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Article ; Online: Effects of chronic hypercapnia on ammonium transport in the mouse kidney.

Abdulnour-Nakhoul, Solange / Hering-Smith, Kathleen / Hamm, L Lee / Nakhoul, Nazih L

2019 Volume 7, Issue 16, Page(s) e14221

Abstract: Hypercapnia and subsequent respiratory acidosis are serious complications in many patients with respiratory disorders. The acute response to hypercapnia is buffering of ... ...

Abstract	Hypercapnia and subsequent respiratory acidosis are serious complications in many patients with respiratory disorders. The acute response to hypercapnia is buffering of H
MeSH term(s)	Acidosis, Respiratory/etiology ; Acidosis, Respiratory/metabolism ; Ammonium Compounds/metabolism ; Animals ; Cation Transport Proteins/metabolism ; Hypercapnia/complications ; Hypercapnia/metabolism ; Kidney Tubules, Collecting/metabolism ; Membrane Glycoproteins/metabolism ; Mice
Chemical Substances	Ammonium Compounds ; Cation Transport Proteins ; Membrane Glycoproteins ; Rh type B glycoprotein, rat ; Rh type C glycoprotein, rat
Language	English
Publishing date	2019-08-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2724325-4
ISSN	2051-817X ; 2051-817X
ISSN (online)	2051-817X
ISSN	2051-817X
DOI	10.14814/phy2.14221
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Article ; Online: Structural determinants of NH3 and NH4+ transport by mouse Rhbg, a renal Rh glycoprotein.

Abdulnour-Nakhoul, Solange / Le, Trang / Rabon, Edd / Hamm, L Lee / Nakhoul, Nazih L

American journal of physiology. Renal physiology

2016 Volume 311, Issue 6, Page(s) F1280–F1293

Abstract: Renal Rhbg is localized to the basolateral membrane of intercalated cells and is involved in ... ...

Abstract	Renal Rhbg is localized to the basolateral membrane of intercalated cells and is involved in NH
MeSH term(s)	Ammonia/metabolism ; Animals ; Biological Transport ; Glycoproteins/genetics ; Glycoproteins/metabolism ; Hydrogen-Ion Concentration ; Kidney/metabolism ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Mice ; Mutagenesis, Site-Directed ; Oocytes/metabolism ; Xenopus laevis
Chemical Substances	Glycoproteins ; Membrane Transport Proteins ; RhBG protein, mouse ; Ammonia (7664-41-7)
Language	English
Publishing date	2016-09-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	603837-2
ISSN	1522-1466 ; 0363-6127
ISSN (online)	1522-1466
ISSN	0363-6127
DOI	10.1152/ajprenal.00556.2015
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Article: Lumen-to-surface pH gradients in opossum and rabbit esophagi: role of submucosal glands.

Abdulnour-Nakhoul, S / Nakhoul, N L / Orlando, R C

American journal of physiology. Gastrointestinal and liver physiology

2000 Volume 278, Issue 1, Page(s) G113–20

Abstract: The opossum esophagus, like that of humans, contains a network of submucosal glands with the capacity to secrete bicarbonate ions into the esophageal lumen. To evaluate the role of these glands in protecting the epithelial surface from acid insult, we ... ...

