The Influence of Magnesium Deficiency and Parathyroid Hormone on Adenosine 3′:5′-Cyclic Monophosphate Concentrations in Rat Kidney Cortex

1973 ◽  
Vol 1 (4) ◽  
pp. 884-886 ◽  
Author(s):  
J. P. ASHBY ◽  
F. W. HEATON
1989 ◽  
Vol 77 (3) ◽  
pp. 273-279 ◽  
Author(s):  
Karen Pardy ◽  
B. C. Williams ◽  
A. R. Noble

1. The role of Ca2+ in the control of renin release was investigated using a collagenase-dispersed rat kidney cortex cell preparation. 2. Superfusion with a series of low [Ca2+] buffers in either ascending or descending order of concentration increased renin release. Exposure to 0.06 mmol/l Ca2+ increased release by 120% (P < 0.001) when presented as the first buffer in ascending order of concentration and by 79% (P < 0.001) when presented as the fourth and last in a series of descending order. 3. The Ca2+ entry blocking drug diltiazem in a range of concentrations increased renin release and at 10−5 mol/l diltiazem the mean stimulation was 35% (P < 0.01). 4. 8-(N,N-Diethylamino)octyl-3,4,5-trimethoxybenzoate (TMB-8) reduces the release of Ca2+ from intracellular stores and, studied over a range of concentrations, this compound increased renin release. At 10−5 mol/l TMB-8 the mean increase was 44% (P < 0.001). 5. None of these experimental manipulations, low [Ca2+], diltiazem or TMB-8, had any effect on the release of adenosine 3′:5′-cyclic monophosphate into the cell superfusate, indicating that a decrease in intracellular [Ca2+] increases renin release by a mechanism which is independent of changes in adenosine 3′:5′-cyclic monophosphate production. 6. Effects of low [Ca2+], diltiazem and TMB-8 on renin secretion were all shown to be reversible when superfusion with control buffer was resumed.


1974 ◽  
Vol 63 (2) ◽  
pp. 369-375 ◽  
Author(s):  
T. J. MARTIN ◽  
N. VAKAKIS ◽  
J. A. EISMAN ◽  
S. J. LIVESEY ◽  
G. W. TREGEAR

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.


1973 ◽  
Vol 134 (1) ◽  
pp. 157-165 ◽  
Author(s):  
Anne Roobol ◽  
George A. O. Alleyne

1. The effect of Ca2+, glucagon, adrenaline and adenosine 3′:5′-cyclic monophosphate on gluconeogenesis by rat kidney-cortex slices was studied. 2. Glucose formation from a range of substrates, with the exception of glycerol, was increased by an increase in extracellular Ca2+ concentration. 3. Hormones and adenosine 3′:5′-cyclic monophosphate, at low Ca2+ concentrations, stimulated glucose production from several substrates, but not from glycerol, fructose, malate or fumarate. 4. Hormonal stimulation was not detected in the absence of Ca2+ or at 2.5mm-Ca2+. 5. Ca2+, hormones and adenosine 3′:5′-cyclic monophosphate had no effect on phosphoenolpyruvate carboxylase activity. 6. It is proposed that Ca2+ and adenosine 3′:5′-cyclic monophosphate-mediated hormone action activate the same rate-limiting step in gluconeogenesis: this step is tentatively identified as the rate of transfer of substrates across the mitochondrial membrane.


1994 ◽  
Vol 269 (9) ◽  
pp. 6637-6639
Author(s):  
A. Werner ◽  
S.A. Kempson ◽  
J. Biber ◽  
H. Murer

1973 ◽  
Vol 158 (2) ◽  
pp. 597-604 ◽  
Author(s):  
Åke Ellin ◽  
Sten Orrenius ◽  
Åke Pilotti ◽  
Carl-Gunnar Swahn

1978 ◽  
Vol 172 (1) ◽  
pp. 57-62 ◽  
Author(s):  
W Haase ◽  
A Schäfer ◽  
H Murer ◽  
R Kinne

Orientation of rat renal and intestinal brush-border membrane vesicles was studied with two independent methods: electron-microscopic freeze-fracture technique and immunological methods. With the freeze-fracture technique a distinct asymmetric distribution of particles on the two membrane fracture faces was demonstrated; this was used as a criterion for orientation of the isolated membrane vesicles. For the immunological approach the accessibility or inaccessibility of aminopeptidase M localized on the outer surface of the cell membrane to antibodies was used. With both methods we showed that the brush-border membrane vesicles isolated from rat kidney cortex and from rat small intestine for transport studies are predominantly orientated right-side out.


Author(s):  
Kodo Ito ◽  
Kenichi Yamada ◽  
Setsuko Yoshida ◽  
Keiji Hasunuma ◽  
Yasushi Tamura ◽  
...  

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