Linked Life Data

19472194

Source:http://linkedlifedata.com/resource/pubmed/id/19472194

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2009-6-1
pubmed:abstractText
The asparagine-proline-alanine sequences (NPA motifs) in Loops B and E of aquaporin are highly conserved. To investigate the role of two NPA motifs in the structure and function of aquaporin water channels, we generated human aquaporins (AQP)-1 mutations with NPA1 deletion, NPA2 deletion and NPA1,2 double deletion. Immunoblotting and immunofluorescence analysis indicated that all the three human AQP1 mutants possessed identical protein pattern and similar plasma membrane expression pattern compared to wild-type AQP1. Plasma membrane osmotic water permeability analysis, measured by YFP-based fluorescence quenching method and Xenopus oocyte expression assays, demonstrated that NPA1 or NPA2 deletion significantly reduced human AQP1 water permeability nearly 50% compared to wild-type AQP1, while NPA1,2 double deletion had little effect on human AQP1 water permeability. These results provide evidence that NPA motifs are important for water permeation but not essential for the expression, intracellular processing and the basic structure of human aquaporin 1.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1521-6551
pubmed:author
pubmed:copyrightInfo
(c) 2009 IUBMB.
pubmed:issnType
Electronic
pubmed:volume
61
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
651-7
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Expression and functional characterization of NPA motif-null aquaporin-1 mutations.
pubmed:affiliation
Key Laboratory of Industrial Microbiology, Ministry of Education, College of Biotechnology, Tianjin University of Science and Technology, Tianjin, China. jiangyong@tust.edu.cn
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't