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Article ; Online: Alterations in gene expression and microbiome composition upon calcium-sensing receptor deletion in the mouse esophagus.

Abdulnour-Nakhoul, Solange M / Kolls, Jay K / Flemington, Erik K / Ungerleider, Nathan A / Nakhoul, Hani N / Song, Kejing / Nakhoul, Nazih L

American journal of physiology. Gastrointestinal and liver physiology

2024 Volume 326, Issue 4, Page(s) G438–G459

Abstract: The calcium-sensing receptor (CaSR), a G protein-coupled receptor, regulates ... ...

Abstract	The calcium-sensing receptor (CaSR), a G protein-coupled receptor, regulates Ca
MeSH term(s)	Animals ; Mice ; Calcium/metabolism ; Receptors, Calcium-Sensing/genetics ; Receptors, Calcium-Sensing/metabolism ; Esophagus/metabolism ; Microbiota ; Inflammation ; Gene Expression
Chemical Substances	Calcium (SY7Q814VUP) ; Receptors, Calcium-Sensing
Language	English
Publishing date	2024-01-09
Publishing country	United States
Document type	Journal Article
ZDB-ID	603840-2
ISSN	1522-1547 ; 0193-1857
ISSN (online)	1522-1547
ISSN	0193-1857
DOI	10.1152/ajpgi.00066.2023
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Article ; Online: Ussing Chamber Methods to Study the Esophageal Epithelial Barrier.

Abdulnour-Nakhoul, Solange M / Nakhoul, Nazih L

Methods in molecular biology (Clifton, N.J.)

2020 Volume 2367, Page(s) 215–233

Abstract: The Ussing chamber was developed in 1949 by Hans Ussing and quickly became a powerful tool to study ion and solute transport in epithelia. The chamber has two compartments strictly separating the apical and basolateral sides of the tissue under study. ... ...

Abstract	The Ussing chamber was developed in 1949 by Hans Ussing and quickly became a powerful tool to study ion and solute transport in epithelia. The chamber has two compartments strictly separating the apical and basolateral sides of the tissue under study. The two sides of the tissue are connected via electrodes to a modified electrometer/pulse generator that allows measurement of electrical parameters, namely, transepithelial voltage, current, and resistance. Simultaneously, permeability of the tissue to specific solutes or markers can be monitored by using tracers or isotopes to measure transport from one side of the tissue to the other. In this chapter, we will describe the use of the Ussing chamber to study the barrier properties of the mouse esophageal epithelium. We will also briefly describe the use of the modified Ussing chamber to simultaneously study transepithelial and cellular electrophysiology in the rabbit esophageal epithelium. Lastly, we will cover the use of the Ussing chamber to study bicarbonate secretion in the pig esophagus. These examples highlight the versatility of the Ussing chamber technique in investigating the physiology and pathophysiology of epithelia including human biopsies.
MeSH term(s)	Animals ; Epithelium ; Esophagus ; Mice ; Permeability ; Rabbits ; Swine
Language	English
Publishing date	2020-09-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/7651_2020_324
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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

Physiological reports

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: Calcium-sensing receptor deletion in the mouse esophagus alters barrier function.

Nakhoul, Nazih L / Tu, Chia-Ling / Brown, Karen L / Islam, M Toriqul / Hodges, Anna G / Abdulnour-Nakhoul, Solange M

American journal of physiology. Gastrointestinal and liver physiology

2019 Volume 318, Issue 1, Page(s) G144–G161

Abstract: Calcium-sensing receptor (CaSR) is the molecular sensor by which cells respond to small changes in extracellular ... ...

Abstract	Calcium-sensing receptor (CaSR) is the molecular sensor by which cells respond to small changes in extracellular Ca
MeSH term(s)	Adherens Junctions/metabolism ; Adherens Junctions/pathology ; Animals ; Cadherins/metabolism ; Cell Differentiation ; Cell Proliferation ; Claudins/metabolism ; Electric Impedance ; Esophageal Mucosa/metabolism ; Esophageal Mucosa/microbiology ; Esophageal Mucosa/pathology ; Female ; Gene Deletion ; Male ; Mice, Knockout ; Permeability ; Receptors, Calcium-Sensing/deficiency ; Receptors, Calcium-Sensing/genetics ; Signal Transduction ; Tight Junctions/metabolism ; Tight Junctions/pathology ; beta Catenin/metabolism ; cdc42 GTP-Binding Protein/metabolism ; rac GTP-Binding Proteins/metabolism
Chemical Substances	CASR protein, mouse ; CTNNB1 protein, mouse ; Cadherins ; Cdc42 protein, mouse ; Cdh1 protein, mouse ; Claudins ; Receptors, Calcium-Sensing ; beta Catenin ; cdc42 GTP-Binding Protein (EC 3.6.5.2) ; rac GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2019-11-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	603840-2
ISSN	1522-1547 ; 0193-1857
ISSN (online)	1522-1547
ISSN	0193-1857
DOI	10.1152/ajpgi.00021.2019
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Article ; Online: Proton-pump inhibitor vs. H2-receptor blocker use and overall risk of CKD progression.

Cholin, Liza / Ashour, Tarek / Mehdi, Ali / Taliercio, Jonathan J / Daou, Remy / Arrigain, Susana / Schold, Jesse D / Thomas, George / Nally, Joseph / Nakhoul, Nazih L / Nakhoul, Georges N

BMC nephrology

2021 Volume 22, Issue 1, Page(s) 264

Abstract: Background: The relationship between proton-pump inhibitor (PPI) use and chronic kidney disease (CKD) progression remains controversial. Specifically, there is a lack of data evaluating renal outcomes in established CKD patients. The aim of our study is ...

Abstract	Background: The relationship between proton-pump inhibitor (PPI) use and chronic kidney disease (CKD) progression remains controversial. Specifically, there is a lack of data evaluating renal outcomes in established CKD patients. The aim of our study is to determine the risk of progression to end-stage kidney disease (ESKD) or death amongst CKD patients on PPI, histamine-2 receptor blocker (H2B), or no anti-acid therapy. Methods: Using our CKD registry, we evaluated the relationship between PPI and H2B use and outcomes amongst patients with CKD (eGFR < 60), with at least 2 PCP visits in the year prior. A Cox proportional hazards model was used to evaluate the relationship between medication groups and overall mortality, while competing risks regression models were used to determine the risk of ESKD with death as a competing risk. Results: 25,455 patients met inclusion criteria and were stratified according to medication group: no antacid therapy (15,961), PPI use (8646), or H2B use (848). At 4 years, the cumulative incidence of ESKD with death as a competing risk was 2.0% (95% CI: 1.7, 2.4), 1.5% (0.8, 2.8), and 1.6%(1.4, 1.9) among PPI, H2B, and no medication respectively (P = 0.22). The cumulative incidence of death with ESKD as a competing risk was 17.6% (95% CI: 16.6, 18.6), 16.7% (13.7, 19.8), and 17.3% (16.6, 18.0) (P = 0.71). Conclusions: Use of PPI in a CKD population was not associated with increased mortality or progression to ESKD when compared to H2 blocker and to no acid suppressing therapy.
MeSH term(s)	Comorbidity ; Disease Progression ; Female ; Histamine H2 Antagonists/administration & dosage ; Histamine H2 Antagonists/adverse effects ; Humans ; Incidence ; Kaplan-Meier Estimate ; Kidney Failure, Chronic/diagnosis ; Kidney Failure, Chronic/mortality ; Male ; Middle Aged ; Negative Results ; Outcome Assessment, Health Care ; Proportional Hazards Models ; Proton Pump Inhibitors/administration & dosage ; Proton Pump Inhibitors/adverse effects ; Registries/statistics & numerical data ; Renal Insufficiency, Chronic/epidemiology ; Renal Insufficiency, Chronic/physiopathology ; Risk Assessment ; Stomach Diseases/drug therapy ; Stomach Diseases/epidemiology ; United States/epidemiology
Chemical Substances	Histamine H2 Antagonists ; Proton Pump Inhibitors
Language	English
Publishing date	2021-07-15
Publishing country	England
Document type	Journal Article
ZDB-ID	2041348-8
ISSN	1471-2369 ; 1471-2369
ISSN (online)	1471-2369
ISSN	1471-2369
DOI	10.1186/s12882-021-02449-0
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Article ; Online: Characteristics of mammalian Rh glycoproteins (SLC42 transporters) and their role in acid-base transport.

Nakhoul, Nazih L / Lee Hamm, L

Molecular aspects of medicine

2013 Volume 34, Issue 2-3, Page(s) 629–637

Abstract: The mammalian Rh glycoproteins belong to the solute transporter family SLC42 and include RhAG, present in red blood cells, and two non-erythroid members RhBG and RhCG that are expressed in various tissues, including kidney, liver, skin and the GI tract. ... ...

