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Book ; Online ; E-Book: Pulmonary Pathology

Popper, Helmut / Murer, Bruno

A Practical Guide

(Essentials of Diagnostic Pathology,)

2020

Abstract: This book provides an up-to-date overview of diagnostics in lung and pleura pathology. It helps surgical and clinical pathologist solve problem cases in lung and pleura tumor pathology as well as in other fields of pulmonary/pleura pathology such as ... ...

Author's details	by Helmut Popper, Bruno Murer
Series title	Essentials of Diagnostic Pathology,
Abstract	This book provides an up-to-date overview of diagnostics in lung and pleura pathology. It helps surgical and clinical pathologist solve problem cases in lung and pleura tumor pathology as well as in other fields of pulmonary/pleura pathology such as interstitial lung disease, rare tumors, metabolic diseases, infectious pneumonias, pneumoconiosis, drug induced lung diseases, developmental and pediatric pulmonary pathology. Focusing on practical issues and providing numerous illustrated examples of typical and atypical cases, it guides residents as well as experienced pathologists through the problems and pitfalls in pulmonary and pleura pathology. References have been kept to a minimum.
Keywords	Pathology ; Respiratory organs—Diseases ; Pneumology/Respiratory System
Subject code	616.24
Language	English
Size	1 online resource (X, 597 p. 1693 illus., 1669 illus. in color.)
Edition	1st ed. 2020.
Publisher	Springer International Publishing ; Imprint: Springer
Publishing place	Cham
Document type	Book ; Online ; E-Book
Remark	Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
ISBN	3-030-22664-6 ; 3-030-22662-X ; 978-3-030-22664-0 ; 978-3-030-22662-6
DOI	10.1007/978-3-030-22664-0
Database	ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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Article: Characterization of basolateral Na/H exchange (Na/H-1) in MDCK cells.

Vilella, S / Guerra, L / Helmle-Kolb, C / Murer, H

Pflugers Archiv : European journal of physiology

1992 Volume 420, Issue 3-4, Page(s) 275–280

Abstract: ... by ethylisopropylamiloride indicating Na/H exchange activity. Na/H exchange activity showed an apparent Km for Na+ ... by dimethylamiloride was competitive with Na+ interaction. Lowering pHi prior to analysis of Na/H exchange leads ... to sharp activation of Na/H exchange; the apparent Vmax for Na/H exchange is increased more than tenfold ...

Abstract	MDCK cells were grown to confluent monolayers on permeant filter supports; pH was analysed by using the pH-sensitive fluorescent probe 2'7'-biscarboxyethyl-5,6-carboxyfluorescein and a routine spectrofluorometer equipped with a perfusion cuvette [Krayer-Pawlowska et al. (1990) J Membr Biol 120:173-183]. Superfusion of the basolateral (but not apical) cell surface with Na(+)-containing solutions led to immediate recovery of pHi from an acid load (NH4 prepulse). This pHi recovery was reversibly inhibited by ethylisopropylamiloride indicating Na/H exchange activity. Na/H exchange activity showed an apparent Km for Na+ of about 25 nM Na+ and an apparent Ki for inhibition by dimethylamiloride of around 0.2 microM; inhibition by dimethylamiloride was competitive with Na+ interaction. Lowering pHi prior to analysis of Na/H exchange leads to sharp activation of Na/H exchange; the apparent Vmax for Na/H exchange is increased more than tenfold by lowering the pHi from 7.0 to 6.7 without an effect on apparent Km values for Na+ interaction. It is concluded that MDCK cells (strain I) grown on a permeant support contain only basolateral Na/H exchange activity, most likely Na/H-1 [for nomenclature see Igarashi et al. (1991) Kidney Int 40:S84-S89].
MeSH term(s)	Amiloride/analogs & derivatives ; Amiloride/pharmacology ; Animals ; Calibration ; Carrier Proteins/antagonists & inhibitors ; Carrier Proteins/metabolism ; Cell Line ; Dogs ; Fluorescence ; Hydrogen-Ion Concentration ; Kinetics ; Perfusion ; Sodium/metabolism ; Sodium-Hydrogen Exchangers
Chemical Substances	Carrier Proteins ; Sodium-Hydrogen Exchangers ; Amiloride (7DZO8EB0Z3) ; Sodium (9NEZ333N27) ; ethylisopropylamiloride (VW50CE070T)
Language	English
Publishing date	1992-03
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	6380-0
ISSN	1432-2013 ; 0031-6768
ISSN (online)	1432-2013
ISSN	0031-6768
DOI	10.1007/bf00374459
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Article ; Online: Baloch Mashkat (Muscat) and the Sultan Qaboos Era

