Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2007-5-14
pubmed:abstractText
Aquaporin channels facilitate the transport of water, glycerol, and other small solutes across cell membranes. The physiological roles of many aquaporins remain unclear. To better understand aquaporin function, we characterized the aquaporin gene family in the nematode Caenorhabditis elegans. Eight canonical aquaporin-encoding genes (aqp) are present in the worm genome. Expression of aqp-2, aqp-3, aqp-4, aqp-6, or aqp-7 in Xenopus oocytes increased water permeability five- to sevenfold. Glycerol permeability was increased three to sevenfold by expression of aqp-1, aqp-3, or aqp-7. Green fluorescent protein transcriptional and translational reporters demonstrated that aqp genes are expressed in numerous C. elegans cell types, including the intestine, excretory cell, and hypodermis, which play important roles in whole animal osmoregulation. To define the role of C. elegans aquaporins in osmotic homeostasis, we isolated deletion alleles for four aqp genes, aqp-2, aqp-3, aqp-4, and aqp-8, which are expressed in osmoregulatory tissues and mediate water transport. Single, double, triple, and quadruple aqp mutant animals exhibited normal survival, development, growth, fertility, and movement under normal and hypertonic culture conditions. aqp-2;aqp-3;aqp-4;aqp-8 quadruple mutants exhibited a slight defect in recovery from hypotonic stress but survived hypotonic stress as well as wild-type animals. These results suggest that C. elegans aquaporins are not essential for whole animal osmoregulation and/or that deletion of aquaporin genes activates mechanisms that compensate for loss of water channel function.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0363-6143
pubmed:author
pubmed:issnType
Print
pubmed:volume
292
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
C1867-73
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:17229810-Amino Acid Sequence, pubmed-meshheading:17229810-Animals, pubmed-meshheading:17229810-Aquaporins, pubmed-meshheading:17229810-Caenorhabditis elegans, pubmed-meshheading:17229810-Caenorhabditis elegans Proteins, pubmed-meshheading:17229810-Cell Membrane Permeability, pubmed-meshheading:17229810-Cloning, Molecular, pubmed-meshheading:17229810-Gene Expression, pubmed-meshheading:17229810-Genes, Reporter, pubmed-meshheading:17229810-Genotype, pubmed-meshheading:17229810-Glycerol, pubmed-meshheading:17229810-Green Fluorescent Proteins, pubmed-meshheading:17229810-Microinjections, pubmed-meshheading:17229810-Molecular Sequence Data, pubmed-meshheading:17229810-Mutation, pubmed-meshheading:17229810-Oocytes, pubmed-meshheading:17229810-Phenotype, pubmed-meshheading:17229810-Phylogeny, pubmed-meshheading:17229810-Promoter Regions, Genetic, pubmed-meshheading:17229810-Sodium Chloride, pubmed-meshheading:17229810-Water, pubmed-meshheading:17229810-Water-Electrolyte Balance, pubmed-meshheading:17229810-Xenopus
pubmed:year
2007
pubmed:articleTitle
Functional analysis of the aquaporin gene family in Caenorhabditis elegans.
pubmed:affiliation
Department of Biological Chemistry, Johns Hopkins University, Baltimore, Maryland, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural