Linked Life Data

16513835

Source:http://linkedlifedata.com/resource/pubmed/id/16513835

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2006-5-18
pubmed:abstractText
The beta-arrestin-dependent endocytosis of the beta2-adrenergic receptor (beta2AR) has been demonstrated by confocal fluorescence microscopy. Furthermore, a constitutively activated beta2AR is also constitutively desensitized and down-regulated. To clarify the function of beta-arrestin 1 or 2 for TSH receptor (TSHR) desensitization and examine whether constitutively activated TSHR mutants are internalized in a different way, we investigated the TSHR trafficking in association with beta-arrestins in cotransfection experiments in HEK 293 cells using confocal laser-scanning microscopy. We found that both beta-arrestins are able to internalize the TSHR in HEK 293 cells. However, whereas the beta-arrestin 1-mediated TSHR internalization reached its maximum 20 min after TSH stimulation, the beta-arrestin 2-mediated TSHR internalization already reached its maximum 5 min after TSH stimulation. Furthermore, an increased basal desensitization and internalization of constitutively activated TSHR mutants N670S, S505N, and F631L cotransfected with beta-arrestin 2 could not be found. After TSH stimulation the constitutively activated mutants showed the same time course for internalization as the wild-type-TSHR. In summary, contrary to data obtained for the beta2AR, the constitutive activation of the TSHR does not influence the desensitization and time course for internalization of the receptor, and in agreement with findings for the FSH and LH receptors, these results characterize the TSH receptor as a member of the class A of G protein-coupled receptors, which have a higher affinity to beta-arrestin 2 than beta-arrestin 1 and do not colocalize with beta-arrestins in endosomes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0013-7227
pubmed:author
pubmed:issnType
Print
pubmed:volume
147
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3114-22
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
The human thyrotropin receptor is predominantly internalized by beta-arrestin 2.
pubmed:affiliation
III Medical Department, University of Leipzig, 04103 Leipzig, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't