George Murer

Arabian Humanities, Vol

Cultural Performance, Cosmopolitanism, and Translocal Consciousness

2022 Volume 15

Abstract: Baloch cultural life in Muscat is a vivid part of Oman's national landscape as it has evolved from the time the late Sultan Qaboos took power. Although often typecast as soldiers or police officers, Omani Baloch are deeply integrated into a broad ... ...

Abstract	Baloch cultural life in Muscat is a vivid part of Oman's national landscape as it has evolved from the time the late Sultan Qaboos took power. Although often typecast as soldiers or police officers, Omani Baloch are deeply integrated into a broad spectrum of professions and social milieus. These include communities of arts and letters at the heart of the Omani cultural renaissance championed by the late Sultan and embodied in institutions such as Royal Opera House, the Muscat International Film Festival, and the Oud Hobbyists Association. The many nuances to Baloch identity have led to a plurality of social spaces, from literary forums intertwined with South Asian intellectual spheres to ceremonial contexts in which Omanis of Baloch, Peninsular Arab, and East African heritage converge. Networks of patronage and transnational circulations of songs and poetry among Baloch attest to the longevity of Western Indian Ocean circuits of cultural exchange.
Keywords	Baloch ; Balochistan ; Persian Gulf ; Arabian Gulf ; Spirit Possession ; Indian Ocean ; Social Sciences ; H
Subject code	390
Language	English
Publishing date	2022-01-01T00:00:00Z
Publisher	Centre Français d’Archéologie et de Sciences Sociales de Sanaa
Document type	Article ; Online
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Article: H+ extrusion by an apical vacuolar-type H(+)-ATPase in rat renal proximal tubules.

Zimolo, Z / Montrose, M H / Murer, H

The Journal of membrane biology

1992 Volume 126, Issue 1, Page(s) 19–26

Abstract: The activity of Na+/H(+)-exchange and H(+)-ATPase was measured in the absence of CO2/HCO3 ... type H(+)-ATPase. Readdition of Na+ in the presence of bafilomycin A1 produced an immediate recovery ... inhibitor of Na+/H+ exchange. The transport rate of the H(+)-ATPase is about 40% of Na+/H(+)-exchange ...

