Linked Life Data

7721741

Source:http://linkedlifedata.com/resource/pubmed/id/7721741

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1995-5-19
pubmed:abstractText
The functional role of the rat parathyroid hormone(PTH)/PTH-related peptide (PTHrP) receptor's carboxyl-terminal region was characterized by comparing the binding and signaling properties of receptors that have 78 and 111 amino acid deletions (R513 and R480, respectively), with those of the 591-amino acid wild-type (WT) receptor. R480 and R513 have 4- and 1.5-fold lower apparent Kd values for rat PTH-(1-34) (rPTH), compared with the WT receptor (WT, 1.81 +/- 0.19 nM; R513, 1.24 +/- 0.12 nM; R480, 0.48 +/- 0.05 nM, mean +/- S.E.). PTH (100 nM)-stimulated cAMP accumulation and polyphosphoinositide hydrolysis both correlated positively with receptor expression. However, whereas PTH-stimulated polyphosphoinositide hydrolysis was indistinguishable among WT and either truncated mutant at comparable levels of expressed receptors, maximal PTH-stimulated cAMP accumulation was 4-6- and 2-3-fold higher in cells expressing R480 and R513, respectively. Furthermore, pretreatment of COS-7 cells with 100 ng/ml of pertussis toxin (PTX) enhanced PTH-stimulated cAMP accumulation in cells expressing the WT receptor, but failed to do so in cells expressing either R480 or R513. Thus, sequences in the PTH/PTHrP receptor's carboxyl-terminal tail lower the affinity of the WT receptor for agonist; directly interact with, or indirectly facilitate the interaction of the receptor with a PTX-sensitive G protein that inhibits adenylyl cyclase; and decrease the efficacy with which the receptor interacts with Gs.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8458-65
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:7721741-Adenylate Cyclase, pubmed-meshheading:7721741-Adenylate Cyclase Toxin, pubmed-meshheading:7721741-Amino Acid Sequence, pubmed-meshheading:7721741-Animals, pubmed-meshheading:7721741-Cell Line, pubmed-meshheading:7721741-Cyclic AMP, pubmed-meshheading:7721741-Enzyme Activation, pubmed-meshheading:7721741-GTP-Binding Proteins, pubmed-meshheading:7721741-Molecular Sequence Data, pubmed-meshheading:7721741-Parathyroid Hormone, pubmed-meshheading:7721741-Pertussis Toxin, pubmed-meshheading:7721741-Radioligand Assay, pubmed-meshheading:7721741-Rats, pubmed-meshheading:7721741-Receptor, Parathyroid Hormone, Type 1, pubmed-meshheading:7721741-Receptors, Parathyroid Hormone, pubmed-meshheading:7721741-Type C Phospholipases, pubmed-meshheading:7721741-Virulence Factors, Bordetella
pubmed:year
1995
pubmed:articleTitle
Truncation of the carboxyl-terminal region of the rat parathyroid hormone (PTH)/PTH-related peptide receptor enhances PTH stimulation of adenylyl cyclase but not phospholipase C.
pubmed:affiliation
Endocrine Unit, Massachusetts General Hospital, Boston 02114, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.