The Stimulation of Na+, K+-ATPase Activity in the Medulla of the Rat Kidney by [arginine] Vasopressin and Its Analogues

1984 ◽  
Vol 66 (5) ◽  
pp. 561-567 ◽  
Author(s):  
Corinna Pippard ◽  
P. H. Baylis
Keyword(s):  
Atpase Activity ◽  
Arginine Vasopressin ◽  
Rat Kidney ◽  
Arginine Vasotocin ◽  
Minimum Essential Medium ◽  
Outer Medulla ◽  
Tubular Cells ◽  
Lysine Vasopressin ◽  
Convoluted Tubules ◽  
Stimulation Of

1. Total and Na+,K+-ATPase activities have been measured in sections (10 μm thick) from blocks of rat kidney cultured for 5 h at 37°C, pH 7.5, in Glasgow Eagle's Minimum Essential Medium. 2. Synthetic [arginine]vasopressin ([Arg]VP) stimulated ATPase activity in the thick tubular cells of the renal outer medulla over the concentration range 0.01-10 fmol/l, but failed to affect ATPase activity in the proximal and distal convoluted tubules of the cortex. 3. The increase in medullary total ATPase activity induced by [Arg]VP and its analogues was wholly due to stimulation of Na+,K+-ATPase activity. 4. Stimulation of medullary ATPase activity was blocked by [Arg]VP antiserum. 5. The [Arg]VP analogues desmopressin, [lysine]vasopressin, [arginine]vasotocin and oxytocin stimulated medullary Na+,K+-ATPase activity, the three last-named analogues being considerably less potent than [Arg]VP.

Prolactin stimulates Na+-K+-ATPase activity located in the outer renal medulla of the rat

1986 ◽  
Vol 108 (1) ◽  
pp. 95-99 ◽  
Author(s):  
C. Pippard ◽  
P. H. Baylis
Keyword(s):  
Enzyme Activity ◽  
Atpase Activity ◽  
Arginine Vasopressin ◽  
Renal Medulla ◽  
Outer Medulla ◽  
Stimulatory Action ◽  
Maximal Stimulation ◽  
Human Prolactin ◽  
Cytochemical Technique ◽  
Stimulation Of

ABSTRACT The effect of rat prolactin on rat renal Na+-K+-ATPase activity was investigated by a cytochemical technique. Rat prolactin caused stimulation of Na+-K+-ATPase activity only in the outer medulla of the kidney, and not in renal cortical structures. Peak enzyme activity in cultured rat renal segments occurred after tissue had been exposed to rat prolactin for 2 min, and the time of maximal stimulation did not vary with the concentration of prolactin. There was a curvilinear response in Na +-K+-ATPase activity over the rat prolactin concentration range, 0·04–40 ng/1, but higher prolactin concentrations caused inhibition of enzyme activity. Na+-K+-ATPase response was totally blocked by specific rat prolactin antiserum. Human prolactin had no consistent effect on rat medullary Na+-K+-ATPase activity. Addition of specific tri-iodothyronine and arginine vasopressin antisera to rat prolactin was without effect, confirming that the stimulatory action of rat prolactin on Na+-K+-ATPase was not due to contamination with these hormones which are known to stimulate this enzyme. J. Endocr. (1986) 108, 95–99

Localization of mRNAs coding for isozymes of plasma membrane Ca(2+)-ATPase pump in rat kidney

1992 ◽  
Vol 263 (1) ◽  
pp. F7-F14 ◽  
Author(s):  
M. Magosci ◽  
M. Yamaki ◽  
J. T. Penniston ◽  
T. P. Dousa
Keyword(s):  
Plasma Membrane ◽  
Rat Kidney ◽  
Rat Plasma ◽  
Rt Pcr ◽  
Chain Reaction ◽  
Outer Medulla ◽  
Unique Distribution ◽  
Polymerase Chain ◽  
Convoluted Tubules ◽  
Specific Mrna

