Distribution of parathyroid hormone-stimulated adenylate cyclase in plasma membranes of cells of the kidney cortex

1975 ◽  
Vol 24 (1) ◽  
pp. 131-144 ◽  
Author(s):  
Linda J. Shlatz ◽  
Irving L. Schwartz ◽  
Evamaria Kinne-Saffran ◽  
Rolf Kinne
Keyword(s):  
Parathyroid Hormone ◽  
Adenylate Cyclase ◽  
Plasma Membranes ◽  
Kidney Cortex

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.

CHICK KIDNEY ADENYLATE CYCLASE: SENSITIVITY TO PARATHYROID HORMONE AND SYNTHETIC HUMAN AND BOVINE PEPTIDES

1974 ◽  
Vol 63 (2) ◽  
pp. 369-375 ◽  
Author(s):  
T. J. MARTIN ◽  
N. VAKAKIS ◽  
J. A. EISMAN ◽  
S. J. LIVESEY ◽  
G. W. TREGEAR
Keyword(s):  
Parathyroid Hormone ◽  
Adenylate Cyclase ◽  
Plasma Membranes ◽  
Rat Kidney ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Kidney Cortex ◽  
Rat Kidney Cortex ◽  
Similar Preparation ◽  
Chick Kidney

SUMMARY Adenylate cyclase activity of crude plasma membranes from chick kidney was stimulated by low doses of parathyroid hormone (PTH). Sensitivity to PTH was ten to twenty times greater than that of a similar preparation from rat kidney cortex. Synthetic peptides consisting of the NH2-terminal 34 amino acids of bovine PTH (BPTH) and of human PTH (HPTH) were assayed, as were several analogues of these peptides. Bovine PTH (1–34) and HPTH (1–34) were equivalent in their action on chick kidney but the human peptide had only 20% of the activity of the bovine peptide on rat kidney cortex adenylate cyclase. Bovine proPTH ( −6→ + 34) and (Tyr1)-BPTH (1–34) had less activity than BPTH (1–34). Bovine PTH (2–34) inhibited the response to BPTH (1–34). Neither salmon calcitonin nor vasopressin stimulated adenylate cyclase activity.

EFFECT OF GUANYL NUCLEOTIDES ON PARATHYROID HORMONE-RESPONSIVE ADENYLATE CYCLASE IN CHICK KIDNEY

1976 ◽  
Vol 69 (3) ◽  
pp. 401-412 ◽  
Author(s):  
N. H. HUNT ◽  
T. J. MARTIN ◽  
V. P. MICHELANGELI ◽  
J. A. EISMAN
Keyword(s):  
Parathyroid Hormone ◽  
Adenylate Cyclase ◽  
Plasma Membranes ◽  
Enzyme Activation ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Amino Terminal ◽  
Nucleotide Analogue ◽  
Amino Terminal Fragment ◽  
Chick Kidney

SUMMARY Both guanosine 5′-triphosphate (GTP) and 5′-guanylylimidodiphosphate (Gpp(NH)p) activated adenylate cyclase (EC 4.6.1.1) in chick kidney plasma membranes. Half-maximal stimulation occurred at 3·1 × 10−6 m for both agents. The maximum increases in adenylate cyclase activity produced by GTP and Gpp(NH)p were respectively 130 and 720% over basal activity. At the end of a 12 min incubation period GTP concentration was 85% of that originally added in the presence of an ATP-regenerating system but less than 20% in its absence. GTP and guanosine 5′-diphosphate inhibited the activation of adenylate cyclase by Gpp(NH)p, suggesting that they all acted at a common site. Gpp(NH)p facilitated the stimulation of adenylate cyclase activity by bovine parathyroid hormone (BPTH) and by the synthetic amino terminal fragment BPTH (1–34), decreasing the concentrations required for half-maximal enzyme activation by a factor of approximately eight in both cases. This property was not shared by the native nucleotide GTP. Gpp(NH)p rendered active (at certain concentrations) a synthetic parathyroid hormone peptide fragment, BPTH (2–34), which was incapable of activating adenylate cyclase in the absence of the nucleotide analogue. This suggested that the GTP analogue, in addition to a direct effect upon adenylate cyclase activity, was capable of influencing hormone interaction with the enzyme complex.

