Parathyroid Hormone Receptor in Bovine Kidney Cortex Plasma Membranes

1973 ◽  
Vol 44 (6) ◽  
pp. 25P-26P
Author(s):  
H. S. Sutcliffe ◽  
T. J. Martin
Keyword(s):  
Parathyroid Hormone ◽  
Hormone Receptor ◽  
Plasma Membranes ◽  
Kidney Cortex ◽  
Bovine Kidney ◽  
Parathyroid Hormone Receptor

scholarly journals Binding of parathyroid hormone to bovine kidney-cortex plasma membranes

1973 ◽  
Vol 134 (4) ◽  
pp. 913-921 ◽  
Author(s):  
H. S. Sutcliffe ◽  
T. J. Martin ◽  
J. A. Eisman ◽  
R. Pilczyk
Keyword(s):  
Parathyroid Hormone ◽  
Adenylate Cyclase ◽  
Plasma Membranes ◽  
Specific Activity ◽  
Specific Binding ◽  
Rat Kidney ◽  
Kidney Cortex ◽  
Bovine Kidney ◽  
Hormone Sensitive ◽  
Chloramine T

1. Plasma membranes were purified from bovine kidney cortex, with a fourfold increase in specific activity of parathyroid hormone-sensitive adenylate cyclase over that in the crude homogenate. The membranes were characterized by enzyme studies. 2. Parathyroid hormone was labelled with 125I by an enzymic method and the labelled hormone shown to bind to the plasma membranes and to be specifically displaced by unlabelled hormone. Parathyroid hormone labelled by the chloramine-t procedure showed no specific binding. 75Se-labelled human parathyroid hormone, prepared in cell culture, also bound to the membranes. 3. Parathyroid hormone was shown to retain biological activity after iodination by the enzymic method, but no detectable activity remained after chloramine-t treatment. 4. High concentration of pig insulin inhibited binding of labelled parathyroid hormone to plasma membranes and partially inhibited the hormone-sensitive adenylate cyclase activity in a crude kidney-cortex preparation. 5. EDTA enhanced and Ca2+ inhibited binding of labelled parathyroid hormone to plasma membranes. 6. Whereas rat kidney homogenates were capable of degrading labelled parathyroid hormone to trichloroacetic acid-soluble fragments, neither crude homogenates nor purified membranes from bovine kidney showed this property. 7. Binding of parathyroid hormone is discussed in relation to metabolism and initial events in hormone action.

Dissociation of β-Arrestin-Dependent Desensitization and Signaling Using 'Biased' Parathyroid Hormone Receptor Ligands

2019 ◽  
Author(s):  
Kathryn M. Appleton ◽  
Mi-Hye Lee ◽  
Erik G. Strungs ◽  
Carlos Nogueras-Ortiz ◽  
Diane Gesty-Palmer ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Hormone Receptor ◽  
Receptor Ligands ◽  
Parathyroid Hormone Receptor

scholarly journals Use of Backbone Modification To Enlarge the Spatiotemporal Diversity of Parathyroid Hormone Receptor-1 Signaling via Biased Agonism

2019 ◽  
Vol 141 (37) ◽  
pp. 14486-14490 ◽  
Author(s):  
Shi Liu ◽  
Frederic G. Jean-Alphonse ◽  
Alex D. White ◽  
Denise Wootten ◽  
Patrick M. Sexton ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
Hormone Receptor ◽  
Parathyroid Hormone Receptor ◽  
Biased Agonism ◽  
Backbone Modification
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