We have studied localization of mRNAs coding isozymes of rat plasma membrane Ca(2+)-adenosinetriphosphatase pump (rPMCA) in the rat kidney, with use of reverse transcription (RT) with subsequent amplification by polymerase chain reaction (PCR). When zones of the kidney were separated by macrodissection, a large amount of mRNA coding isozyme rPMCA1 was found in all zones; mRNA for isozyme rPMCA2 was abundant in cortex and in outer medulla, and mRNA for isozyme rPMCA3 was prominent in outer medulla. The mRNAs were analyzed in microdissected cortical nephron segments by use of RT-PCR approach described previously [T. Moriyama, H. R. Murphy, B. M. Martin, and A. Garcia-Perez. Am. J. Physiol. 258 (Renal Fluid Electrolyte Physiol. 27): F1470-F1474, 1990]. We detected mRNA for isozyme rPMCA2 in microdissected distal convoluted tubules (DCT) and in cortical thick ascending limbs (CTAL) and, less consistently, also in proximal convoluted tubule and in glomeruli. The mRNA for isozyme rPMCA1 was abundant in glomeruli but was absent in all examined cortical tubular segments. Our results document that mRNAs for all three major isozymes of rPMCA are present and show a unique distribution in the three major zones of rat renal parenchyma. Specific mRNA coding for rPMCA2 was detected in cortical tubules, namely in CTAL and DCT, whereas mRNA coding isozyme rPMCA1 was found in glomeruli. We suggest that isozyme rPMCA2 might be specifically related to epithelial cells and their function, whereas rPMCA1 is probably a component of nonepithelial cells including these in glomeruli.

Mechanism of prostaglandin E2-induced increase of proximal sodium reabsorption in the rat

1990 ◽  
Vol 258 (1) ◽  
pp. R82-R86 ◽  
Author(s):  
Y. Kinoshita ◽  
F. G. Knox
Keyword(s):  
Angiotensin Ii ◽  
Prostaglandin E2 ◽  
Rat Kidney ◽  
Sodium Reabsorption ◽  
Sprague Dawley ◽  
Sprague Dawley Rats ◽  
Convoluted Tubules ◽  
Stimulation Of ◽  
Interstitial Infusion

Prostaglandin E2, when infused directly into the renal interstitium, enhances sodium reabsorption by the superficial proximal convoluted tubules of anesthetized Sprague-Dawley rats. The present study was designed to investigate the role of angiotensin II in the prostaglandin E2-induced stimulation of proximal sodium reabsorption. Micropuncture at the superficial late proximal tubule demonstrated a significant increase in the fractional reabsorption of sodium from 39.9 +/- 2.3% in control conditions to 51.8 +/- 3.0% (n = 9, P less than 0.01) during the renal interstitial infusion of prostaglandin E2. The stimulatory effect of prostaglandin E2 on proximal sodium reabsorption was markedly attenuated by pretreatment with saralasin. During intravenous saralasin infusion, prostaglandin E2 did not significantly change the fractional reabsorption of sodium from 42.2 +/- 5.8 to 45.4 +/- 6.0% (n = 7, NS). In summary, the stimulatory effect of renal interstitial infusion of prostaglandin E2 on proximal sodium reabsorption was attenuated by pretreatment with saralasin. Therefore renal interstitial infusion of prostaglandin E2 may enhance proximal sodium reabsorption, at least in part, through stimulation of angiotensin II production in the rat kidney.

Stimulation of Na+/K+-ATPase activity by polyamines in the rat renal medullary cells of the thick ascending limb of Henle's loop

1990 ◽  
Vol 127 (3) ◽  
pp. 377-382 ◽  
Author(s):  
J. A. Charlton ◽  
P. H. Baylis
Keyword(s):  
Atpase Activity ◽  
Arginine Vasopressin ◽  
Thick Ascending Limb ◽  
Stimulus Response ◽  
Spermine Synthase ◽  
Medullary Thick Ascending Limb ◽  
Henle's Loop ◽  
Specific Inhibitors ◽  
Stimulation Of

ABSTRACT Previous studies have indicated that ornithine decarboxylase (ODC) may be involved in the stimulation of Na+/K+-ATPase activity by arginine vasopressin (AVP) in the rat renal medullary thick ascending limb of Henle's loop. The present study was aimed at establishing the role of the polyamines, the conversion products of ODC activity, in the stimulation of Na+/K+-ATPase by AVP. Using cytochemical methods, we have demonstrated an increase in Na+/K+-ATPase activity after stimulation with putrescine, spermidine and spermine (each 1 mmol/l) for 2·5,2 and 1·5 min respectively. The specific inhibitors of spermidine and spermine synthase, bis-cyclohexylammonium sulphate and N-alkylated-1,3-diaminopropane respectively, inhibited the stimulation of Na+/K+-ATPase by AVP, this inhibition being reversed by spermine. These findings suggest that polyamines are involved in the stimulus-response coupling of the hormone-mediated response. Journal of Endocrinology (1990) 127, 377–382

scholarly journals Aldose reductase and sorbitol dehydrogenase distribution in rat kidney.

