Modulation of ouabain-insensitive Na+-ATPase activity in the renal proximal tubule by Mg2+, MgATP and furosemide

Caruso-Neves, Celso; Coelho-Souza, S.A.; Vives, D.; Goes, G.; Lara, Lucienne S.; Lopes, Anibal Gil

doi:10.1016/s1357-2725(02)00059-6

Cited by 29 publications

(20 citation statements)

References 26 publications

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“…All the reagents were obtained from SIGMA, USA. The ATPase activity was measured according to the method previously described [9][10][11][12][13]. The reaction was started by the addition of the homogenates to a final protein concentration of 0.1-0.3 mg/ml, and stopped after 10 minutes by the addition of charcoal activated by HCl (0.1 N).…”

Section: Methodsmentioning

confidence: 99%

“…Due to its fundamental role in the physiological cellular homeostasis, the lack of expression of Na + ,K + -ATPase in IC is an intriguing condition. On the other hand, the furosemide inhibitable, ouabain insensitive Na + -ATPase [7,8] has been detected in proximal tubules and in MDCK cells [9,10], being modulated by hormones and autacoids such as angiotensin, and adenosine [11][12][13]. This enzyme could be the alternate molecular mechanism responsible for adequate survival of these cells in the absence of the classical Na + ,K + -ATPase sensitive to ouabain.…”

Section: Introductionmentioning

confidence: 99%

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Lack of Na+,K+-ATPase expression in intercalated cells may be compensated by Na+-ATPase: A study on MDCK – C11 cells

Sampaio

Bezerra

Peçanha

et al. 2008

Cell. Mol. Life Sci.

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The lack of Na(+),K(+)-ATPase expression in intercalated cells (IC) is an intriguing condition due to its fundamental role in cellular homeostasis. In order to better understand this question we compared the activities of Na(+),K(+)-ATPase and Na(+)-ATPase in two MDCK cell clones: the C11, with IC characteristics, and the C7, with principal cells (PC) characteristics. The Na(+),K(+)-ATPase activity found in C11 cells is far lower than in C7 cells and the expression of its beta-subunit is similar in both cells. On the other hand, a subset of C11 without alpha-subunit expression has been found. In C11 cells the Na(+)-ATPase activity is higher than that of the Na(+),K(+)-ATPase, and it is increased by medium alkalinization, suggesting that it could account for the cellular Na(+)-homeostasis. Although further studies are necessary for a better understanding of these findings, the presence of Na(+)-ATPase may explain the adequate survival of cells that lack Na(+),K(+)-ATPase.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Lack of Na+,K+-ATPase expression in intercalated cells may be compensated by Na+-ATPase: A study on MDCK – C11 cells

Sampaio

Bezerra

Peçanha

et al. 2008

Cell. Mol. Life Sci.

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“…ATPase activity was measured as previously reported [26-28]. Na + -ATPase and (Na + ,K + )-ATPase activities expressed in nmol Pi x mg -1 x min -1 were obtained by subtracting the enzyme activity in the absence and presence of furosemide (2 mM) and ouabain (1 mM), respectively [27,28]. …”

Section: Methodsmentioning

confidence: 99%

The effect of saponins from Ampelozizyphus amazonicus Ducke on the renal Na+ pumps’ activities and urinary excretion of natriuretic peptides

Diniz

Portella

Cardoso

et al. 2012

BMC Complement Altern Med

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BackgroundIn a previous study, we showed that a saponin mixture isolated from the roots of Ampelozizyphus amazonicus Ducke (SAPAaD) reduces urine excretion in rats that were given an oral loading of 0.9 % NaCl (4 ml/100 g body weight). In the present study, we investigated whether atrial natriuretic peptides (ANP) and renal ATPases play a role in the SAPAaD- induced antidiuresis in rats.MethodsTo evaluate the effect of SAPAaD on furosemide-induced diuresis, Wistar rats (250-300 g) were given an oral loading of physiological solution (0.9 % NaCl, 4 ml/100 g body weight) to impose a uniform water and salt state. The solution containing furosemide (Furo, 13 mg/kg) was given 30 min after rats were orally treated with 50 mg/kg SAPAaD (SAPAaD + Furo) or 0.5 ml of 0.9 % NaCl (NaCl + Furo). In the SAPAaD + NaCl group, rats were pretreated with SAPAaD and 30 min later they received the oral loading of physiological solution. Animals were individually housed in metabolic cages, and urine volume was measured every 30 min throughout the experiment (3 h). To investigate the role of ANP and renal Na+ pumps on antidiuretic effects promoted by SAPAaD, rats were given the physiological solution (as above) containing SAPAaD (50 mg/kg). After 90 min, samples of urine and blood from the last 30 min were collected. Kidneys and atria were also removed after previous anesthesia. ANP was measured by radioimmunoassay (RIA) and renal cortical activities of Na+- and (Na+,K+)-ATPases were calculated from the difference between the [32P] Pi released in the absence and presence of 1 mM furosemide/2 mM ouabain and in the absence and presence of 1 mM ouabain, respectively.ResultsIt was observed that SAPAaD inhibited furosemide-induced diuresis (at 90 min: from 10.0 ± 1.0 mL, NaCl + Furo group, n = 5, to 5.9 ± 1.0 mL, SAPAaD + Furo group n = 5, p < 0.05), increased both Na+-ATPase (from 25.0 ± 5.9 nmol Pi.mg-1.min-1, control, to 52.7 ± 8.9 nmol Pi.mg-1.min-1, p < 0.05) and (Na+,K+)-ATPase (from 47.8 ± 13.3 nmol Pi.mg-1.min-1, control, to 79.8 ± 6.9 nmol Pi .mg-1.min-1, p < 0.05) activities in the renal cortex. SAPAaD also lowered urine ANP (from 792 ± 132 pg/mL, control, to 299 ± 88 pg/mL, p < 0.01) and had no effect on plasma or atrial ANP.ConclusionWe concluded that the SAPAaD antidiuretic effect may be due to an increase in the renal activities of Na+- and (Na+,K+)-ATPases and/or a decrease in the renal ANP.