Abstract	The activity of Na+/H(+)-exchange and H(+)-ATPase was measured in the absence of CO2/HCO3 by microfluorometry at the single cell level in rat proximal tubules (superficial S1/S2 segments) loaded with BCECF [2'7'-bis(carboxyethyl)5-6-carboxyfluorescein- acetoxymethylester]. Intracellular pH (pHi) was lowered by a NH4Cl-prepulse technique. In the absence of Na+ in the superfusion solutions, pHi recovered from the acid load by a mechanism inhibited by 0.1 microM bafilomycin A1, a specific inhibitor of a vacuolar-type H(+)-ATPase. Readdition of Na+ in the presence of bafilomycin A1 produced an immediate recovery of pHi by a mechanism sensitive to the addition of 10 microM EIPA (ethylisopropylamiloride), a specific inhibitor of Na+/H+ exchange. The transport rate of the H(+)-ATPase is about 40% of Na+/H(+)-exchange activity at a similar pHi (0.218 +/- 0.028 vs. 0.507 +/- 0.056 pH unit/min. Pre-exposure of the tubules to 30 mM fructose, 0.5 mM iodoacetate and 1 mM KCN (to deplete intracellular ATP) prevented a pHi recovery in Na(+)-free media; readdition of Na+ led to an immediate pHi recovery. Tubules pre-exposed to Cl(-)-free media for 2 hr also reduced the rate of Na(+)-independent pHi recovery. In free-flow electrophoretic separations of brush border membranes and basolateral membranes, a bafilomycin A1-sensitive ATPase activity was found to be associated with the brush border membrane fraction; half maximal inhibition is at 6 x 10(-10) M bafilomycin A1.(ABSTRACT TRUNCATED AT 250 WORDS)
MeSH term(s)	Adenosine Triphosphate/pharmacology ; Amiloride/analogs & derivatives ; Amiloride/pharmacology ; Animals ; Anti-Arrhythmia Agents/pharmacology ; Anti-Bacterial Agents/pharmacology ; Antifungal Agents/pharmacology ; Biological Transport/drug effects ; Biological Transport/physiology ; Carrier Proteins/physiology ; Cell Fractionation ; Cytophotometry ; Electrophoresis ; Fluorescence ; Hydrogen/metabolism ; Hydrogen-Ion Concentration ; Kidney Tubules, Proximal/enzymology ; Kidney Tubules, Proximal/metabolism ; Kidney Tubules, Proximal/physiology ; Macrolides ; Male ; Proton-Translocating ATPases/analysis ; Proton-Translocating ATPases/metabolism ; Proton-Translocating ATPases/physiology ; Rats ; Rats, Inbred Strains ; Sodium-Hydrogen Exchangers
Chemical Substances	Anti-Arrhythmia Agents ; Anti-Bacterial Agents ; Antifungal Agents ; Carrier Proteins ; Macrolides ; Sodium-Hydrogen Exchangers ; Amiloride (7DZO8EB0Z3) ; Hydrogen (7YNJ3PO35Z) ; bafilomycin A1 (88899-55-2) ; Adenosine Triphosphate (8L70Q75FXE) ; Proton-Translocating ATPases (EC 3.6.3.14) ; ethylisopropylamiloride (VW50CE070T)
Language	English
Publishing date	1992-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3082-x
ISSN	1432-1424 ; 0022-2631
ISSN (online)	1432-1424
ISSN	0022-2631
DOI	10.1007/bf00233457
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Article: Acute regulation of Na/H exchanger NHE3 by adenosine A(1) receptors is mediated by calcineurin homologous protein.

Di Sole, Francesca / Cerull, Robert / Babich, Victor / Quiñones, Henry / Gisler, Serge M / Biber, Jürg / Murer, Heini / Burckhardt, Gerhard / Helmle-Kolb, Corinna / Moe, Orson W

The Journal of biological chemistry

2003 Volume 279, Issue 4, Page(s) 2962–2974

Abstract: ... receptor (A(1)R) by N(6)-cyclopentidyladenosine (CPA) inhibits the Na(+)/H(+) exchanger 3 (NHE3) via ...

Abstract	Adenosine is an autacoid that regulates renal Na(+) transport. Activation of adenosine A(1) receptor (A(1)R) by N(6)-cyclopentidyladenosine (CPA) inhibits the Na(+)/H(+) exchanger 3 (NHE3) via phospholipase C/Ca(2+)/protein kinase C (PKC) signaling pathway. Mutation of PKC phosphorylation sites on NHE3 does not affected regulation of NHE3 by CPA, but amino acid residues 462 and 552 are essential for A(1)R-dependent control of NHE3 activity. One binding partner of the NHE family is calcineurin homologous protein (CHP). We tested the role of NHE3-CHP interaction in mediating CPA-induced inhibition of NHE3 in opossum kidney (OK) and Xenopus laevis uroepithelial (A6) cells. Both native and transfected NHE3 and CHP are present in the same immuno-complex by co-immunoprecipitation. CPA (10(-6) M) increases CHP-NHE3 interaction by 30 - 60% (native and transfected proteins). Direct CHP-NHE3 interaction is evident by yeast two-hybrid assay (bait, NHE3(C terminus); prey, CHP); the minimal interacting region is localized to the juxtamembrane region of NHE3(C terminus) (amino acids 462-552 of opossum NHE3). The yeast data were confirmed in OK cells where truncated NHE3 (NHE3(delta552)) still shows CPA-stimulated CHP interaction. Overexpression of the polypeptide from the CHP binding region (NHE3(462-552)) interferes with the ability of CPA to inhibit NHE3 activity and to increase CHPNHE3(Full-length) interaction. Reduction of native CHP expression by small interference RNA abolishes the ability of CPA to inhibit NHE3 activity. We conclude that CHPNHE3 interaction is regulated by A(1)R activation and this interaction is a necessary and integral part of the signaling pathway between adenosine and NHE3.
MeSH term(s)	Adenosine/metabolism ; Amino Acid Sequence ; Animals ; Calcium-Binding Proteins/genetics ; Calcium-Binding Proteins/metabolism ; Cell Line ; Intracellular Space/metabolism ; Molecular Sequence Data ; Protein Transport ; Receptor, Adenosine A1/metabolism ; Saccharomyces cerevisiae ; Sequence Alignment ; Signal Transduction ; Sodium-Hydrogen Exchanger 3 ; Sodium-Hydrogen Exchangers/genetics ; Sodium-Hydrogen Exchangers/metabolism
Chemical Substances	Calcium-Binding Proteins ; Receptor, Adenosine A1 ; Sodium-Hydrogen Exchanger 3 ; Sodium-Hydrogen Exchangers ; Adenosine (K72T3FS567)
Language	English
Publishing date	2003-10-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M306838200
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Article: Regulation of renal proximal tubular Na/H-exchange: a tissue culture approach.