1977 ◽  
Vol 25 (1) ◽  
pp. 1-8 ◽  
Author(s):  
C N Corder ◽  
J G Collins ◽  
T S Brannan ◽  
J Sharma
Keyword(s):  
Aldose Reductase ◽  
Alloxan Diabetes ◽  
Rat Kidney ◽  
Sorbitol Dehydrogenase ◽  
Outer Medulla ◽  
Developing Kidney ◽  
Enzymatic Changes ◽  
Developing Rat ◽  
Convoluted Tubules ◽  
Sorbitol Pathway

The sorbitol pathway catalyzes the conversion of glucose to fructose via the intermediate sorbitol. It consists of aldose reductase (AR) and sorbitol dehydrogenase (SDH). In adult (44 day) kidney zones, AR was highest in the outer medulla. In substructures AR was highest in distal convoluted tubule. The AR was greatest in newborn and 8-day zones of developing rat kidney. Acute alloxan diabetes was associated with decreased AR in small arteries, but not glomeruli. The SDH was lowest in outer medulla. It was most active in glomeruli and distal convoluted tubules. The diabetic state leads to no change of SDH in arteries but an increase in glomeruli. SDH increased with development. This study demonstrates AR and SDH in substructures of the kidney. The pathway is present in developing kidney. In diabetes the enzymatic changes would tend to decrease accumulation of sorbitol.

Stimulation of rat renal medullary Na+/K+-ATPase by arginine vasopressin is mediated by the V2 receptor

1990 ◽  
Vol 127 (2) ◽  
pp. 213-216 ◽  
Author(s):  
J. A. Charlton ◽  
P. H. Baylis
Keyword(s):  
Atpase Activity ◽  
Arginine Vasopressin ◽  
Thick Ascending Limb ◽  
Medullary Thick Ascending Limb ◽  
Henle's Loop ◽  
Cytochemical Bioassay ◽  
V2 Receptor ◽  
Stimulation Of

ABSTRACT In previous studies, we have demonstrated that 1–10 fmol arginine vasopressin (AVP)/l maximally stimulates the activity of the enzyme Na+/K+-ATPase in the rat renal medullary thick ascending limb (MTAL) of Henle's loop after 4 or 10 min of stimulation when measured using a cytochemical bioassay. We have tested the hypothesis that this stimulation is mediated by the V2 receptor in the MTAL. A cytochemical bioassay was used to investigate the effect of specific V1 and V2/V1 antagonists and a synthetic V2 agonist [1-deamino,8-d-arginine]-vasopressin (dDAVP), on the activity of Na+/K+-ATPase. There was no effect of the V1 antagonist (1 fmol-1 μmol/l) in inhibiting the activity of Na+/K+-ATPase stimulated by 1 fmol AVP/l. In contrast, 100 pmol of the V2/V1 antagonist/l significantly (P < 0·001) inhibited the stimulation of Na+/K+-ATPase activity by 1 fmol AVP/l from 55·5±4·3 (s.e.m.) to 31·9±1·6 mean integrated extinction (MIE) after 4 min of stimulation and from 67·0±3·2 to 36·9±0·7 MIE after 10 min of stimulation. Similarly, the stimulation of Na+/K+-ATPase by 10 fmol dDAVP/l was inhibited by the V2/V1 antagonist from 55·1±1·0 to 26·1±0·5 MIE after 4 min of stimulation. We conclude that the stimulation of Na+/K+-ATPase by AVP is mediated by the V2 receptor in the rat renal MTAL. Journal of Endocrinology (1990) 127, 213–216

scholarly journals Cellular and subcellular localization of enzymes of arginine metabolism in rat kidney

1992 ◽  
Vol 282 (2) ◽  
pp. 369-375 ◽  
Author(s):  
S N Dhanakoti ◽  
M E Brosnan ◽  
G R Herzberg ◽  
J T Brosnan
Keyword(s):  
Rat Kidney ◽  
Subcellular Fractionation ◽  
Kidney Cortex ◽  
Ornithine Aminotransferase ◽  
Outer Medulla ◽  
Argininosuccinate Synthase ◽  
Distal Tubules ◽  
Convoluted Tubules ◽  
Inner Cortex ◽  
Proximal Convoluted Tubules

