Study type: In vitro · Status: Verified against declared source

Interaction of amyloid beta with humanin and acetylcholinesterase is modulated by ATP.

FEBS open bio · 2020

Study scale: Besides its well‐documented intracellular role as a molecular energy source, ATP is known to be a ubiquitous extracellular messenger that acts on purinergic receptors to activate a number of intracellular signaling cascades [1, 2].

Abstract only: Open source record

Product or molecular entity relationships

Humanin: Exact entity relationship. Legacy citation custody associates this source with the catalog record; no product-relevance conclusion is implied.

Plain-language verified summary

Question

ELISAs were carried out as we previously reported [65, 80, 82].

Methods

The mechanisms by which Aβ monomers are converted into functional entities and various types of dysfunctional assemblies are largely obscure [16].

Scale or participants

Besides its well‐documented intracellular role as a molecular energy source, ATP is known to be a ubiquitous extracellular messenger that acts on purinergic receptors to activate a number of intracellular signaling cascades [1, 2].

Key findings

Humanin (HN) is known to bind amyloid beta (Aβ)‐inducing cytoprotective effects, while binding of acetylcholinesterase (AChE) to Aβ increases its aggregation and cytotoxicity.

Limitations and uncertainty

Humanin (HN) is a secreted 21‐ to 24‐amino acid mitochondrial‐derived peptide [53, 54].

Verified against declared source. Verification is limited to the declared source and review scope. It does not mean independent replication or establish efficacy, safety, or suitability.