Abstract	The opossum esophagus, like that of humans, contains a network of submucosal glands with the capacity to secrete bicarbonate ions into the esophageal lumen. To evaluate the role of these glands in protecting the epithelial surface from acid insult, we measured the lumen-to-surface pH gradient in opossum esophagus at different luminal pH and compared it to that of rabbit esophagus, an organ devoid of submucosal glands. Sections of opossum and rabbit esophageal epithelium were mounted luminal side up in a modified Ussing chamber. pH-sensitive microelectrodes, positioned within 5 microm of the epithelial cell surface, were used to monitor surface pH during perfusion with solutions of different pH. At luminal pH 7. 5, the pH(s) of both opossum and rabbit were similar (pH(s) = 7.5). Lowering luminal pH from 7.5 to 3.5 in opossum decreased pH(s) to 4.2+/-0.16, a value significantly higher than pH of perfusate, whereas in rabbit this maneuver decreased pH(s) to 3.69+/-0.08, a value not significantly different from pH of perfusate. In opossum but not in rabbit, addition of carbachol to the serosal solution increased basal pH(s) to 7.8+/- 0.1 and significantly blunted the decline in pH(s) on perfusion with acidic Ringer solution (pH 3.5), with pH(s) falling to 5.6+/-0.45. The effect of carbachol on surface buffering was inhibited by prior treatment with atropine. Luminal acidification to pH 2.0 in opossum (as in rabbit) abolished the lumen-to-surface pH gradient even after addition of serosal carbachol. We conclude that the presence of submucosal glands in esophagus contributes through bicarbonate secretion to creation of a lumen-to-surface pH gradient. Although this gradient can be modulated by carbachol, its capacity to buffer (and therefore to protect) the epithelial surface against back-diffusing H(+) is limited and dissipated at pH 2.0.
MeSH term(s)	Acids/pharmacology ; Animals ; Carbachol/pharmacology ; Cholinergic Agonists/pharmacology ; Electrochemistry/instrumentation ; Esophagus/drug effects ; Esophagus/metabolism ; Hydrogen/metabolism ; Hydrogen-Ion Concentration ; Microelectrodes ; Mucous Membrane/physiology ; Opossums ; Rabbits
Chemical Substances	Acids ; Cholinergic Agonists ; Hydrogen (7YNJ3PO35Z) ; Carbachol (8Y164V895Y)
Language	English
Publishing date	2000-01
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	603840-2
ISSN	1522-1547 ; 0193-1857
ISSN (online)	1522-1547
ISSN	0193-1857
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Article: Effect of norepinephrine on intracellular pH in kidney proximal tubule: role of Na+-(HCO-3)n cotransport.

Abdulnour-Nakhoul, S / Khuri, R N / Nakhoul, N L

The American journal of physiology

1998 Volume 275, Issue 1, Page(s) F33–45

Abstract: We examined the effect of norepinephrine (NE) on intracellular pH (pHi) and activity of Na+ (aNai) in the isolated perfused kidney proximal tubule of Ambystoma, using single-barreled voltage and ion-selective microelectrodes. In control HCO-3 Ringer, ... ...

Abstract	We examined the effect of norepinephrine (NE) on intracellular pH (pHi) and activity of Na+ (aNai) in the isolated perfused kidney proximal tubule of Ambystoma, using single-barreled voltage and ion-selective microelectrodes. In control HCO-3 Ringer, addition of 10(-6) M NE to the bath reversibly depolarized the basolateral membrane potential (V1), the luminal membrane potential (V2), and the transepithelial potential difference (V3) and increased pHi by 0. 14 +/- 0.02. These effects were mimicked by isoproterenol but were abolished after pretreatment with SITS or in the absence of CO2/HCO-3. Removal of bath Na+ depolarized V1 and V2, hyperpolarized V3, and decreased pHi. These effects are largely mediated by the electrogenic Na+-(HCO-3)n cotransporter. In the presence of NE, the effects of Na+ removal on membrane potential differences and the rate of change of pHi were significantly smaller. Reducing bath HCO-3 concentration from 10 to 2 mM at constant CO2 (pH 6.8) depolarized V1 and V2, decreased pHi, and lowered aNai. These changes are also due to Na+-(HCO-3)n. In the presence of NE, reducing bath [HCO-3] caused a smaller depolarizations of V1 and V2, and the rate of pHi decrease was significantly reduced. Our results indicate: 1) NE causes an increase in pHi; 2) the NE-induced alkalinization is mediated by a SITS-sensitive and HCO-3-dependent transporter on the basolateral membrane; and 3) in the presence of NE, the reduced effects caused by basolateral HCO-3 changes or Na+ removal are indicative of an inhibitory effect of NE on Na+-(HCO-3)n cotransport.
MeSH term(s)	4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid/pharmacology ; Ambystoma ; Animals ; Carrier Proteins/drug effects ; Carrier Proteins/metabolism ; Cell Membrane/drug effects ; Cell Membrane/physiology ; Hydrogen-Ion Concentration ; In Vitro Techniques ; Isoproterenol/pharmacology ; Kidney Tubules, Proximal/drug effects ; Kidney Tubules, Proximal/physiology ; Membrane Potentials/drug effects ; Norepinephrine/pharmacology ; Perfusion ; Sodium/metabolism ; Sodium-Bicarbonate Symporters
Chemical Substances	Carrier Proteins ; Sodium-Bicarbonate Symporters ; 4-Acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic Acid (27816-59-7) ; Sodium (9NEZ333N27) ; Isoproterenol (L628TT009W) ; Norepinephrine (X4W3ENH1CV)
Language	English
Publishing date	1998
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2948-8
ISSN	0002-9513
ISSN	0002-9513
DOI	10.1152/ajprenal.1998.275.1.F33
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Article: Transcellular chloride pathways in ambystoma proximal tubule.