Abstract	The mammalian Rh glycoproteins belong to the solute transporter family SLC42 and include RhAG, present in red blood cells, and two non-erythroid members RhBG and RhCG that are expressed in various tissues, including kidney, liver, skin and the GI tract. The Rh proteins in the red blood cell form an "Rh complex" made up of one D-subunit, one CE-subunit and two RhAG subunits. The Rh complex has a well-known antigenic effect but also contributes to the stability of the red cell membrane. RhBG and RhCG are related to the NH4(+) transporters of the yeast and bacteria but their exact function is yet to be determined. This review describes the expression and molecular properties of these membrane proteins and their potential role as NH3/NH4(+) and CO2 transporters. The likelihood that these proteins transport gases such as CO2 or NH3 is novel and significant. The review also describes the physiological importance of these proteins and their relevance to human disease.
MeSH term(s)	Blood Proteins/genetics ; Blood Proteins/metabolism ; Blood Proteins/physiology ; Carbon Dioxide/metabolism ; Cation Transport Proteins/genetics ; Cation Transport Proteins/metabolism ; Cation Transport Proteins/physiology ; Glycoproteins/genetics ; Glycoproteins/metabolism ; Glycoproteins/physiology ; Humans ; Membrane Glycoproteins/genetics ; Membrane Glycoproteins/metabolism ; Membrane Glycoproteins/physiology ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Membrane Transport Proteins/physiology ; Models, Genetic ; Models, Molecular ; Multigene Family/genetics ; Protein Conformation ; Quaternary Ammonium Compounds/metabolism ; Skin/metabolism ; Substrate Specificity ; Viscera/metabolism
Chemical Substances	Blood Proteins ; Cation Transport Proteins ; Glycoproteins ; Membrane Glycoproteins ; Membrane Transport Proteins ; Quaternary Ammonium Compounds ; RHAG protein, human ; RHBG protein, human ; RHCG protein, human ; Carbon Dioxide (142M471B3J)
Language	English
Publishing date	2013-03-16
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	197640-0
ISSN	1872-9452 ; 0098-2997
ISSN (online)	1872-9452
ISSN	0098-2997
DOI	10.1016/j.mam.2012.05.013
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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 ; Online: Acid-base and potassium homeostasis.

Lee Hamm, L / Hering-Smith, Kathleen S / Nakhoul, Nazih L

Seminars in nephrology

2013 Volume 33, Issue 3, Page(s) 257–264

Abstract: Acid-base balance and potassium disorders are often clinically linked. Importantly, acid-base disorders alter potassium transport. In general, acidosis causes decreased K(+) secretion and increased reabsorption in the collecting duct. Alkalosis has the ... ...

Abstract	Acid-base balance and potassium disorders are often clinically linked. Importantly, acid-base disorders alter potassium transport. In general, acidosis causes decreased K(+) secretion and increased reabsorption in the collecting duct. Alkalosis has the opposite effects, often leading to hypokalemia. Potassium disorders also influence acid-base homeostasis. Potassium depletion causes increased H(+) secretion, ammoniagenesis and H-K-ATPase activity. Hyperkalemia decreases ammoniagenesis and NH4(+) transport in the thick ascending limb. Some combined potassium and acid-base disorders involve indirect factors such as aldosterone, impaired renal function, volume depletion, and diarrhea. In summary, disorders of potassium and acid-base homeostasis are mechanistically linked and clinically important.
MeSH term(s)	Acid-Base Equilibrium/physiology ; Acid-Base Imbalance/metabolism ; Acid-Base Imbalance/physiopathology ; Homeostasis/physiology ; Humans ; Hyperkalemia/metabolism ; Hyperkalemia/physiopathology ; Hypokalemia/metabolism ; Hypokalemia/physiopathology ; Kidney Tubules/metabolism ; Potassium/metabolism
Chemical Substances	Potassium (RWP5GA015D)
Language	English
Publishing date	2013-08-16
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	604652-6
ISSN	1558-4488 ; 0270-9295
ISSN (online)	1558-4488
ISSN	0270-9295
DOI	10.1016/j.semnephrol.2013.04.006
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Article: Non-erythroid Rh glycoproteins: a putative new family of mammalian ammonium transporters.

Nakhoul, Nazih L / Hamm, L Lee

Pflugers Archiv : European journal of physiology

2004 Volume 447, Issue 5, Page(s) 807–812

Abstract: The Rhesus (Rh) glycoproteins, originally described in human blood cells, are mostly recognized for their immunogenic characteristics and importance in pregnancy. The Rh proteins in the red blood cell are expressed as an "Rh complex" made up of one D- ... ...

