Amiloride enhances the secretion but not the synthesis of renin in renal juxtaglomerular cells. 1991

A Kurtz, and R Della Bruna, and H Scholz, and W Baier
Physiologisches Institut, Universität Regensburg, Federal Republic of Germany.

In this study we have examined a potential role of the sodium/proton exchange system in the regulation of renin secretion. We found that the inhibitors of the Na+/H+ antiport, amiloride (1 mM) and ethylisopropylamiloride (EIPA, 50 microM), led to a 125% increase of renin secretion from cultured mouse juxtaglomerular cells. The stimulatory effect of EIPA on renin secretion was dependent on the extracellular concentrations of sodium and hydrogen ions. While lowering the extracellular pH from 7.3 to 7.0, and lowering [Na+]e from 130 mM to 5 mM had no effect on basal renin release, it markedly attenuated or even blunted the effect of EIPA on renin secretion. The stimulatory effect of forskolin on renin secretion, however, was not altered by decreases of extracellular pH and of sodium. Inhibition of basal renin release was achieved with angiotensin II (1 microM). In the presence of EIPA the inhibitory effect angiotensin II was markedly attenuated. Although effective on renin secretion, neither amiloride nor EIPA exerted a significant effect on the denovo synthesis of renin in cultured mouse JG cells. These findings are compatible with the idea that an amiloride-sensitive transport process, presumably the Na+/H+ exchanger, acts indirectly as an inhibitory signal transduction system for renin secretion from renal juxtaglomerular cells.

UI MeSH Term Description Entries
D007606 Juxtaglomerular Apparatus A complex of cells consisting of juxtaglomerular cells, extraglomerular mesangium lacis cells, the macula densa of the distal convoluted tubule, and granular epithelial peripolar cells. Juxtaglomerular cells are modified SMOOTH MUSCLE CELLS found in the walls of afferent glomerular arterioles and sometimes the efferent arterioles. Extraglomerular mesangium lacis cells are located in the angle between the afferent and efferent glomerular arterioles. Granular epithelial peripolar cells are located at the angle of reflection of the parietal to visceral angle of the renal corpuscle. Apparatus, Juxtaglomerular
D012083 Renin A highly specific (Leu-Leu) endopeptidase that generates ANGIOTENSIN I from its precursor ANGIOTENSINOGEN, leading to a cascade of reactions which elevate BLOOD PRESSURE and increase sodium retention by the kidney in the RENIN-ANGIOTENSIN SYSTEM. The enzyme was formerly listed as EC 3.4.99.19. Angiotensin-Forming Enzyme,Angiotensinogenase,Big Renin,Cryorenin,Inactive Renin,Pre-Prorenin,Preprorenin,Prorenin,Angiotensin Forming Enzyme,Pre Prorenin,Renin, Big,Renin, Inactive
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D002478 Cells, Cultured Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others. Cultured Cells,Cell, Cultured,Cultured Cell
D000584 Amiloride A pyrazine compound inhibiting SODIUM reabsorption through SODIUM CHANNELS in renal EPITHELIAL CELLS. This inhibition creates a negative potential in the luminal membranes of principal cells, located in the distal convoluted tubule and collecting duct. Negative potential reduces secretion of potassium and hydrogen ions. Amiloride is used in conjunction with DIURETICS to spare POTASSIUM loss. (From Gilman et al., Goodman and Gilman's The Pharmacological Basis of Therapeutics, 9th ed, p705) Amidal,Amiduret Trom,Amiloberag,Amiloride Hydrochloride,Amiloride Hydrochloride, Anhydrous,Kaluril,Midamor,Midoride,Modamide,Anhydrous Amiloride Hydrochloride,Hydrochloride, Amiloride,Hydrochloride, Anhydrous Amiloride,Trom, Amiduret
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012504 Saralasin An octapeptide analog of angiotensin II (bovine) with amino acids 1 and 8 replaced with sarcosine and alanine, respectively. It is a highly specific competitive inhibitor of angiotensin II that is used in the diagnosis of HYPERTENSION. 1-Sar-8-Ala Angiotensin II,1-Sarcosine-8-Alanine Angiotensin II,(Sar(1),Ala(8))ANGII,(Sar1,Val5,Ala8)Angiotensin II,Angiotensin II, Sar(1)-Ala(8)-,Angiotensin II, Sarcosyl(1)-Alanine(8)-,Sar-Arg-Val-Tyr-Val-His-Pro-Ala,Saralasin Acetate,Saralasin Acetate, Anhydrous,Saralasin Acetate, Hydrated,1 Sar 8 Ala Angiotensin II,1 Sarcosine 8 Alanine Angiotensin II,Angiotensin II, 1-Sar-8-Ala,Angiotensin II, 1-Sarcosine-8-Alanine,Anhydrous Saralasin Acetate,Hydrated Saralasin Acetate
D017923 Sodium-Hydrogen Exchangers A family of plasma membrane exchange glycoprotein antiporters that transport sodium ions and protons across lipid bilayers. They have critical functions in intracellular pH regulation, cell volume regulation, and cellular response to many different hormones and mitogens. Na(+)-H(+)-Antiporter,Na(+)-H(+)-Exchanger,Sodium-Hydrogen Antiporter,Na(+)-H(+)-Antiporters,Na(+)-H(+)-Exchangers,SLC9 Na(+)-H(+) Exchangers,SLC9 Protein Family,SLC9 Proteins,SLC9-NHE Protein Family,Sodium-Hydrogen Antiporters,Sodium-Hydrogen Exchanger,Sodium-Proton Antiporter,Sodium-Proton Antiporters,Solute Carrier 9 Protein Family,Solute Carrier 9 Proteins,Antiporter, Sodium-Hydrogen,Antiporter, Sodium-Proton,Antiporters, Sodium-Hydrogen,Antiporters, Sodium-Proton,Exchanger, Sodium-Hydrogen,Exchangers, Sodium-Hydrogen,Protein Family, SLC9,Protein Family, SLC9-NHE,SLC9 NHE Protein Family,Sodium Hydrogen Antiporter,Sodium Hydrogen Antiporters,Sodium Hydrogen Exchanger,Sodium Hydrogen Exchangers,Sodium Proton Antiporter,Sodium Proton Antiporters

Related Publications

A Kurtz, and R Della Bruna, and H Scholz, and W Baier
January 2013, Pflugers Archiv : European journal of physiology,
A Kurtz, and R Della Bruna, and H Scholz, and W Baier
September 1996, The American journal of physiology,
A Kurtz, and R Della Bruna, and H Scholz, and W Baier
January 2001, Methods in molecular medicine,
A Kurtz, and R Della Bruna, and H Scholz, and W Baier
July 1995, The American journal of physiology,
A Kurtz, and R Della Bruna, and H Scholz, and W Baier
February 2004, American journal of physiology. Renal physiology,
A Kurtz, and R Della Bruna, and H Scholz, and W Baier
January 1995, The American journal of physiology,
A Kurtz, and R Della Bruna, and H Scholz, and W Baier
October 1998, Pflugers Archiv : European journal of physiology,
A Kurtz, and R Della Bruna, and H Scholz, and W Baier
February 2024, The Journal of physiology,
A Kurtz, and R Della Bruna, and H Scholz, and W Baier
October 1991, The Journal of clinical investigation,
A Kurtz, and R Della Bruna, and H Scholz, and W Baier
September 2020, Kidney international,
Copied contents to your clipboard!