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“…The limiting step of sodium reabsorption in the proximal tubule is basolateral membrane transport (Feraille & Doucet, 2001). This transport is mediated by two sodium pumps: the classic ouabain‐sensitive Na + –K + ‐ATPase and the ouabain‐insensitive, furosemide‐sensitive Na + ‐ATPase, called the second sodium pump (Proverbio et al 1989; Feraille & Doucet, 2001; Caruso‐Neves et al 2002; De Souza et al 2007). Both enzymes are involved in the genesis of the sodium electrochemical gradient and are the target of the hormones involved in the regulation of extracellular volume (Rangel et al 1999; Feraille & Doucet, 2001; Caruso‐Neves et al 2004).…”

mentioning

confidence: 99%

“…Both enzymes are involved in the genesis of the sodium electrochemical gradient and are the target of the hormones involved in the regulation of extracellular volume (Rangel et al 1999; Feraille & Doucet, 2001; Caruso‐Neves et al 2004). Furthermore, the observation that Na + ‐ATPase is about 10 times less active than Na + –K + ‐ATPase (Rangel et al 1999; Caruso‐Neves et al 2002) suggests that this enzyme may be involved in fine tuning, whereas Na + –K + ‐ATPase is responsible for most of the Na + reabsorption in the proximal tubule.…”

mentioning

confidence: 99%

The angiotensin receptor type 1–G_q protein–phosphatidyl inositol phospholipase Cβ–protein kinase C pathway is involved in activation of proximal tubule Na⁺‐ATPase activity by angiotensin(1–7) in pig kidneys

Lara¹,

Corrêa²,

Lavelle³

et al. 2008

Experimental Physiology

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In a previous study, we observed that angiotensin(1-7) (Ang(1-7)) stimulates proximal tubule Na+-ATPase activity through the angiotensin receptor type 1 (AT1R). Here we aimed to study the signalling pathways involved. Our results show that the stimulatory effect of Ang(1-7) on Na+-ATPase activity through AT1R involves a Gq protein-phosphatidyl inositol-phospholipase Cbeta (PI-PLCbeta) pathway because: (1) the effect was reversed by GDPbetaS, a non-hydrolysable GDP analogue, and by a monoclonal Gq protein antibody; (2) the effect was similar and not additive to that of GTPgammaS, a non-hydrolysable GTP analogue; (3) Ang(1-7) induced a rapid decrease (30 s) in phosphatidylinositol 4,5-bisphosphate levels, a PI-PLCbeta substrate; and (4) U73122, a specific inhibitor of PI-PLCbeta, abolished Ang(1-7)-induced stimulation of Na+-ATPase activity. Angiotensin(1-7) increased the protein kinase C (PKC) activity similarly to phorbol-12-myristate-13-acetate (PMA), an activator of PKC. This effect was reversed by losartan, a specific antagonist of AT1R. The stimulatory effects of Ang(1-7) and PMA on Na+-ATPase activity are similar, non-additive and reversed by calphostin C, a specific inhibitor of PKC. A catalytic subunit of PKC (PKC-M) increased the Na+-ATPase activity. These data show that Ang(1-7) stimulates Na+-ATPase activity through the AT1R-Gq protein-PI-PLCbeta-PKC pathway. This effect is similar to that described for angiotensin II, showing for the first time that these compounds could have similar effects in the renal system.

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Modulation of ouabain-insensitive Na+-ATPase activity in the renal proximal tubule by Mg2+, MgATP and furosemide

Cited by 29 publications

References 26 publications

Lack of Na+,K+-ATPase expression in intercalated cells may be compensated by Na+-ATPase: A study on MDCK – C11 cells

Lack of Na+,K+-ATPase expression in intercalated cells may be compensated by Na+-ATPase: A study on MDCK – C11 cells

The effect of saponins from Ampelozizyphus amazonicus Ducke on the renal Na+ pumps’ activities and urinary excretion of natriuretic peptides

The angiotensin receptor type 1–G_q protein–phosphatidyl inositol phospholipase Cβ–protein kinase C pathway is involved in activation of proximal tubule Na⁺‐ATPase activity by angiotensin(1–7) in pig kidneys

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Modulation of ouabain-insensitive Na+-ATPase activity in the renal proximal tubule by Mg2+, MgATP and furosemide

Cited by 29 publications

References 26 publications

Lack of Na+,K+-ATPase expression in intercalated cells may be compensated by Na+-ATPase: A study on MDCK – C11 cells

Lack of Na+,K+-ATPase expression in intercalated cells may be compensated by Na+-ATPase: A study on MDCK – C11 cells

The effect of saponins from Ampelozizyphus amazonicus Ducke on the renal Na+ pumps’ activities and urinary excretion of natriuretic peptides

The angiotensin receptor type 1–Gq protein–phosphatidyl inositol phospholipase Cβ–protein kinase C pathway is involved in activation of proximal tubule Na+‐ATPase activity by angiotensin(1–7) in pig kidneys

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The angiotensin receptor type 1–G_q protein–phosphatidyl inositol phospholipase Cβ–protein kinase C pathway is involved in activation of proximal tubule Na⁺‐ATPase activity by angiotensin(1–7) in pig kidneys