Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/47279
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dc.contributor.author | Boassa, D. | - |
dc.contributor.author | Yool, A. | - |
dc.date.issued | 2003 | - |
dc.identifier.citation | BMC Physiology, 2003; 3(Article 1):1-13 | - |
dc.identifier.issn | 1472-6793 | - |
dc.identifier.issn | 1472-6793 | - |
dc.identifier.uri | http://hdl.handle.net/2440/47279 | - |
dc.description.abstract | BACKGROUND Aquaporin-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. RESULTS Voltage 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). CONCLUSIONS These 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. | - |
dc.language.iso | en | - |
dc.publisher | BioMed Central Ltd. | - |
dc.rights | © 2003 Boassa and Yool; licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL. | - |
dc.source.uri | http://www.biomedcentral.com/1472-6793/3/12 | - |
dc.subject | Oocytes | - |
dc.subject | Animals | - |
dc.subject | Xenopus laevis | - |
dc.subject | Humans | - |
dc.subject | Nitroprusside | - |
dc.subject | Amino Acids | - |
dc.subject | Peptides | - |
dc.subject | Aquaporins | - |
dc.subject | Ion Channels | - |
dc.subject | Cyclic GMP | - |
dc.subject | Nitric Oxide Donors | - |
dc.subject | Blood Group Antigens | - |
dc.subject | Patch-Clamp Techniques | - |
dc.subject | Mutagenesis, Site-Directed | - |
dc.subject | Amino Acid Sequence | - |
dc.subject | Conserved Sequence | - |
dc.subject | Protein Structure, Tertiary | - |
dc.subject | Membrane Potentials | - |
dc.subject | Dose-Response Relationship, Drug | - |
dc.subject | Osmotic Pressure | - |
dc.subject | Female | - |
dc.subject | Aquaporin 1 | - |
dc.subject | Cyclic Nucleotide-Gated Cation Channels | - |
dc.title | Single amino acids in the carboxyl terminal domain of aquaporin-1 contribute to cGMP-dependent ion channel activation | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1186/1472-6793-3-12 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Yool, A. [0000-0003-1283-585X] | - |
Appears in Collections: | Aurora harvest Molecular and Biomedical Science publications |
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hdl_47279.pdf | Published version | 443.25 kB | Adobe PDF | View/Open |
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