STATES OF ACTIVATION OF CHICK KIDNEY ADENYLATE CYCLASE INDUCED BY PARATHYROID HORMONE AND GUANYL NUCLEOTIDES

1977 ◽  
Vol 72 (1) ◽  
pp. 69-79 ◽  
Author(s):  
V. P. MICHELANGELI ◽  
N. H. HUNT ◽  
T. J. MARTIN
Keyword(s):  
Parathyroid Hormone ◽  
Adenylate Cyclase ◽  
Plasma Membranes ◽  
Stable State ◽  
Enzyme Activation ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Incubation Stage ◽  
Subsequent Addition ◽  
Chick Kidney

SUMMARY Several aspects of the activation of adenylate cyclase by guanosine 5′-triphosphate (GTP), 5′-guanylylimidodiphosphate (Gpp(NH)p) and bovine parathyroid hormone (bPTH) have been studied in chick kidney plasma membrane preparations. GTP (10−4 mol/l), Gpp(NH)p (10−4 mol/l) and bPTH (10 i.u./ml) activated adenylate cyclase without any significant time lag. However a 2 min delay was observed before the activity of the enzyme increased after the addition of bPTH (−6 → + 34) to incubations. The early (0–3 min) effects of GTP and Gpp(NH)p upon chick kidney adenylate cyclase activity were antagonized by the addition of the alternative guanyl nucleotide. After 5 min of incubation with kidney plasma membranes, Gpp(NH)p induced a stable state of activation of adenylate cyclase which was not reversible by subsequent addition of GTP. GTP did not induce an irreversible state of enzyme activation. In pre-incubation studies, GTP did not produce a persistent enzyme activation and did not modify the effect of Gpp(NH)p added subsequently at the incubation stage. Gpp(NH)p produced a stable state of activation of adenylate cyclase which was not inhibited by addition of GTP at the incubation stage. Bovine PTH (2–34) inhibited the effect of bPTH upon adenylate cyclase activity when the native hormone (10 i.u./ml) had been incubated with plasma membranes for up to 8 min before addition of the analogue (5 μg/ml). Incubation of plasma membranes with bPTH (2–34) for as little as 10 s prevented activation of adenylate cyclase by subsequent addition of bPTH. This pattern was confirmed in pre-incubation studies. After pre-incubation of kidney membranes with bPTH and bPTH (2–34), followed by washing, an acid extract of the membranes contained immunoreactive bPTH. Gpp(NH)p produced a greater increase in adenylate cyclase activity in membranes pre-incubated with bPTH or bPTH (2–34) than in membranes pre-incubated with buffer alone, suggesting that the hormone and analogue facilitated the interaction of Gpp(NH)p with adenylate cyclase.

scholarly journals Cortical cell populations from rabbit kidney isolated by free-flow electrophoresis: characterization by measurement of hormone-sensitive adenylate cyclase.

1982 ◽  
Vol 92 (2) ◽  
pp. 505-513 ◽  
Author(s):  
A Vandewalle ◽  
B Köpfer-Hobelsberger ◽  
H G Heidrich
Keyword(s):  
Alkaline Phosphatase ◽  
Parathyroid Hormone ◽  
Adenylate Cyclase ◽  
Fast Moving ◽  
Cortical Cell ◽  
Free Flow ◽  
Rabbit Kidney ◽  
Kidney Cortex ◽  
Cell Populations ◽  
Slow Moving

Free-flow electrophoresis allows the separation of different cell populations from a cell suspension isolated from rabbit kidney cortex after perfusion of the kidneys with a calcium-binder, followed by gentle mechanical treatment. After electrophoretic separation, analysis of the adenylate cyclase activities after stimulation by various hormones allows the precise determination of the origin of the cell populations with different electrophoretic mobilities. Adenylate cyclase from the slow-moving main cell population was only sensitive to parathyroid hormone. These cells had also high alkaline phosphatase content, further demonstrating their proximal origin. The various fast-moving cell populations had adenylate cyclase sensitive to isoproterenol and arginine vasopressin but were less sensitive to parathyroid hormone than the slow-moving cells. Their alkaline phosphatase content was also much lower. This indicates that these fast-moving cell populations originate from both the granulous segment of the distal tubule and from the collecting ducts. The adenylate cyclase activity and the cyclic AMP contents of isolated proximal cells maintained in culture medium were also investigated.

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