Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2006-5-1
pubmed:abstractText
When swollen, skate red blood cells increase permeability and allow efflux of a number of solutes, including taurine. Hypoosmosis-induced taurine permeability appears to involve the red cell anion exchanger. However, three isoforms have been cloned from these cells. Therefore, to determine the ability of the individual isoform skate anion exchanger 1 (skAE1) to mediate hypoosmosis-induced taurine permeability as well as associated regulatory events, skAE1 was expressed in Xenopus oocytes. This study focused on investigating the role of tyrosine kinases and lipid rafts in the regulation of the channel. The results showed that tyrosine kinase inhibitors and lipid raft-disrupting agents inhibited the volume-sensitive organic osmolyte channel while protein tyrosine phosphatase inhibitors activated the channel in oocytes expressing skAE1. To study the role of lipid rafts in the activation of the volume-sensitive organic osmolyte channel, the cellular localization of skAE1 was investigated. Also, the role of tyrosine kinases was investigated by examining the tyrosine phosphorylation state of skAE1. Hypoosmotic stress induced mobilization of skAE1 into light membranes and the cell surface as well as tyrosine phosphorylation of skAE1. These events are involved in the activation of the volume-sensitive organic osmolyte channel in Xenopus oocytes expressing skAE1.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0022-2631
pubmed:author
pubmed:issnType
Print
pubmed:volume
208
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
241-50
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
The activation pathway of the volume-sensitive organic osmolyte channel in Xenopus laevis oocytes expressing skate anion exchanger 1 (AE1).
pubmed:affiliation
Division of Biology and Medicine, Brown University, Providence, RI 02912, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, N.I.H., Extramural