporter component SLC6A19.

    L-Theanine → Mouse B0AT1 / Slc6a19 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/theanine-research/36615799.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0bb37e6a5f3624dc13eb87705f21721a6cf7cc2151b0ecf87dedef2ff11c95be", "start_char": 0, "end_char": 1077, "text_sha256": "0bb37e6a5f3624dc13eb87705f21721a6cf7cc2151b0ecf87dedef2ff11c95be"}
    experimental_model
    Intestinal transporter and phosphorylation assays
    exposure
    Oral L-theanine supplementation in the mouse experiment
    limitations
    Transporter expression and mTOR pathway activation were associated. Without an intervention blocking the proposed pathway, dependency is not established; no human protein-absorption benefit inferred.
    nutrient_topic
    L-Theanine research collection; topical membership is not evidence of a direct dietary effect. · L-Theanine
    organism
    Mice
    plain_language
    Each transporter remains searchable separately from the overall amino acid response.
    primary_references
    [theanine-p36615799] L-Theanine Regulates the Abundance of Amino Acid Transporters in Mice Duodenum and Jejunum via the mTOR Signaling Pathway. (2022). https://pubmed.ncbi.nlm.nih.gov/36615799/ DOI: 10.3390/nu15010142
    tissue_or_cell_type
    Intestinal amino acid transport and mTOR signaling

    L-Theanine: metabolism, neural signaling, nutrient connections and human outcomes (2026-09-17) · lines 705–716

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Intestinal transporter and phosphorylation assays · source_derived_draft · unverified_draft

    ### theanine-mouse-intestinal-slc6a19 The study reported increased mRNA and protein expression of the mouse intestinal transporter component SLC6A19. Condition category: normal nutrient_topic: L-Theanine research collection; topical membership is not evidence of a direct dietary effect. plain_language: Each transporter remains searchable separately from the overall amino acid response. organism: Mice tissue_or_cell_type: Intestinal amino acid transport and mTOR signaling experimental_model: Intestinal transporter and phosphorylation assays limitations: Transporter expression and mTOR pathway activation were associated. Without an intervention blocking the proposed pathway, dependency is not established; no human protein-absorption benefit inferred. exposure: Oral L-theanine supplementation in the mouse experiment evidence_span: {"source_cache": "artifacts/theanine-research/36615799.abstract.txt", "locator": "Primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "0bb37e6a5f3624dc13eb87705f21721a6cf7cc2151b0ecf87dedef2ff11c95be", "start_char": 0, "end_char": 1077, "text_sha256": "0bb37e6a5f3624dc13eb87705f21721a6cf7cc2151b0ecf87dedef2ff11c95be"} [theanine-p36615799] L-Theanine Regulates the Abundance of Amino Acid Transporters in Mice Duodenum and Jejunum via the mTOR Signaling Pathway. (2022). https://pubmed.ncbi.nlm.nih.gov/36615799/ DOI: 10.3390/nu15010142
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Ace2 deletion removed intestinal B0AT1 expression and abolished sodium-dependent isoleucine uptake in mouse ileum segments.

    Mouse angiotensin-converting enzyme 2 / Ace2 → Isoleucine uptake in mouse ileum source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text
    experimental_model
    Ace2-null mouse intestine; expression, interaction and uptake assays.
    limitations
    Kidney accessory-protein dependence differs; not evidence that every change in ACE2 produces dietary isoleucine deficiency.
    nutrient_topic
    L-Isoleucine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Isoleucine
    plain_language
    A working transporter also needs its accessory protein in this tissue.
    primary_references
    Tissue-specific amino acid transporter partners ACE2 and collectrin differentially interact with hartnup mutations. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19185582/ · DOI 10.1053/j.gastro.2008.10.055
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Isoleucine: transport, translation, catabolism and cross-nutrient mechanisms (2026-09-19) · lines 26–32

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Ace2-null mouse intestine; expression, interaction and uptake assays. · source_derived_draft · unverified_draft

