ArticleBMC physiology2003
Single amino acids in the carboxyl terminal domain of aquaporin-1 contribute to cGMP-dependent ion channel activation.
Article in BMC physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 44 citations in OpenAlex.
- Structural Domains Associated with Permeation, Gating, and Selectivity of Aquaporin Ion Channels Found Across Phyla.Advances in experimental medicine and biology · 2026Review
- Aging alters the expression of trophic factors and tight junction proteins in the mouse choroid plexus.Fluids and barriers of the CNS · 2024Article
- From Homeostasis to Pathology: Decoding the Multifaceted Impact of Aquaporins in the Central Nervous System.International journal of molecular sciences · 2023Review
- Aquaporins and Ion Channels as Dual Targets in the Design of Novel Glioblastoma Therapeutics to Limit Invasiveness.Cancers · 2023Review
- Choroid Plexus Aquaporins in CSF Homeostasis and the Glymphatic System: Their Relevance for Alzheimer's Disease.International journal of molecular sciences · 2023Review
- Methods for studying mammalian aquaporin biology.Biology methods & protocols · 2023Review
- Review
- Signaling Mechanisms and Pharmacological Modulators Governing Diverse Aquaporin Functions in Human Health and Disease.International journal of molecular sciences · 2022Review
- Human Aquaporins: Functional Diversity and Potential Roles in Infectious and Non-infectious Diseases.Frontiers in genetics · 2021Review
- Inhibition of the Aquaporin-1 Cation Conductance by Selected Furan Compounds Reduces Red Blood Cell Sickling.Frontiers in pharmacology · 2021Article
- Combined pharmacological administration of AQP1 ion channel blocker AqB011 and water channel blocker Bacopaside II amplifies inhibition of colon cancer cell migration.Scientific reports · 2019Article
- Review
- Identification of Loop D Domain Amino Acids in the Human Aquaporin-1 Channel Involved in Activation of the Ionic Conductance and Inhibition by AqB011.Frontiers in chemistry · 2018Article
- Role of Aquaporin 1 Signalling in Cancer Development and Progression.International journal of molecular sciences · 2017Review
- Bumetanide Derivatives AqB007 and AqB011 Selectively Block the Aquaporin-1 Ion Channel Conductance and Slow Cancer Cell Migration.Molecular pharmacology · 2016Article
- Stimulation of aquaporin-mediated fluid transport by cyclic GMP in human retinal pigment epithelium in vitro.Investigative ophthalmology & visual science · 2012Article
- Inhibition of aquaporin-1 and aquaporin-4 water permeability by a derivative of the loop diuretic bumetanide acting at an internal pore-occluding binding site.Molecular pharmacology · 2009Article
- Ion channel function of aquaporin-1 natively expressed in choroid plexus.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- Structure, function and translational relevance of aquaporin dual water and ion channels.Molecular aspects of medicineReview
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
backgroundAquaporin-1 (AQP1) functions as an osmotic water channel and a gated cation channel. Activation of the AQP1 ion conductance by intracellular cGMP was hypothesized to involve the carboxyl (C-) terminus, based on amino acid sequence alignments with cyclic-nucleotide-gated channels and cGMP-selective phosphodiesterases.
resultsVoltage clamp analyses of human AQP1 channels expressed in Xenopus oocytes demonstrated that the nitric oxide donor, sodium nitroprusside (SNP; 3-14 mM) activated the ionic conductance response in a dose-dependent manner. Block of soluble guanylate cyclase prevented the response. Enzyme immunoassays confirmed a linear dose-dependent relationship between SNP and the resulting intracellular cGMP levels (up to 1700 fmol cGMP /oocyte at 14 mM SNP). Results here are the first to show that the efficacy of ion channel activation is decreased by mutations of AQP1 at conserved residues in the C-terminal domain (aspartate D237 and lysine K243).
conclusionsThese data support the idea that the limited amino acid sequence similarities found between three diverse classes of cGMP-binding proteins are significant to the function of AQP1 as a cGMP-gated ion channel, and provide direct evidence for the involvement of the AQP1 C-terminal domain in cGMP-mediated ion channel activation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.