Abstract	The Rhesus (Rh) glycoproteins, originally described in human blood cells, are mostly recognized for their immunogenic characteristics and importance in pregnancy. The Rh proteins in the red blood cell are expressed as an "Rh complex" made up of one D-subunit, one CE-subunit and two Rh-associated glycoprotein (RhAG) subunits. In addition to its antigenic property, the Rh complex is thought to contribute to membrane stability and structure of red blood cells. The exact function is yet to be determined. Recently, two non-erythroid Rh glycoproteins were cloned from mice (Rhcg and Rhbg) and humans (RhCG and RhBG). RhCG is expressed at the membrane surface alone with no apparent need for heteromeric interaction with other glycoproteins. It is more similar to RhAG than to Rh CE/D, occurs late in development and is expressed abundantly and broadly in kidney and testis. In the kidney RhCG is localized to the apical cell membrane of the collecting duct. Rhbg and its human analog (RhBG) are expressed mainly in liver, skin and the kidney tubules. In the kidney collecting duct, Rhbg is localized to the basolateral membrane. Based on structural similarities to the methylammonium and ammonium permease/ammonium (MEP/Amt) transporters in yeast and their sequence homology, these proteins probably function as NH(4)(+) transporters. An initial study has indicated that RhAG or RhCG promote efflux of NH(4)(+), whereas another study has suggested that RhAG functions as an NH(4)(+)-H(+) exchanger. Evidence for such a function is still circumstantial and data indicating that Rh proteins function as NH(4)(+) transporters are indirect.
MeSH term(s)	Animals ; Biological Transport/physiology ; Humans ; Mammals ; Membrane Glycoproteins/chemistry ; Membrane Glycoproteins/physiology ; Multigene Family/physiology ; Quaternary Ammonium Compounds/metabolism ; Rh-Hr Blood-Group System/chemistry ; Rh-Hr Blood-Group System/physiology
Chemical Substances	Membrane Glycoproteins ; Quaternary Ammonium Compounds ; Rh-Hr Blood-Group System
Language	English
Publishing date	2004-02
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	6380-0
ISSN	1432-2013 ; 0031-6768
ISSN (online)	1432-2013
ISSN	0031-6768
DOI	10.1007/s00424-003-1142-8
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Article: Vacuolar H(+)-ATPase in the kidney.

Nakhoul, Nazih L / Hamm, L Lee

Journal of nephrology

2002 Volume 15 Suppl 5, Page(s) S22–31

Abstract: Proton-translocating vacuolar ATPases (H+V-ATPase) are increasingly recognized as essential components of most eukaryotic cells. This electrogenic transporter is present in the cell membranes of many differentiated cell types and in the membranes of many ...

Abstract	Proton-translocating vacuolar ATPases (H+V-ATPase) are increasingly recognized as essential components of most eukaryotic cells. This electrogenic transporter is present in the cell membranes of many differentiated cell types and in the membranes of many subcellular organelles. The primary active pump is a multi-subunit enzyme with a membrane-bound component (V0 domain) and an intracellular catalytic component (V1 domain). The V0 domain is responsible for proton translocation and the V1 domain is responsible for ATP hydrolysis. All the subunits of the H+V-ATPase are now identified and many of their structural and molecular properties are characterized. The H+V-ATPase plays an important role in many physiological processes such as receptor-mediated transport, endocytosis, protein degradation and processing, and intracellular trafficking. In the cell membranes, it contributes to regulation of intracellular pH, secretion of acid, and generation of transmembrane electrical gradients that serve as a driving force for transport across the membrane of these cells. The role of this transporter is perhaps most significant in the kidney where it has been demonstrated in almost all segments of the nephron. H+V-ATPase in the apical membranes contributes significantly to proximal tubule bicarbonate reabsorption and is chiefly responsible for H+ secretion in the distal portions of the nephron. Basolateral H+V-ATPase in other cell types drives luminal HCO3- secretion. Regulation of distal nephron H+V-ATPase is predominantly via shuttling of transporters into and out of the surface membrane.
MeSH term(s)	Animals ; Hydrogen-Ion Concentration ; Kidney/enzymology ; Kidney/metabolism ; Protein Structure, Tertiary ; Proton-Translocating ATPases/chemistry ; Proton-Translocating ATPases/metabolism ; Vacuoles/enzymology
Chemical Substances	Proton-Translocating ATPases (EC 3.6.3.14)
Language	English
Publishing date	2002-03
Publishing country	Italy
Document type	Journal Article ; Review
ZDB-ID	1093991-x
ISSN	1724-6059 ; 1121-8428 ; 1120-3625
ISSN (online)	1724-6059
ISSN	1121-8428 ; 1120-3625
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