    ## isoleucine-intestinal-ace2 A working transporter also needs its accessory protein in this tissue. Ace2 deletion removed intestinal B0AT1 expression and abolished sodium-dependent isoleucine uptake in mouse ileum segments. Model: Ace2-null mouse intestine; expression, interaction and uptake assays. Limitations: Kidney accessory-protein dependence differs; not evidence that every change in ACE2 produces dietary isoleucine deficiency. Evidence access: Primary full text Tissue-specific amino acid transporter partners ACE2 and collectrin differentially interact with hartnup mutations. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19185582/ · DOI 10.1053/j.gastro.2008.10.055
    Complete structured claim and evidence

  2. Replacing sodium during mouse ileum uptake assays removed the sodium-dependent component of radiolabeled L-isoleucine uptake.

    Sodium ion → Isoleucine uptake in mouse ileum source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary full text
    experimental_model
    Everted mouse ileum; 1 mM L-isoleucine, five-minute uptake assay.
    limitations
    Does not imply extra dietary sodium improves absorption in sodium-replete people.
    nutrient_topic
    L-Isoleucine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Isoleucine
    plain_language
    An ion gradient helps the intestine take up this amino acid.
    primary_references
    Tissue-specific amino acid transporter partners ACE2 and collectrin differentially interact with hartnup mutations. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19185582/ · DOI 10.1053/j.gastro.2008.10.055

    L-Isoleucine: transport, translation, catabolism and cross-nutrient mechanisms (2026-09-19) · lines 18–24

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Everted mouse ileum; 1 mM L-isoleucine, five-minute uptake assay. · source_derived_draft · unverified_draft

    ## isoleucine-intestinal-sodium An ion gradient helps the intestine take up this amino acid. Replacing sodium during mouse ileum uptake assays removed the sodium-dependent component of radiolabeled L-isoleucine uptake. Model: Everted mouse ileum; 1 mM L-isoleucine, five-minute uptake assay. Limitations: Does not imply extra dietary sodium improves absorption in sodium-replete people. Evidence access: Primary full text Tissue-specific amino acid transporter partners ACE2 and collectrin differentially interact with hartnup mutations. · 2009 · https://pubmed.ncbi.nlm.nih.gov/19185582/ · DOI 10.1053/j.gastro.2008.10.055
    Complete structured claim and evidence

  3. Gly-Trp feeding restored serum tryptophan and reduced DSS-colitis susceptibility in Ace2-deficient mice, bypassing loss of single-amino-acid uptake.

    Glycyl-L-tryptophan / Gly-Trp dipeptide → Mouse susceptibility to chemically induced colitis in tryptophan experiments source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary full text, Figure 2 and rescue results
    experimental_model
    Ace2-mutant mouse dietary rescue.
    limitations
    Not a clinical Gly-Trp treatment recommendation or evidence that free tryptophan always bypasses transporter loss.
    nutrient_topic
    Tryptophan collection; molecular form, preparation, species, exposure and manipulation remain explicit. · L-Tryptophan
    plain_language
    A dipeptide delivery route bypassed missing transport support.
    primary_references
    ACE2 links amino acid malnutrition to microbial ecology and intestinal inflammation. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22837003/ · DOI 10.1038/nature11228
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Tryptophan: transport, protein synthesis, neuroactive metabolites, NAD and microbial pathways (2026-09-19) · lines 74–80

    AI-assisted research curation; primary-abstract references and experimental limitations individually identified. Not publisher full text. · supports · Ace2-mutant mouse dietary rescue. · source_derived_draft · unverified_draft

    ## tryptophan-glytrp-bypass A dipeptide delivery route bypassed missing transport support. Gly-Trp feeding restored serum tryptophan and reduced DSS-colitis susceptibility in Ace2-deficient mice, bypassing loss of single-amino-acid uptake. Model: Ace2-mutant mouse dietary rescue. Limitations: Not a clinical Gly-Trp treatment recommendation or evidence that free tryptophan always bypasses transporter loss. Evidence access: Primary full text, Figure 2 and rescue results ACE2 links amino acid malnutrition to microbial ecology and intestinal inflammation. · 2012 · https://pubmed.ncbi.nlm.nih.gov/22837003/ · DOI 10.1038/nature11228
    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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