Component

E-cadherin ectodomain proteolysis

Independent biological entity. Read linked claims for experimental scope and context.

1 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

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. Calcium binding protected the recombinant mouse E-cadherin ectodomain from tryptic cleavage; calcium depletion caused a reversible conformational change.

    Calcium ion → E-cadherin ectodomain proteolysis source_derived_draftungraded
    Experimental context and source evidence
    compartment_description
    Extracellular domain
    experimental_model
    Calcium titration, electron microscopy and trypsin assay
    limitations
    In-vitro calcium removal is not dietary calcium deficiency; the soluble fragment did not self-associate under these assay conditions.
    nutrient_topic
    Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
    organism
    Mus musculus protein expressed in insect cells
    plain_language
    Bound calcium helps keep the adhesion protein folded and resistant to protease attack.
    primary_references
    [pokutta1994] Conformational changes of the recombinant extracellular domain of E-cadherin upon calcium binding (1994). https://febs.onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1994.tb19080.x DOI: 10.1111/j.1432-1033.1994.tb19080.x
    tissue_or_cell_type
    Purified extracellular domain

    Calcium: mechanism-first literature curation (2026-09-17) · lines 1140–1150

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Calcium titration, electron microscopy and trypsin assay · source_derived_draft · unverified_draft

    ### calcium-protects-e-cadherin-from-proteolysis Calcium binding protected the recombinant mouse E-cadherin ectodomain from tryptic cleavage; calcium depletion caused a reversible conformational change. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Bound calcium helps keep the adhesion protein folded and resistant to protease attack. organism: Mus musculus protein expressed in insect cells tissue_or_cell_type: Purified extracellular domain experimental_model: Calcium titration, electron microscopy and trypsin assay limitations: In-vitro calcium removal is not dietary calcium deficiency; the soluble fragment did not self-associate under these assay conditions. compartment_description: Extracellular domain [pokutta1994] Conformational changes of the recombinant extracellular domain of E-cadherin upon calcium binding (1994). https://febs.onlinelibrary.wiley.com/doi/10.1111/j.1432-1033.1994.tb19080.x DOI: 10.1111/j.1432-1033.1994.tb19080.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