Murer, H / Krapf, R / Helmle-Kolb, C

Kidney international. Supplement

1994 Volume 44, Page(s) S23–31

MeSH term(s)	Acid-Base Equilibrium ; Animals ; Cell Membrane/metabolism ; Culture Techniques ; Humans ; Kidney Tubules, Proximal/cytology ; Kidney Tubules, Proximal/metabolism ; Parathyroid Hormone/physiology ; Sodium-Hydrogen Exchangers/metabolism
Chemical Substances	Parathyroid Hormone ; Sodium-Hydrogen Exchangers
Language	English
Publishing date	1994-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	193442-9
ISSN	2157-1716 ; 0098-6577 ; 2157-1724
ISSN (online)	2157-1716
ISSN	0098-6577 ; 2157-1724
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Article: Regulation of the transfected Na+/H+-exchanger NHE3 in MDCK cells by vasotocin.

Helmle-Kolb, C / Di Sole, F / Forgo, J / Hilfiker, H / Tse, C M / Casavola, V / Donowitz, M / Murer, H

Pflugers Archiv : European journal of physiology

1997 Volume 434, Issue 1, Page(s) 123–131

Abstract: ... the sensitivity to inhibitors and the regulation of the Na+/H+-exchanger by vasotocin in NHE3 transfectants ... to that of the intrinsic basolateral Na+/H+-exchanger in untransfected and control transfected MDCK cells. By Southern blot ... analysis we documented that the NHE3 transcript is expressed in NHE3 transfectants. Na+/H+-exchange ...

