Amiloride-sensitive sodium channels in confluent M-1 mouse cortical collecting duct cells

1995 ◽  
Vol 148 (2) ◽  
Author(s):  
B. Letz ◽  
A. Ackermann ◽  
C.M. Canessa ◽  
B.C. Rossier ◽  
C. Korbmacher
Keyword(s):  
Sodium Channels ◽  
Collecting Duct ◽  
Cortical Collecting Duct ◽  
Duct Cells ◽  
Collecting Duct Cells

Whole cell and unitary amiloride-sensitive sodium currents in M-1 mouse cortical collecting duct cells

1996 ◽  
Vol 270 (4) ◽  
pp. C998-C1010 ◽  
Author(s):  
M. L. Chalfant ◽  
T. G. O'Brien ◽  
M. M. Civan
Keyword(s):  
Collecting Duct ◽  
Cell Permeability ◽  
Na Channel ◽  
Na Channels ◽  
Cortical Collecting Duct ◽  
Ionic Selectivity ◽  
Whole Cell ◽  
Duct Cells ◽  
Excised Patches ◽  
Collecting Duct Cells

Amiloride-sensitive whole cell currents have been reported in M-1 mouse cortical collecting duct cells (Korbmacher et al., J. Gen. Physiol. 102: 761-793, 1993). We have confirmed that amiloride inhibits the whole cell currents but not necessarily the measured whole cell currents. Anomalous responses were eliminated by removing external Na+ and/or introducing paraepithelial shunts. The amiloride-sensitive whole cell currents displayed Goldman rectification. The ionic selectivity sequence of the amiloride-sensitive conductance was Li+ > Na+ >> K+. Growth of M-1 cells on permeable supports increased the amiloride-sensitive whole cell permeability, compared with cells grown on plastic. Single amiloride-sensitive channels were observed, which conformed to the highly selective low-conductance amiloride-sensitive class [Na(5)] of epithelial Na+ channels. Hypotonic pretreatment markedly slowed run-down of channel activity. The gating of the M-1 Na+ channel in excised patches was complex. Open- and closed-state dwell-time distributions from patches that display one operative channel were best described with two or more exponential terms each. We conclude that 1) study of M-1 whole cell Na+ currents is facilitated by reducing the transepithelial potential to zero, 2) these M-1 currents reflect the operation of Na(5) channels, and 3) the Na+ channels display complex kinetics, involving > or = 2 open and > or = 2 closed states.

scholarly journals Lipidomic and proteomic analysis of exosomes from mouse cortical collecting duct cells

2017 ◽  
Vol 31 (12) ◽  
pp. 5399-5408 ◽  
Author(s):  
Viet D. Dang ◽  
Kishore Kumar Jella ◽  
Ragy R. T. Ragheb ◽  
Nancy D. Denslow ◽  
Abdel A. Alli
Keyword(s):  
Proteomic Analysis ◽  
Collecting Duct ◽  
Cortical Collecting Duct ◽  
Duct Cells ◽  
Collecting Duct Cells

Role of AQP2 during apoptosis in cortical collecting duct cells

2009 ◽  
Vol 101 (4) ◽  
pp. 237-250 ◽  
Author(s):  
Pilar Flamenco ◽  
Luciano Galizia ◽  
Valeria Rivarola ◽  
Juan Fernandez ◽  
Paula Ford ◽  
...  
Keyword(s):  
Collecting Duct ◽  
Cortical Collecting Duct ◽  
Duct Cells ◽  
Collecting Duct Cells

scholarly journals Intracellular Na+ Controls Cell Surface Expression of Na,K-ATPase via a cAMP-independent PKA Pathway in Mammalian Kidney Collecting Duct Cells

2003 ◽  
Vol 14 (7) ◽  
pp. 2677-2688 ◽  
Author(s):  
Manlio Vinciguerra ◽  
Georges Deschênes ◽  
Udo Hasler ◽  
David Mordasini ◽  
Martine Rousselot ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Cell Surface ◽  
Atpase Activity ◽  
Collecting Duct ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Cortical Collecting Duct ◽  
Mammalian Kidney ◽  
Duct Cells ◽  
Collecting Duct Cells

In the mammalian kidney the fine control of Na+ reabsorption takes place in collecting duct principal cells where basolateral Na,K-ATPase provides the driving force for vectorial Na+ transport. In the cortical collecting duct (CCD), a rise in intracellular Na+ concentration ([Na+]i) was shown to increase Na,K-ATPase activity and the number of ouabain binding sites, but the mechanism responsible for this event has not yet been elucidated. A rise in [Na+]i caused by incubation with the Na+ ionophore nystatin, increased Na,K-ATPase activity and cell surface expression to the same extent in isolated rat CCD. In cultured mouse mpkCCDcl4 collecting duct cells, increasing [Na+]i either by cell membrane permeabilization with amphotericin B or nystatin, or by incubating cells in a K+-free medium, also increased Na,K-ATPase cell surface expression. The [Na+]i-dependent increase in Na,K-ATPase cell-surface expression was prevented by PKA inhibitors H89 and PKI. Moreover, the effects of [Na+]i and cAMP were not additive. However, [Na+]i-dependent activation of PKA was not associated with an increase in cellular cAMP but was prevented by inhibiting the proteasome. These findings suggest that Na,K-ATPase may be recruited to the cell membrane following an increase in [Na+]i through cAMP-independent PKA activation that is itself dependent on proteasomal activity.

