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protein

Aquaporin-1

aka AQP-1

AQP1
protein:P29972disease:adad:direction:up

Gene

AQP1

Organism

Homo sapiens(9606)

Length

269 aa

Mass

28,526 Da

AI summarysource-grounded · cited inline
claude-haiku-4-5-20251001

Aquaporin-1 (AQP1) is a water channel protein that facilitates transport of water across cell membranes, maintaining cellular water homeostasis (UniProt: P29972). Beyond water transport, it exhibits permeability to small solutes and gases including hydrogen peroxide, glycerol, ammonia, nitric oxide, and carbon dioxide, and may function as a non-selective gated cation channel. In erythrocytes, AQP1 associates with the ankyrin-1 complex and participates in a CO2 metabolon linking gas diffusion to anion exchange and carbonic acid interconversion.

AQP1 is expressed across multiple tissues and plays roles in water homeostasis in organs including the kidney, brain microvessels, and red blood cells (UniProt: P29972). No specific disease associations are documented in UniProt for this protein.

In Alzheimer's Disease, AQP1 is significantly upregulated in post-mortem AD brain tissue relative to age-matched controls, with a mean log2 fold-change of 1.571 across two subcellular fractions in TMT-labeled proteomics (Chaparral AD proteomics). This upregulation may reflect altered water homeostasis or glial responses characteristic of AD pathology, though the functional consequence remains to be determined.

Generated from the curated entity record below. May contain errors — verify against source links.

Proteomics Evidence · AD

↑ Up in AD

P3

not detected

P2

not detected

S2

+2.054

S3

+1.088

Mean log₂FC across detected fractions: +1.571 (2 of 4 fractions detected)

Human post-mortem AD brain vs age-matched controls, TMT-labeled, 4 subcellular fractions (P2, P3, S2, S3), DDA proteomics.

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Function

Forms a water channel that facilitates the transport of water across cell membranes, playing a crucial role in water homeostasis in various tissues (PubMed:1373524, PubMed:23219802). Could also be permeable to small solutes including hydrogen peroxide, glycerol and gases such as amonnia (NH3), nitric oxide (NO) and carbon dioxide (CO2) (PubMed:16682607, PubMed:17012249, PubMed:19273840, PubMed:33028705, PubMed:8584435). Recruited to the ankyrin-1 complex, a multiprotein complex of the erythrocyte membrane, it could be part of a CO2 metabolon, linking facilitated diffusion of CO2 across the membrane, anion exchange of Cl(-)/HCO3(-) and interconversion of dissolved CO2 and carbonic acid in the cytosol (PubMed:17012249, PubMed:35835865). In vitro, it shows non-selective gated cation channel activity and may be permeable to cations like K(+) and Na(+) in vivo (PubMed:36949749, PubMed:8703053)

Sources

Last updated 5/8/2026, 6:31:00 AM