Expression of Multiple Na+/H+ Exchanger Isoforms in Cultured Epithelial Cells from Rat Efferent Duct and Cauda Epididymidis1

Leung, George Pak-Heng; Tse, Chung Ming; Chew, Sek-Jin; Wong, Patrick

doi:10.1095/biolreprod64.2.482

Cited by 49 publications

(57 citation statements)

References 52 publications

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“…However, in efferent ducts, CFTR was found in the apical surface of the nonciliated cells in human, similarly as previously shown for rat (Ruz et al 2004). In rat, NHE3 is found on the apical pole of the nonciliated cells of the efferent ducts and principal cells of the epididymal ducts (Pushkin et al 2000, Bagnis et al 2001, Kaunisto et al 2001, Leung et al 2001, Kaunisto & Rajaniemi 2002), while we found it only in the former in human. Rat V-ATPase is expressed widely in the male reproductive tract, e.g., in the efferent ducts and epididymis, (Herak-Kramberger et al 2001) but the human ortholog was found in AMRC of epididymal ducts only.…”

Section: Discussionsupporting

confidence: 88%

Expression of ion transport-associated proteins in human efferent and epididymal ducts

Kujala¹,

Hihnala²,

Tienari³

et al. 2007

Reproduction

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Appropriate intraluminal microenvironment in the epididymis is essential for maturation of sperm. To clarify whether the anion transporters SLC26A2, SLC26A6, SLC26A7, and SLC26A8 might participate in generating this proper intraluminal milieu, we studied the localization of these proteins in the human efferent and the epididymal ducts by immunohistochemistry. In addition, immunohistochemistry of several SLC26-interacting proteins was performed: the Na C /H C exchanger 3 (NHE3), the Cl K channel cystic fibrosis transmembrane conductance regulator (CFTR), the proton pump V-ATPase, their regulator Na C /H C exchanger regulating factor 1 (NHERF-1), and carbonic anhydrase II (CAII). Our results show that SLC26A6, CFTR, NHE3, and NHERF-1 are co-expressed on the apical side of the nonciliated cells, and SLC26A2 appears in the cilia of the ciliated cells in the human efferent ducts. In the epididymal ducts, SLC26A6, CFTR, NHERF-1, CAII, and V-ATPase (B and E subunits) were co-localized to the apical mitochondria rich cells, while SLC26A7 was expressed in a subgroup of basal cells. SLC26A8 was not found in the structures studied. This is the first study describing the localization of SLC26A2, A6 and A7, and NHERF-1 in the efferent and the epididymal ducts. Immunolocalization of human CFTR, NHE3, CAII, and V-ATPase in these structures differs partly from previous reports from rodents. Our findings suggest roles for these proteins in male fertility, either independently or through interaction and reciprocal regulation with co-localized proteins shown to affect fertility, when disrupted. Reproduction (2007) 133 775-784

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Section: Discussionsupporting

confidence: 88%

Expression of ion transport-associated proteins in human efferent and epididymal ducts

Kujala¹,

Hihnala²,

Tienari³

et al. 2007

Reproduction

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“…-/-males Fluid reabsorption in the epididymis depends on crucial water and ion transporter proteins located on the surface of epithelial cells, including Na + -K + -ATPase, NHE3 and aquaporin 9 (Aqp9) (Bahr et al, 2006;Leung et al, 2001;Pastor et al, 2001). Na + transportation is actively linked to H + secretion and fluid reabsorption (Wong and Yeung et al, 1978;Chew et al, 2000).…”

Section: Reduced Expression Of Water and Ion Transporters In Reproducmentioning

confidence: 99%

G protein-coupled receptor 48 upregulates estrogen receptor α expression via cAMP/PKA signaling in the male reproductive tract