Rat kidneys extract citrulline derived from the intestinal metabolism of glutamine and convert it stoichiometrically into arginine. This pathway constitutes the major endogenous source of arginine. We investigated the localization of enzymes of arginine synthesis, argininosuccinate synthase and lyase, and of breakdown, arginase and ornithine aminotransferase, in five regions of rat kidney, in cortical tubule fractions and in subcellular fractions of cortex. Argininosuccinate synthase and lyase were found almost exclusively in cortex. Arginase and ornithine aminotransferase were found in inner cortex and outer medulla. Since cortical tissue primarily consists of proximal convoluted and straight tubules, distal tubules and glomeruli, we prepared cortical tubule fragments by collagenase digestion of cortices and fractionated them on a Percoll gradient. Argininosuccinate synthase and lyase were found to be markedly enriched in proximal convoluted tubules, whereas less than 10% of arginase and ornithine aminotransferase, were recovered in this fraction. Arginine production from citrulline was also enriched in proximal convoluted tubules. Subcellular fractionation of kidney cortex revealed that argininosuccinate synthase and lyase are cytosolic. We therefore conclude that arginine synthesis occurs in the cytoplasm of the cells of the proximal convoluted tubule.

scholarly journals Immunohistochemical Localization of Arginine and Citrulline in Rat Renal Tissue

1997 ◽  
Vol 45 (6) ◽  
pp. 875-881 ◽  
Author(s):  
Eiko Aoki ◽  
Ikuo K. Takeuchi
Keyword(s):  
Amino Acids ◽  
Epithelial Cells ◽  
Rat Kidney ◽  
Immunohistochemical Method ◽  
Moderate Intensity ◽  
Outer Medulla ◽  
Collecting Ducts ◽  
Outer Stripe ◽  
Convoluted Tubules ◽  
Proximal Convoluted Tubules

Using antibodies highly specific for L-arginine and L-citrulline, we localized these amino acids in rat kidney with immunohistochemical methods. Highest levels of arginine immunoreactivity were observed in epithelial cells of proximal tubules in the outer stripe of the outer medulla and the collecting ducts in the cortex. Staining intensity of proximal convoluted tubules in the outer stripe decreased from the inner side to the outer side. In the inner medulla, collecting ducts were labeled with moderate intensity. Staining within the cortex was apparent only with collecting ducts. Citrulline immunoreactivity was localized in the epithelial cells of collecting ducts both in the cortex and medulla. Immunoreactivity was also found in glomerular podocytes and in the epithelial cells of proximal convoluted tubules in the outer medulla. These localizations were different from those of other amino acids previously reported. The precise cellular distribution of arginine and citrulline in rat kidney was determined for the first time by an immunohistochemical method in the present study.

scholarly journals Comparison of the distribution of tissue kallikrein and esterase A, a kallikrein-like enzyme, in rat kidney using specific monoclonal antibodies.

1988 ◽  
Vol 36 (10) ◽  
pp. 1251-1254 ◽  
Author(s):  
J A Simson ◽  
J L Condon ◽  
L Chao ◽  
J Chao
Keyword(s):  
Monoclonal Antibodies ◽  
Collecting Duct ◽  
Rat Kidney ◽  
Tissue Kallikrein ◽  
Cortical Collecting Duct ◽  
Kidney Tubule ◽  
Outer Medulla ◽  
Apical Cytoplasm ◽  
Straight Tubules ◽  
Convoluted Tubules

Tissue kallikrein (E.C. 3.4.21.35) and arginine esterase A, another closely related, kinin-generating serine protease, have been localized by immunocytochemistry in rat kidney, using monoclonal antibodies that do not crossreact with other kallikrein-related enzymes or with tonin. Kallikrein was present primarily in the apical cytoplasm of the connecting tubule and the cortical collecting duct. Esterase A, on the other hand, was present primarily in the basolateral region of both proximal and distal straight tubules in the outer medulla and medullary rays. In addition, esterase A was demonstrable in distal convoluted tubules and, to a lesser extent, in proximal convoluted tubules. The presence of different kinin-generating enzymes at these sites would permit the formation of kinins from appropriate substrates on both the vascular and luminal poles of separate segments of the kidney tubule.

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