Abdulnour-Nakhoul, S / Boulpaep, E L

The Journal of membrane biology

1998 Volume 166, Issue 1, Page(s) 15–35

Abstract: The transport mechanisms of Ambystoma proximal tubule that mediate transcellular Cl- absorption linked to Na+ were investigated in isolated perfused tubules using Cl--selective and voltage-recording microelectrodes. In control solutions intracellular ... ...

Abstract	The transport mechanisms of Ambystoma proximal tubule that mediate transcellular Cl- absorption linked to Na+ were investigated in isolated perfused tubules using Cl--selective and voltage-recording microelectrodes. In control solutions intracellular activity of Cl- (aiCl) is 11.3 +/- 0.5 mm, the basolateral (V1), apical (V2), and transepithelial (V3) potential differences are -68 +/- 1.2 mV, +62 +/- 1.2 mV and -6.4 +/- 0.3 mV, respectively. When Na+ absorption is decreased by removal of organic substrates from the lumen, aiCl falls by 1.3 +/- 0.3 mm and V2 hyperpolarizes by +11.4 +/- 1.7 mV. Subsequent removal of Na+ from the lumen causes aiCl to fall further by 2.3 +/- 0.4 mm and V2 to hyperpolarize further by +15.3 +/- 2.4 mV. The contribution of transporters and channels to the observed changes of aiCl was examined using ion substitutions and inhibitors. Apical Na/Cl or Na/K/2Cl symport is excluded because bumetanide, furosemide or hydrochlorothiazide have no effect on aiCl. The effects of luminal HCO-3 removal and/or of disulfonic stilbenes argue against the presence of apical Cl-base exchange such as Cl-HCO3 or Cl-OH. The effects of basolateral HCO-3 removal, of basolateral Na+ removal and/or of disulfonic stilbenes are compatible with presence of basolateral Na-independent Cl-base exchange and Na-driven Cl-HCO3 exchange. Several lines of evidence favor conductive Cl- transport across both the apical and basolateral membrane. Addition of the chloride-channel blocker diphenylamine-2-carboxylate to the lumen or bath, increases the aiCl by 2.4 +/- 0.6 mm or 2.9 +/- 1.0 mm respectively. Moreover, following inhibition by DIDS of all anion exchangers in HCO-3-free Ringer, the equilibrium potential for Cl- does not differ from the membrane potential V2. Finally, the logarithmic changes in aiCl in various experimental conditions correlate well with the simultaneous changes in either basolateral or apical membrane potential. These findings strongly support the presence of Cl- channels at the apical and basolateral cell membranes of the proximal tubule.
MeSH term(s)	Ambystoma/physiology ; Animals ; Cell Membrane/physiology ; Chloride Channels/physiology ; Chlorides/physiology ; Ion Transport ; Membrane Potentials ; Sodium/physiology
Chemical Substances	Chloride Channels ; Chlorides ; Sodium (9NEZ333N27)
Language	English
Publishing date	1998-11-01
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	3082-x
ISSN	1432-1424 ; 0022-2631
ISSN (online)	1432-1424
ISSN	0022-2631
DOI	10.1007/s002329900444
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Article ; Online: Mechanisms of ammonia and ammonium transport by rhesus-associated glycoproteins.