Abstract	NHE3 is most likely the isoform involved in renal reabsorption of HCO3- and Na+. The functional properties of the "cloned" NHE3 isoform, including its transport regulation by extra- and intracellular stimuli, have so far been studied using non-epithelial expression systems. In the present report we stably transfected NHE3 cDNA (rabbit isoform) into Madin-Darby canine kidney cells (MDCK) cells and compared the sensitivity to inhibitors and the regulation of the Na+/H+-exchanger by vasotocin in NHE3 transfectants to that of the intrinsic basolateral Na+/H+-exchanger in untransfected and control transfected MDCK cells. By Southern blot analysis we documented that the NHE3 transcript is expressed in NHE3 transfectants. Na+/H+-exchange activity, measured as sodium-dependent recovery of intracellular pH from an acid load using 2', 7'-bis(carboxymethyl)-5(6)-carboxy-fluorescein (BCECF), was equally present at the basolateral cell surface of all cell lines; however, NHE3 transfectants demonstrated transport activity in the apical membrane that was significantly higher than that in untransfected or control transfected MDCK cells. Studies with ethylisopropylamiloride (EIPA) have shown that there is a similar sensitivity to inhibitors of the apical and/or basolateral Na+/H+-exchanger in transfected and untransfected MDCK cell lines. In contrast, the apical Na+/H+-exchanger (as compared to the basolateral Na+/H+-exchanger) of NHE3 transfectants was found to be relatively insensitive to the inhibitor HOE 694. Vasotocin decreased the activity of the apical Na+/H+-exchanger in NHE3 transfectants and stimulated the activity of the basolateral Na+/H+-exchanger in transfected (with NHE3 or pMAMneo) and untransfected MDCK cells. Phorbol ester, as expected, increased the activity of the Na+/H+-exchanger in the basolateral membrane of all cell lines; also, it stimulated transport activity at the apical cell surface of NHE3 transfectants. No change of Na+/H+-exchange activities was seen in studies with 8-bromo-cAMP. The PKC inhibitor calphostin C completely suppressed regulation of the apical and/or basolateral Na+/H+-exchanger by vasotocin, it partially blocked activation of the apical Na+/H+-exchanger in NHE3 transfectants by phorbol 12-myristate 13-acetate (PMA), and completely blocked stimulation of basolateral Na+/H+-exchanger by PMA. Consistent with a V1 receptor action, the effects of vasotocin in NHE3 transfectants and in MDCK cells were blocked by the V1 receptor antagonist, d(CH2)5Tyr(Me)-AVP, but were not reproduced by the V2 receptor agonist desmopressin. It is concluded that NHE3 in the apical membrane of NHE3-transfected MDCK cells contributes to the differential regulation of the apical and basolateral Na+/H+-exchanger by vasotocin; NHE3 is inhibited and endogenous Na+/H+-exchange activity is stimulated by vasotocin via V1 receptor activation of the protein kinase C pathway.
MeSH term(s)	Animals ; Cells, Cultured ; Dogs ; Kidney/drug effects ; Sodium-Hydrogen Exchangers/drug effects ; Transfection ; Vasotocin/pharmacology
Chemical Substances	Sodium-Hydrogen Exchangers ; Vasotocin (W6S6URY8OF)
Language	English
Publishing date	1997-05
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	6380-0
ISSN	1432-2013 ; 0031-6768
ISSN (online)	1432-2013
ISSN	0031-6768
DOI	10.1007/s004240050372
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Article: Characterization of acute inhibition of Na/H exchanger NHE-3 by dopamine in opossum kidney cells.

Wiederkehr, M R / Di Sole, F / Collazo, R / Quiñones, H / Fan, L / Murer, H / Helmle-Kolb, C / Moe, O W

Kidney international

2001 Volume 59, Issue 1, Page(s) 197–209

Abstract: ... volume from a Na load. Natriuresis is effected partly through inhibiting the proximal tubule Na/H ...

Abstract	Background: Dopamine (DA) is a principal natriuretic hormone that defends extracellular fluid volume from a Na load. Natriuresis is effected partly through inhibiting the proximal tubule Na/H exchanger NHE-3. Changes in NHE-3 phosphorylation is one mechanism by which NHE-3 activity is regulated. Methods: We used opossum kidney (OK) cells to characterize the differential and synergistic effects of DA receptor subtype-1 (DA1) and -2 (DA2) agonists and the effect of blockade of protein kinase A (PKA) or protein kinase C (PKC) on NHE-3 activity and phosphorylation. Results: DA and DA1 agonists inhibited NHE-3 activity, and DA1 antagonist blocked the effect of either DA or DA1 agonist. DA2 agonist alone had no effect, but DA2 antagonist reduced the DA effect on NHE-3 activity. DA1 and DA2 agonists together were more potent than DA1 alone. PKA inhibition eliminated the effect of DA1 agonist and partially blocked the effect of DA on NHE-3 activity. PKC inhibition did not block the DA effect. DA1 agonist and PKA activation phosphorylated NHE-3 on identical sites. Despite lack of effect on NHE-3 activity, DA2 agonists increased NHE-3 phosphorylation. DA-induced NHE-3 phosphorylation was distinct from DA1 and PKA but closely resembled DA2. Conclusion: We postulate the following: (1) DA modifies NHE-3 phosphorylation by activating PKA through DA1 and by other kinases/phosphatases via DA2. (2) DA1 is sufficient to inhibit NHE-3, while DA2 is insufficient but plays a synergistic role by altering NHE-3 phosphorylation.
MeSH term(s)	2,3,4,5-Tetrahydro-7,8-dihydroxy-1-phenyl-1H-3-benzazepine/pharmacology ; Animals ; Bromocriptine/pharmacology ; Cells, Cultured ; Cyclic AMP/pharmacology ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Dopamine/pharmacology ; Dopamine Agonists/pharmacology ; Dose-Response Relationship, Drug ; Kidney/cytology ; Kidney/metabolism ; Opossums ; Phosphorylation ; Protein Kinase C/metabolism ; Receptors, Dopamine D1/agonists ; Receptors, Dopamine D1/metabolism ; Receptors, Dopamine D2/agonists ; Receptors, Dopamine D2/metabolism ; Sodium-Hydrogen Exchanger 3 ; Sodium-Hydrogen Exchangers/antagonists & inhibitors ; Time Factors
Chemical Substances	Dopamine Agonists ; Receptors, Dopamine D1 ; Receptors, Dopamine D2 ; Sodium-Hydrogen Exchanger 3 ; Sodium-Hydrogen Exchangers ; Bromocriptine (3A64E3G5ZO) ; 2,3,4,5-Tetrahydro-7,8-dihydroxy-1-phenyl-1H-3-benzazepine (67287-49-4) ; Cyclic AMP (E0399OZS9N) ; Cyclic AMP-Dependent Protein Kinases (EC 2.7.11.11) ; Protein Kinase C (EC 2.7.11.13) ; Dopamine (VTD58H1Z2X)
Language	English
Publishing date	2001-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	120573-0
ISSN	1523-1755 ; 0085-2538
ISSN (online)	1523-1755
ISSN	0085-2538
DOI	10.1046/j.1523-1755.2001.00480.x
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Article: Stimulation of Na+/H+ exchange activity by endothelin in opossum kidney cells.

