Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
1998-5-21
pubmed:databankReference
pubmed:abstractText
Amiloride-sensitive sodium channels have been implicated in reproductive and early developmental processes of several species. These include the fast block of polyspermy in Xenopus oocytes that follows the sperm binding to the egg or blastocoel expansion in mammalian embryo. We have now identified a gene called dGNaC1 that is specifically expressed in the gonads and early embryo in Drosophila melanogaster. The corresponding protein belongs to the superfamily of cationic channels blocked by amiloride that includes Caenorhabditis elegans degenerins, the Helix aspersa FMRF-amide ionotropic receptor (FaNaC), the mammalian epithelial Na+ channel (ENaC), and acid-sensing ionic channels (ASIC, DRASIC, and MDEG). Expression of dGNaC1 in Xenopus oocytes generates a constitutive current that does not discriminate between Na+ and Li+, but is selective for Na+ over K+. This current is blocked by amiloride (IC50 = 24 microM), benzamil (IC50 = 2 microM), and ethylisopropyl amiloride (IC50 = 49 microM). These properties are clearly different from those obtained after expression of the previously cloned members of this family, including ENaC and the human alphaENaC-like subunit, deltaNaC. Interestingly, the pharmacology of dGNaC1 is not very different from that found for the Na+ channel characterized in rabbit preimplantation embryos. We postulate that this channel may participate in gametogenesis and early embryonic development in Drosophila.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9424-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9545267-Amiloride, pubmed-meshheading:9545267-Amino Acid Sequence, pubmed-meshheading:9545267-Animals, pubmed-meshheading:9545267-Caenorhabditis elegans, pubmed-meshheading:9545267-Cations, pubmed-meshheading:9545267-Drosophila Proteins, pubmed-meshheading:9545267-Drosophila melanogaster, pubmed-meshheading:9545267-Embryo, Nonmammalian, pubmed-meshheading:9545267-Epithelial Sodium Channel, pubmed-meshheading:9545267-Female, pubmed-meshheading:9545267-Helix (Snails), pubmed-meshheading:9545267-Humans, pubmed-meshheading:9545267-Male, pubmed-meshheading:9545267-Membrane Potentials, pubmed-meshheading:9545267-Molecular Sequence Data, pubmed-meshheading:9545267-Multigene Family, pubmed-meshheading:9545267-Oocytes, pubmed-meshheading:9545267-Rabbits, pubmed-meshheading:9545267-Recombinant Proteins, pubmed-meshheading:9545267-Sequence Alignment, pubmed-meshheading:9545267-Sequence Homology, Amino Acid, pubmed-meshheading:9545267-Sex Characteristics, pubmed-meshheading:9545267-Sodium, pubmed-meshheading:9545267-Sodium Channels, pubmed-meshheading:9545267-Sperm-Ovum Interactions, pubmed-meshheading:9545267-Testis, pubmed-meshheading:9545267-Xenopus laevis
pubmed:year
1998
pubmed:articleTitle
dGNaC1, a gonad-specific amiloride-sensitive Na+ channel.
pubmed:affiliation
Institut de Pharmacologie Moléculaire et Cellulaire, CNRS UPR 411, 660 route des Lucioles, Sophia Antipolis, 06560 Valbonne, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't