Caner, Tolga / Abdulnour-Nakhoul, Solange / Brown, Karen / Islam, M Toriqul / Hamm, L Lee / Nakhoul, Nazih L

American journal of physiology. Cell physiology

2015 Volume 309, Issue 11, Page(s) C747–58

Abstract: In this study we characterized ammonia and ammonium (NH3/NH4(+)) transport by the rhesus-associated (Rh) glycoproteins RhAG, Rhbg, and Rhcg expressed in Xenopus oocytes. We used ion-selective microelectrodes and two-electrode voltage clamp to measure ... ...

Abstract	In this study we characterized ammonia and ammonium (NH3/NH4(+)) transport by the rhesus-associated (Rh) glycoproteins RhAG, Rhbg, and Rhcg expressed in Xenopus oocytes. We used ion-selective microelectrodes and two-electrode voltage clamp to measure changes in intracellular pH, surface pH, and whole cell currents induced by NH3/NH4(+) and methyl amine/ammonium (MA/MA(+)). These measurements allowed us to define signal-specific signatures to distinguish NH3 from NH4(+) transport and to determine how transport of NH3 and NH4(+) differs among RhAG, Rhbg, and Rhcg. Our data indicate that expression of Rh glycoproteins in oocytes generally enhanced NH3/NH4(+) transport and that cellular changes induced by transport of MA/MA(+) by Rh proteins were different from those induced by transport of NH3/NH4(+). Our results support the following conclusions: 1) RhAG and Rhbg transport both the ionic NH4(+) and neutral NH3 species; 2) transport of NH4(+) is electrogenic; 3) like Rhbg, RhAG transport of NH4(+) masks NH3 transport; and 4) Rhcg is likely to be a predominantly NH3 transporter, with no evidence of enhanced NH4(+) transport by this transporter. The dual role of Rh proteins as NH3 and NH4(+) transporters is a unique property and may be critical in understanding how transepithelial secretion of NH3/NH4(+) occurs in the renal collecting duct.
MeSH term(s)	Ammonia/metabolism ; Ammonium Compounds/metabolism ; Animals ; Female ; Glycoproteins/metabolism ; Ion Transport/physiology ; Membrane Glycoproteins/metabolism ; Oocytes/metabolism ; Xenopus laevis
Chemical Substances	Ammonium Compounds ; Glycoproteins ; Membrane Glycoproteins ; Ammonia (7664-41-7)
Language	English
Publishing date	2015-09-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	392098-7
ISSN	1522-1563 ; 0363-6143
ISSN (online)	1522-1563
ISSN	0363-6143
DOI	10.1152/ajpcell.00085.2015
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Article: Cytoskeletal changes induced by allosteric modulators of calcium-sensing receptor in esophageal epithelial cells.

Abdulnour-Nakhoul, Solange / Brown, Karen L / Rabon, Edd C / Al-Tawil, Youhanna / Islam, Mohammed T / Schmieg, John J / Nakhoul, Nazih L

Physiological reports

2015 Volume 3, Issue 11

Abstract: The calcium-sensing receptor (CaSR), a G-protein-coupled receptor, plays a role in glandular and fluid secretion in the gastrointestinal tract, and regulates differentiation and proliferation of epithelial cells. We examined the expression of CaSR in ... ...