Walter, R / Helmle-Kolb, C / Forgo, J / Binswanger, U / Murer, H

Pflugers Archiv : European journal of physiology

1995 Volume 430, Issue 1, Page(s) 137–144

Abstract: ... the effects of ET-1 on apical Na+/H+ exchange activity in opossum kidney (OK) cells. ET-1 (at 10(-10) M and 10 ... 8) M) activated Na+/H+ exchange activity within 5 min of exposure. ET-1 (10(-8) M) prevented PTH ... induced (parathyroid hormone; 10(-8) M) inhibition of Na+/H+ exchange activity; it also abolished ...

Abstract	Endothelin-1 (ET-1) controls multiple aspects of kidney function. In this study we have analysed the effects of ET-1 on apical Na+/H+ exchange activity in opossum kidney (OK) cells. ET-1 (at 10(-10) M and 10(-8) M) activated Na+/H+ exchange activity within 5 min of exposure. ET-1 (10(-8) M) prevented PTH-induced (parathyroid hormone; 10(-8) M) inhibition of Na+/H+ exchange activity; it also abolished transport inhibition in response to 10(-3) M IBMX (isobutyl-methylxanthine) and 3 x 10(-7) M TPA (phorbol 12-myristate 13-acetate), but had no effect on the 8-bromo-cAMP-induced (10(-4) M) decrease of transport rate. Basal cAMP content, IBMX- and PTH-stimulated cAMP production were unaffected by ET-1 (10(-8) M). The stimulatory action of ET-1 (10(-8) M) on Na+/H+ exchange activity was prevented by calphostin C (10(-8) M). These data document that OK cells might serve as a useful in vitro model for analysis of cellular mechanisms involved in endothelin action; proteine kinase C activation seems to participate in the observed endothelin effects.
MeSH term(s)	1-Methyl-3-isobutylxanthine/pharmacology ; 8-Bromo Cyclic Adenosine Monophosphate/metabolism ; Animals ; Cells, Cultured ; Cyclic AMP/biosynthesis ; Cyclic AMP/metabolism ; Dogs ; Endothelins/pharmacology ; Enzyme Inhibitors ; Ion Transport ; Kidney Tubules, Proximal/metabolism ; Naphthalenes/pharmacology ; Opossums ; Parathyroid Hormone/metabolism ; Protein Kinase C/antagonists & inhibitors ; Sodium-Hydrogen Exchangers/metabolism ; Tetradecanoylphorbol Acetate/pharmacology
Chemical Substances	Endothelins ; Enzyme Inhibitors ; Naphthalenes ; Parathyroid Hormone ; Sodium-Hydrogen Exchangers ; calphostin complex ; 8-Bromo Cyclic Adenosine Monophosphate (23583-48-4) ; Cyclic AMP (E0399OZS9N) ; Protein Kinase C (EC 2.7.11.13) ; Tetradecanoylphorbol Acetate (NI40JAQ945) ; 1-Methyl-3-isobutylxanthine (TBT296U68M)
Language	English
Publishing date	1995-05
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	6380-0
ISSN	1432-2013 ; 0031-6768
ISSN (online)	1432-2013
ISSN	0031-6768
DOI	10.1007/bf00373849
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Article: Parathyroid hormone treatment induces dissociation of type IIa Na+-P(i) cotransporter-Na+/H+ exchanger regulatory factor-1 complexes.

