Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-2-22
pubmed:abstractText
T47D cells possess specific calcitonin (CT) receptors and a CT-responsive adenylate cyclase. Internalization of part of their CT receptors has been suggested. At 37 degrees C, bound 125I-labelled salmon CT (sCT) becomes increasingly resistant to acid washing, which can remove surface-bound hormone, thus indicating internalization. Monensin and chloroquine, which raise the pH of the lysosomes and thereby inhibit cellular processing of endosomes, inhibit the decrease of total bound activity seen in the controls. Acid-resistant (internalized) activity increases to the levels of total binding. Preincubation with sCT leads to a loss of specific binding. Recovery of CT binding is prevented by monensin, which also inhibits transport of cellular proteins to the cell membrane. Recovery is not influenced by chloroquine. As chloroquine prevents recycling, we conclude that after binding of CT the receptors are internalized, transferred to a lysosomal compartment, and degraded intracellularly without recycling. All receptors seem to undergo internalization. Desensitization to CT in T47D cells is at least partly mediated by intracellular metabolism of CT receptors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0303-7207
pubmed:author
pubmed:issnType
Print
pubmed:volume
58
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9-15
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Down-regulation of calcitonin receptors in T47D cells by internalization of calcitonin-receptor complexes.
pubmed:affiliation
Department of Internal Medicine I, University of Heidelberg, F.R.G.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't