Human AMPA receptor subunit GluA3 / GRIA3: molecular mechanisms & dependencies

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.

Human evidence only

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

Where it participates (unsigned role)

Glutamate at 10 nM promoted integrin-mediated adhesion of tested human T cells to laminin and fibronectin; AMPA antagonists and relevant anti-integrin antibodies blocked the response.
L-Glutamate → Glutamate-evoked human T-cell adhesion source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Human T-cell receptor expression and adhesion assays.
limitations
Antagonist support does not uniquely prove GluA3 is the sole functional subunit; no dietary immune benefit is established.
nutrient_topic
L-Glutamate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Glutamate
plain_language
An extracellular amino acid changed immune-cell behavior in an assay.
primary_references
Human T cells express a functional ionotropic glutamate receptor GluR3, and glutamate by itself triggers integrin-mediated adhesion to laminin and fibronectin and chemotactic migration. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12682273/ · DOI 10.4049/jimmunol.170.8.4362
L-Glutamate / L-glutamic acid: carbon and nitrogen allocation, signaling and cross-nutrient mechanisms (2026-09-19) · lines 354–360
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human T-cell receptor expression and adhesion assays. · source_derived_draft · unverified_draft
## glutamate-immune-adhesion An extracellular amino acid changed immune-cell behavior in an assay. Glutamate at 10 nM promoted integrin-mediated adhesion of tested human T cells to laminin and fibronectin; AMPA antagonists and relevant anti-integrin antibodies blocked the response. Model: Human T-cell receptor expression and adhesion assays. Limitations: Antagonist support does not uniquely prove GluA3 is the sole functional subunit; no dietary immune benefit is established. Evidence access: Primary abstract Human T cells express a functional ionotropic glutamate receptor GluR3, and glutamate by itself triggers integrin-mediated adhesion to laminin and fibronectin and chemotactic migration. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12682273/ · DOI 10.4049/jimmunol.170.8.4362
Complete structured claim and evidence
Glutamate increased CXCR4-mediated T-cell chemotactic migration toward CXCL12 in the reported experiments.
L-Glutamate → Human T-cell migration toward CXCL12 source_derived_draftungraded
Experimental context and source evidence
evidence_access
Primary abstract
experimental_model
Human T-cell chemotaxis experiments in the receptor study.
limitations
This does not establish disease causation or the direction of a clinical immune effect.
nutrient_topic
L-Glutamate collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Glutamate
plain_language
A metabolic signal interacted with a chemokine-guided movement system.
primary_references
Human T cells express a functional ionotropic glutamate receptor GluR3, and glutamate by itself triggers integrin-mediated adhesion to laminin and fibronectin and chemotactic migration. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12682273/ · DOI 10.4049/jimmunol.170.8.4362
L-Glutamate / L-glutamic acid: carbon and nitrogen allocation, signaling and cross-nutrient mechanisms (2026-09-19) · lines 362–368
AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human T-cell chemotaxis experiments in the receptor study. · source_derived_draft · unverified_draft
## glutamate-immune-migration A metabolic signal interacted with a chemokine-guided movement system. Glutamate increased CXCR4-mediated T-cell chemotactic migration toward CXCL12 in the reported experiments. Model: Human T-cell chemotaxis experiments in the receptor study. Limitations: This does not establish disease causation or the direction of a clinical immune effect. Evidence access: Primary abstract Human T cells express a functional ionotropic glutamate receptor GluR3, and glutamate by itself triggers integrin-mediated adhesion to laminin and fibronectin and chemotactic migration. · 2003 · https://pubmed.ncbi.nlm.nih.gov/12682273/ · DOI 10.4049/jimmunol.170.8.4362
Complete structured claim and evidence

The events it takes part in

A mechanism often involves more than two components. These are the full events, with every participant and its role.

Situations it appears in

Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.

In the sources

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

Open hypotheses

Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.

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

Human AMPA receptor subunit GluA3 / GRIA3