Linked Life Data

7642540

Source:http://linkedlifedata.com/resource/pubmed/id/7642540

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
32
pubmed:dateCreated
1995-9-18
pubmed:abstractText
To investigate the role of the carboxy terminus in the regulation of the bombesin (BN) receptor, we constructed two chimeric receptors with carboxyl termini transferred from either m3 muscarinic cholinergic (m3 ACh) (BMC) or cholecystokinin A (CCKA) (BCC) receptors and expressed them in Chinese hamster ovary cells. Previous studies showed that agonist treatment caused rapid internalization of CCKA but not m3 ACh receptors in these cells. In the current study we conducted separate analyses of ligand and receptor internalization and analyzed receptor recycling. Ligand internalization was assessed using acid washing. BN and CCKA receptors internalized ligand with 80 +/- 3 and 85 +/- 7% in an acid-resistant compartment at equilibrium. Ligand internalization of chimeric receptors generally assumed the properties of the donor receptors. Thus, BCC receptors internalized ligand to a similar extent as wild-type CCKA receptors (75 +/- 3%), whereas, BMC receptors showed reduced ligand internalization (38 +/- 1%). Receptor internalization was more directly assessed by determining agonist-induced loss of surface binding. BN and CCKA receptors were largely internalized (56 +/- 8 and 50 +/- 7%, respectively). BCC receptors were also extensively internalized (82 +/- 3%). In contrast, BMC receptors were minimally internalized (22 +/- 8%). Receptor recycling was assessed as recovery from agonist induced loss of binding. BN, CCKA, and BMC receptors showed rapid recycling. In contrast, BCC receptors did not recycle. These data indicate that carboxyl-terminal structures determine both internalization of ligand-receptor complexes and subsequent receptor recycling.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18858-64
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Carboxyl-terminal domains determine internalization and recycling characteristics of bombesin receptor chimeras.
pubmed:affiliation
Department of Physiology, University of Michigan, Ann Arbor 48109-0622, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.