Abstract	The calcium-sensing receptor (CaSR), a G-protein-coupled receptor, plays a role in glandular and fluid secretion in the gastrointestinal tract, and regulates differentiation and proliferation of epithelial cells. We examined the expression of CaSR in normal and pathological conditions of human esophagus and investigated the effect of a CaSR agonist, cinacalcet (CCT), and antagonist, calhex (CHX), on cell growth and cell-cell junctional proteins in primary cultures of porcine stratified squamous esophageal epithelium. We used immunohistochemistry and Western analysis to monitor expression of CaSR and cell-cell adhesion molecules, and MTT assay to monitor cell proliferation in cultured esophageal cells. CCT treatment significantly reduced proliferation, changed the cell shape from polygonal to spindle-like, and caused redistribution of E-cadherin and β-catenin from the cell membrane to the cytoplasm. Furthermore, it reduced expression of β-catenin by 35% (P < 0.02) and increased expression of a proteolysis cleavage fragment of E-cadherin, Ecad/CFT2, by 2.3 folds (P < 0.01). On the other hand, CHX treatment enhanced cell proliferation by 27% (P < 0.01), increased the expression of p120-catenin by 24% (P < 0.04), and of Rho, a GTPase involved in cytoskeleton remodeling, by 18% (P < 0.03). In conclusion, CaSR is expressed in normal esophagus as well as in Barrett's, esophageal adenocarcinoma, squamous cell carcinoma, and eosinophilic esophagitis. Long-term activation of CaSR with CCT disrupted the cadherin-catenin complex, induced cytoskeletal remodeling, actin fiber formation, and redistribution of CaSR to the nuclear area. These changes indicate a significant and complex role of CaSR in epithelial remodeling and barrier function of esophageal cells.
Language	English
Publishing date	2015-11
Publishing country	United States
Document type	Journal Article
ZDB-ID	2724325-4
ISSN	2051-817X
ISSN	2051-817X
DOI	10.14814/phy2.12616
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Article ; Online: Pressure overload induces IL-18 and IL-18R expression, but markedly suppresses IL-18BP expression in a rabbit model. IL-18 potentiates TNF-α-induced cardiomyocyte death.

Yoshida, Tadashi / Friehs, Ingeborg / Mummidi, Srinivas / del Nido, Pedro J / Addulnour-Nakhoul, Solange / Delafontaine, Patrice / Valente, Anthony J / Chandrasekar, Bysani

Journal of molecular and cellular cardiology

2014 Volume 75, Page(s) 141–151

Abstract: Recurrent or sustained inflammation plays a causal role in the development and progression of left ventricular hypertrophy (LVH) and its transition to failure. Interleukin (IL)-18 is a potent pro-hypertrophic inflammatory cytokine. We report that ... ...

Abstract	Recurrent or sustained inflammation plays a causal role in the development and progression of left ventricular hypertrophy (LVH) and its transition to failure. Interleukin (IL)-18 is a potent pro-hypertrophic inflammatory cytokine. We report that induction of pressure overload in the rabbit, by constriction of the descending thoracic aorta induces compensatory hypertrophy at 4weeks (mass/volume ratio: 1.7±0.11) and ventricular dilatation indicative of heart failure at 6weeks (mass/volume ratio: 0.7±0.04). In concordance with this, fractional shortening was preserved at 4weeks, but markedly attenuated at 6weeks. We cloned rabbit IL-18, IL-18Rα, IL-18Rβ, and IL-18 binding protein (IL-18BP) cDNA, and show that pressure overload, while enhancing IL-18 and IL-18R expression in hypertrophied and failing hearts, markedly attenuated the level of expression of the endogenous IL-18 antagonist IL-18BP. Cyclical mechanical stretch (10% cyclic equibiaxial stretch, 1Hz) induced hypertrophy of primary rabbit cardiomyocytes in vitro and enhanced ANP, IL-18, and IL-18Rα expression. Further, treatment with rhIL-18 induced its own expression and that of IL-18Rα via AP-1 activation, and induced cardiomyocyte hypertrophy in part via PI3K/Akt/GATA4 signaling. In contrast, IL-18 potentiated TNF-α-induced cardiomyocyte death, and by itself induced cardiac endothelial cell death. These results demonstrate that pressure overload is associated with enhanced IL-18 and its receptor expression in hypertrophied and failingrabbit hearts. Since IL-18BP expression is markedly inhibited, our results indicate a positive amplification in IL-18 proinflammatory signaling during pressure overload, and suggest IL-18 as a potential therapeutic target in pathological hypertrophy and cardiac failure.
MeSH term(s)	Animals ; Cardiomegaly/diagnostic imaging ; Cardiomegaly/pathology ; Cell Death/drug effects ; Disease Models, Animal ; Endothelial Cells/drug effects ; Endothelial Cells/pathology ; Heart Failure/metabolism ; Humans ; Intercellular Signaling Peptides and Proteins/genetics ; Intercellular Signaling Peptides and Proteins/metabolism ; Interleukin-18/genetics ; Interleukin-18/metabolism ; Male ; Molecular Sequence Data ; Myocytes, Cardiac/drug effects ; Myocytes, Cardiac/metabolism ; Myocytes, Cardiac/pathology ; Pressure ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Rabbits ; Receptors, Interleukin-18/genetics ; Receptors, Interleukin-18/metabolism ; Stress, Mechanical ; Tumor Necrosis Factor-alpha/pharmacology ; Ultrasonography
Chemical Substances	Intercellular Signaling Peptides and Proteins ; Interleukin-18 ; RNA, Messenger ; Receptors, Interleukin-18 ; Tumor Necrosis Factor-alpha ; interleukin-18 binding protein
Language	English
Publishing date	2014-08-07
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	80157-4
ISSN	1095-8584 ; 0022-2828
ISSN (online)	1095-8584
ISSN	0022-2828
DOI	10.1016/j.yjmcc.2014.07.007
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Article: Mechanisms of basolateral Na+ transport in rabbit esophageal epithelial cells.