Adaptation to alkalosis induces cell cycle delay and apoptosis in cortical collecting duct cells: Role of aquaporin-2

2010 ◽  
Vol 224 (2) ◽  
pp. 405-413 ◽  
Author(s):  
Valeria Rivarola ◽  
Pilar Flamenco ◽  
Luciana Melamud ◽  
Luciano Galizia ◽  
Paula Ford ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Collecting Duct ◽  
Cortical Collecting Duct ◽  
Cell Cycle Delay ◽  
Aquaporin 2 ◽  
Duct Cells ◽  
Collecting Duct Cells

scholarly journals Serine Protease Activity in M-1 Cortical Collecting Duct Cells

Hypertension ◽  
2002 ◽  
Vol 39 (4) ◽  
pp. 860-864 ◽  
Author(s):  
Lian Liu ◽  
Kathleen S. Hering-Smith ◽  
Faith R. Schiro ◽  
L. Lee Hamm
Keyword(s):  
Serine Protease ◽  
Protease Activity ◽  
Collecting Duct ◽  
Cortical Collecting Duct ◽  
Duct Cells ◽  
Serine Protease Activity ◽  
Collecting Duct Cells

Whole cell sodium conductance of principal cells freshly isolated from rat cortical collecting duct

1995 ◽  
Vol 269 (3) ◽  
pp. C791-C796 ◽  
Author(s):  
J. K. Bubien
Keyword(s):  
Patch Clamp ◽  
Collecting Duct ◽  
Cortical Collecting Duct ◽  
Patch Clamp Technique ◽  
Whole Cell ◽  
Cyclic Monophosphate ◽  
Principal Cells ◽  
Clamp Technique ◽  
Duct Cells ◽  
Collecting Duct Cells

Cortical collecting duct fragments were manually dissected from 6-wk-old Sprague-Dawley rats. The fragments were enzymatically digested (collagenase A) into single cells, washed, and resuspended in serum-free RPMI 1640. Individual cells were examined electrophysiologically using the whole cell patch-clamp technique. Two morphologically distinct cell types were present in the cell suspension. Small round cells that had a capacitance of 7 pF and larger oval cells with a capacitance of 29 pF were consistently observed. Whole cell electrophysiological examination revealed that the small round cells had virtually no plasma membrane ionic conductance, whereas both inward and outward currents were observed in the larger oval-type cells. Also, superfusion of 250 pM arginine vasopressin specifically increased the inward conductance of only the larger cells. The effect could be completely inhibited by 2 microM amiloride or 100 mumol of the Rp diastereomer of 8-(4-chlorophenylthio)-adenosine 3',5'-cyclic monophosphate (a specific adenosine 3',5'-cyclic monophosphate inhibitor). These findings are consistent with the hypothesis that the larger cells are principal cells and the smaller cells are intercalated cells and directly demonstrate that an amiloride-sensitive whole cell conductance is readily observable in freshly isolated cortical collecting duct cells. Thus the whole cell configuration of the patch-clamp technique appears to be well suited for assessing cellular mechanisms that regulate the ionic conductances of cortical collecting duct cells.

scholarly journals Vasopressin inhibits apoptosis in renal collecting duct cells

2013 ◽  
Vol 304 (2) ◽  
pp. F177-F188 ◽  
Author(s):  
R. Lance Miller ◽  
Pablo C. Sandoval ◽  
Trairak Pisitkun ◽  
Mark A. Knepper ◽  
Jason D. Hoffert
Keyword(s):  
Arginine Vasopressin ◽  
Collecting Duct ◽  
Critical Role ◽  
Terminal Deoxynucleotidyl Transferase ◽  
Cortical Collecting Duct ◽  
Caspase Cleavage ◽  
Mammalian Kidney ◽  
Duct Cells ◽  
V2 Receptor ◽  
Collecting Duct Cells

The peptide hormone arginine vasopressin (AVP) plays a critical role in regulating salt and water transport in the mammalian kidney. Recent studies have also demonstrated that AVP can promote cell survival in neuronal cells through V1 receptors. The current study addresses whether AVP can inhibit apoptosis in kidney collecting duct cells via V2 receptors and also explores the downstream signaling pathways regulating this phenomenon. Terminal deoxynucleotidyl transferase-mediated dUTP-biotin nick-end labeling analysis and caspase cleavage assays demonstrated that 1-desamino-8-d-arginine vasopressin (dDAVP) inhibited apoptosis induced by various agents (staurosporine, actinomycin D, and cycloheximide) in cultured mouse cortical collecting duct cells (mpkCCD). Incubation with dDAVP also inhibited apoptosis induced by the phosphatidylinositol 3-kinase (PI3K) pathway inhibitor LY294002, suggesting that the antiapoptotic effects of dDAVP are largely independent of PI3K signaling. The V2 receptor antagonist SR121463 completely abolished the antiapoptotic effects of dDAVP. In addition, incubation with 8-cpt-cAMP, a cell-permeable analog of cAMP, reproduced the antiapoptotic effects of dDAVP. Both dDAVP and 8-cpt-cAMP increased phosphorylation of proapoptotic Bcl-2 family members Bad and Bok. Bad phosphorylation at Ser-112 and Ser-155 is known to inhibit its proapoptotic activity. Preincubation with H89 blocked dDAVP-induced phosphorylation of both Bad and Bok, suggesting dependence on protein kinase A (PKA). This study provides evidence that AVP can inhibit apoptosis through the V2 receptor and downstream cAMP-mediated pathways in mammalian kidney. The antiapoptotic action of AVP may be relevant to a number of physiological and pathophysiological conditions including osmotic tolerance in the inner medulla, escape from AVP-induced antidiuresis, and polycystic kidney disease.

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