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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

Iida-Klein, Akiko ; Guo, Jun ; Xie, Lin Y. ; Jüppner, Harald ; Potts, John T. ; Kronenberg, Henry M. ; Bringhurst, F. Richard ; Abou-Samra, Abdul B. ; Segre, Gino V.

The Journal of biological chemistry, 1995-04, Vol.270 (15), p.8458-8465 [Periódico revisado por pares]

United States: Elsevier Inc

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Título:
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
Autor: Iida-Klein, Akiko ; Guo, Jun ; Xie, Lin Y. ; Jüppner, Harald ; Potts, John T. ; Kronenberg, Henry M. ; Bringhurst, F. Richard ; Abou-Samra, Abdul B. ; Segre, Gino V.
Assuntos: Adenylate Cyclase Toxin ; Adenylyl Cyclases - metabolism ; Amino Acid Sequence ; Animals ; Cell Line ; Cyclic AMP - metabolism ; Enzyme Activation ; GTP-Binding Proteins - metabolism ; Molecular Sequence Data ; Parathyroid Hormone - metabolism ; Pertussis Toxin ; Radioligand Assay ; Rats ; Receptor, Parathyroid Hormone, Type 1 ; Receptors, Parathyroid Hormone - metabolism ; Type C Phospholipases - metabolism ; Virulence Factors, Bordetella - pharmacology
É parte de: The Journal of biological chemistry, 1995-04, Vol.270 (15), p.8458-8465
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
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content type line 23
Descrição: 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.
Editor: United States: Elsevier Inc
Idioma: Inglês

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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

Iida-Klein, Akiko ; Guo, Jun ; Xie, Lin Y. ; Jüppner, Harald ; Potts, John T. ; Kronenberg, Henry M. ; Bringhurst, F. Richard ; Abou-Samra, Abdul B. ; Segre, Gino V.

United States: Elsevier Inc

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