Abdulnour-Nakhoul, S / Bor, S / Imeryuz, N / Orlando, R C

The American journal of physiology

1999 Volume 276, Issue 2, Page(s) G507–17

Abstract: We examined the mechanisms of cellular Na+ transport, both Cl- dependent and Cl- independent, in the mammalian esophageal epithelium. Rabbit esophageal epithelium was dissected from its muscular layers and mounted in a modified Ussing chamber for ... ...

Abstract	We examined the mechanisms of cellular Na+ transport, both Cl- dependent and Cl- independent, in the mammalian esophageal epithelium. Rabbit esophageal epithelium was dissected from its muscular layers and mounted in a modified Ussing chamber for impalement with ion-selective microelectrodes. In bicarbonate Ringer, transepithelial potential difference was -14.9 +/- 0.9 mV, the transepithelial resistance (RTE) was 1,879 +/- 142 Omega. cm2, the basolateral membrane potential difference (VmBL) was -53 +/- 1.5 mV, and the intracellular activity of Na+ (aNai) was 24.6 +/- 2.1 mM. Removal of Na+ and Cl- from the serosal and luminal baths decreased aNai to 6.6 +/- 0.6 mM. Readdition of Na+ to the serosal bath in the absence of Cl- increased aNai by 21.8 +/- 3.0 mM, whereas VmBL and RTE remained unchanged. When serosal Na+ was readded in the presence of amiloride the increase in aNai and the rate of Na+ entry were decreased by approximately 50%. 5-(N-ethyl-N-isopropyl)amiloride mimicked the effect of amiloride, whereas phenamil did not. Subsequent readdition of Cl- to the serosal bath further increased aNai by 4.4 +/- 1.9 mM. When the cells were acid loaded by pretreatment with NH+4 in nominally HCO-3-free Ringer, intracellular pH measurements showed a pHi recovery that is dependent on the presence of Na+ in the serosal bath and that can be blocked by amiloride. These data indicate that esophageal epithelial cells possess a Na+-dependent, amiloride-sensitive electroneutral mechanism for Na+ entry consistent with the presence of a basolateral Na+/H+ exchanger. The ability of Cl- to further enhance Na+ entry supports the existence of at least one additional Cl--dependent component of basolateral Na+ entry.
MeSH term(s)	Amiloride/analogs & derivatives ; Amiloride/pharmacology ; Ammonia/pharmacology ; Animals ; Bicarbonates/pharmacology ; Biological Transport/physiology ; Bumetanide/pharmacology ; Chlorides/pharmacology ; Epithelial Cells/metabolism ; Esophagus/cytology ; Esophagus/metabolism ; Homeostasis ; Hydrogen-Ion Concentration ; In Vitro Techniques ; Intracellular Membranes/metabolism ; Isotonic Solutions/pharmacology ; Rabbits ; Sodium/metabolism ; Sodium/pharmacology
Chemical Substances	Bicarbonates ; Chlorides ; Isotonic Solutions ; Krebs-Ringer solution ; Bumetanide (0Y2S3XUQ5H) ; phenylamil (2038-35-9) ; Ammonia (7664-41-7) ; Amiloride (7DZO8EB0Z3) ; Sodium (9NEZ333N27) ; ethylisopropylamiloride (VW50CE070T)
Language	English
Publishing date	1999
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2948-8
ISSN	0002-9513
ISSN	0002-9513
DOI	10.1152/ajpgi.1999.276.2.G507
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Article: Effect of norepinephrine on cellular sodium transport in Ambystoma kidney proximal tubule.