Déliot, Nadine / Hernando, Nati / Horst-Liu, Zeya / Gisler, Serge M / Capuano, Paola / Wagner, Carsten A / Bacic, Desa / O'Brien, Stephen / Biber, Jürg / Murer, Heini

American journal of physiology. Cell physiology

2005 Volume 289, Issue 1, Page(s) C159–67

Abstract: The type IIa Na+-P(i) cotransporter (NaP(i)-IIa) and the Na+/H+ exchanger regulatory factor-1 ...

Abstract	The type IIa Na+-P(i) cotransporter (NaP(i)-IIa) and the Na+/H+ exchanger regulatory factor-1 (NHERF1) colocalize in the apical membrane of proximal tubular cells. Both proteins interact in vitro. Herein the interaction between NaP(i)-IIa and NHERF1 is further documented on the basis of coimmunoprecipitation and co-pull-down assays. NaP(i)-IIa is endocytosed and degraded in lysosomes upon parathyroid hormone (PTH) treatment. To investigate the effect of PTH on the NaP(i)-IIa-NHERF1 association, we first compared the localization of both proteins after PTH treatment. In mouse proximal tubules and OK cells, NaP(i)-IIa was removed from the apical membrane after hormonal treatment; however, NHERF1 remained at the membrane. Moreover, PTH treatment led to degradation of NaP(i)-IIa without changes in the amount of NHERF1. The effect of PTH on the NaP(i)-IIa-NHERF1 interaction was further studied using coimmunoprecipitation. PTH treatment reduced the amount of NaP(i)-IIa coimmunoprecipitated with NHERF antibodies. PTH-induced internalization of NaP(i)-IIa requires PKA and PKC; therefore, we next analyzed whether PTH induces changes in the phosphorylation state of either partner. NHERF1 was constitutively phosphorylated. Moreover, in mouse kidney slices, PTH induced an increase in NHERF1 phosphorylation; independent activation of PKA or PKC also resulted in increased phosphorylation of NHERF1 in kidney slices. However, NaP(i)-IIa was not phosphorylated either basally or after exposure to PTH. Our study supports an interaction between NHERF1 and NaP(i)-IIa on the basis of their brush-border membrane colocalization and in vitro coimmunoprecipitation/co-pull-down assays. Furthermore, PTH weakens this interaction as evidenced by different in situ and in vivo behavior. The PTH effect takes place in the presence of increased phosphorylation of NHERF1.
MeSH term(s)	Animals ; Cell Line ; Cell Membrane/metabolism ; Epithelium/metabolism ; Kidney Tubules, Proximal/metabolism ; Mice ; Mice, Inbred Strains ; Opossums ; Parathyroid Hormone/pharmacology ; Phosphoproteins/metabolism ; Phosphorylation ; Sodium-Hydrogen Exchangers/metabolism ; Sodium-Phosphate Cotransporter Proteins ; Sodium-Phosphate Cotransporter Proteins, Type IIa ; Symporters/metabolism ; Tissue Distribution
Chemical Substances	Parathyroid Hormone ; Phosphoproteins ; Slc34a1 protein, mouse ; Sodium-Hydrogen Exchangers ; Sodium-Phosphate Cotransporter Proteins ; Sodium-Phosphate Cotransporter Proteins, Type IIa ; Symporters ; sodium-hydrogen exchanger regulatory factor
Language	English
Publishing date	2005-03-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	392098-7
ISSN	1522-1563 ; 0363-6143
ISSN (online)	1522-1563
ISSN	0363-6143
DOI	10.1152/ajpcell.00456.2004
Database	MEDical Literature Analysis and Retrieval System OnLINE

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