Abdulnour-Nakhoul, S / Khuri, R N / Nakhoul, N L

The American journal of physiology

1994 Volume 267, Issue 5 Pt 2, Page(s) F725–36

Abstract: The effect of norepinephrine (NE) on mechanisms of cellular Na+ transport in the isolated, perfused proximal tubule of Ambystoma tigrinum was examined. Single-barreled voltage and ion-selective microelectrodes were used to determine basolateral (V1), ... ...

Abstract	The effect of norepinephrine (NE) on mechanisms of cellular Na+ transport in the isolated, perfused proximal tubule of Ambystoma tigrinum was examined. Single-barreled voltage and ion-selective microelectrodes were used to determine basolateral (V1), luminal (V2), and transepithelial (V3) membrane potentials and intracellular Na+ activity (alpha Nai). In CO2/HCO3- control solution, addition of NE (10(-6) M) to the bath caused depolarizations of V1, V2, and V3 are decreased alpha Nai. These effects were mimicked by isoproterenol and inhibited by propranolol. Addition of NE in the absence of luminal Na+ and substrates did not cause any changes in V1, V2, V3, or alpha Nai. NE did not affect the changes in membrane potential difference (PD) or alpha Nai caused by removal and readdition of luminal substrates and/or Na+. To study the effect of NE on Na-K-adenosinetriphosphatase (Na-K-ATPase), the pump was inhibited by external K+ removal and then reactivated by readdition of 12 mM K+ to the bath in the presence and absence of NE. Reactivation of the pump caused hyperpolarization of membrane PDs, and alpha Nai recovered monotonically in 3-5 min. The peak hyperpolarizations of V1 and V2 (approximately 1 min) were significantly larger in the presence of NE. During the first 3 min, and also at the same alpha Nai, the rate of decrease of alpha Nai was significantly faster in the presence of NE. In conclusion, these results show a direct effect of NE on cell membrane PDs and alpha Nai in the kidney proximal tubule. Most likely, beta-receptors are involved in mediating the action of NE. Neither Na/H exchange nor Na-substrate cotransport at the luminal membrane are affected by NE. On the other hand, NE activates Na-K-ATPase.
MeSH term(s)	Ambystoma ; Animals ; Biological Transport/drug effects ; Cell Membrane/drug effects ; Cell Membrane/physiology ; Epithelium/drug effects ; Epithelium/physiology ; In Vitro Techniques ; Isoproterenol/pharmacology ; Kidney Tubules, Proximal/drug effects ; Kidney Tubules, Proximal/physiology ; Kinetics ; Membrane Potentials/drug effects ; Norepinephrine/pharmacology ; Perfusion/instrumentation ; Perfusion/methods ; Potassium/pharmacology ; Propranolol/pharmacology ; Sodium/metabolism ; Sodium-Potassium-Exchanging ATPase/metabolism ; Time Factors
Chemical Substances	Sodium (9NEZ333N27) ; Propranolol (9Y8NXQ24VQ) ; Sodium-Potassium-Exchanging ATPase (EC 3.6.3.9) ; Isoproterenol (L628TT009W) ; Potassium (RWP5GA015D) ; Norepinephrine (X4W3ENH1CV)
Language	English
Publishing date	1994-11
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2948-8
ISSN	0002-9513
ISSN	0002-9513
Database	MEDical Literature Analysis and Retrieval System OnLINE

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