Sun

et al. 2010

Development

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SUMMARYThe epididymis and efferent ducts play major roles in sperm maturation, transport, concentration and storage by reabsorbing water, ions and proteins produced from seminiferous tubules. Gpr48-null male mice demonstrate reproductive tract defects and infertility. In the present study, we found that estrogen receptor  (ER) was dramatically reduced in the epididymis and efferent ducts in Gpr48-null male mice. We further revealed that ER could be upregulated by Gpr48 activation via the cAMP/PKA signaling pathway. Moreover, we identified a cAMP responsive element (Cre) motif located at -1307 to -1300 bp in the ER promoter that is able to interact with Cre binding protein (Creb). In conclusion, Gpr48 participates in the development of the male epididymis and efferent ducts through regulation of ER expression via the cAMP/PKA signaling pathway. KEY WORDS: Gpr48, ER(Esr1), Creb, Epididymis, Infertility, MouseG protein-coupled receptor 48 upregulates estrogen receptor  expression via cAMP/PKA signaling in the male reproductive tract DEVELOPMENT 152 is observed in Gpr48-null mice. The expression of ER, NHE3 and aquaporin 1 (Aqp1) is reduced in the proximal segment of the efferent ducts.In the present study, we investigated the role of Gpr48 in the regulation of ER expression and further explored the molecular mechanism underlying this regulation. MATERIALS AND METHODS MiceGpr48-null male mice were housed at 21±1°C with a humidity of 55±10% and a 12-hour light-dark cycle. Food and water were available ad libitum. For genotyping analysis, genomic DNA was isolated from tail biopsy and PCR was carried out using three primers: upstream primer 5Ј-CCAGTCACCACTCTTACACAATGGCTAAAC-3Ј; and downstream primers 5Ј-GGTCTTTGAGCACCAGAGGAC-3Ј and 5Ј-TCCCGTAG -GAGATAGCGTCCTAG-3Ј. With regard to the male fertility assay, each Gpr48+/-and Gpr48 -/-adult male aged 12 weeks was housed with two Gpr48 +/+ females. The females were examined daily for vaginal plugs. The litter number was counted immediately after parturition. The animal protocol was reviewed and approved by the Animal Care Committee of Shanghai Jiao Tong University School of Medicine. Ligation operationTwenty-four mice at 3 weeks of age received bilateral efferent ductile ligation (EGL; n8), bilateral vasoligation (VGL; n8) and sham operations (n8). For EGL, the efferent ductule was doubly ligated close to the epididymis and away from the epididymal and testicular vasculature and vas deferens. For VGL, bilateral vasa deferentia were doubly ligated. The mice receiving EGL, VGL or sham operations were observed daily to ascertain a normal descending of the testes. Immunofluorescence and immunohistochemical stainingAnimal tissues were fixed overnight in Bouin's solution, dehydrated in ethanol, embedded in paraffin and sectioned at 5 m. Immunofluorescence and immunohistochemical staining were performed according to a standard protocol. In brief, the sections were de-paraffined, progressively rehydrated and treated with 3% hydrogen peroxide in methanol for 30 minutes...

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“…First, our results point to a direct and reversible inhibitory effect of NHE1 and ASIC blockers on nAChRs, using antagonist concentrations commonly used in in vitro studies (Leung et al 2001;Nemeth et al 2002;Li et al 2003;Liu & Somps, 2008;Zhang et al 2008). This is a distinct mechanism from the antagonism of these compounds on their primary targets, ASICs and NHE1.…”

Section: Discussionmentioning

confidence: 57%

Cross‐reactivity of acid‐sensing ion channel and Na⁺–H⁺ exchanger antagonists with nicotinic acetylcholine receptors

Santos-Torres

Ślimak

Auer

et al. 2011

The Journal of Physiology

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Non-technical summary Cardiovascular disease and high blood pressure (hypertension) are frequent in the human population. Amiloride is commonly given as a diuretic to reduce hypertension without eliminating potassium, while zoniporide is used to aid in recovery after cardiac failure. We show here that high concentrations of these drugs have additional effects on nicotinic receptors that are present in the brain and body. The possibility that these drugs could affect nicotinic receptors when given as medications should be further investigated.Abstract Nicotinic acetylcholine receptors (nAChRs) are widely distributed throughout the mammalian central and peripheral nervous systems, where they contribute to neuronal excitability and synaptic communication. It has been reported that nAChRs are modulated by BK channels and that BK channels, in turn, are inhibited by acid-sensing ion channels (ASICs). Here we investigate the possible functional interaction between these channels in medial habenula (MHb) neurones. We report that selective antagonists of large-conductance calcium-activated potassium channels and ASIC1a channels, paxilline and psalmotoxin 1, respectively, did not induce detectable changes in nicotine-evoked currents. In contrast, the non-selective ASIC and Na + -H + exchanger (NHE1) antagonists, amiloride and its analogues, suppressed nicotine-evoked responses in MHb neurones of wild-type and ASIC2 null mice, excluding a possible involvement of ASIC2 in the nAChR inhibition by amiloride. Zoniporide, a more selective inhibitor of NHE1, reversibly inhibited α3β4-, α7-and α4-containing ( * ) nAChRs in Xenopus oocytes and in brain slices, as well as in PS120 cells deficient in NHE1 and virally transduced with nAChRs, suggesting a generalized effect of zoniporide in most neuronal nAChR subtypes. Independently from nAChR antagonism, zoniporide profoundly blocked synaptic transmission onto MHb neurones without affecting glutamatergic and GABA receptors. Taken together, these results indicate that amiloride and zoniporide, which are clinically used to treat hypertension and cardiovascular disease, have an inhibitory effect on neuronal nAChRs when used experimentally at high doses. The possible cross-reactivity of these compounds with nAChRs in vivo will require further investigation.

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Expression of Multiple Na+/H+ Exchanger Isoforms in Cultured Epithelial Cells from Rat Efferent Duct and Cauda Epididymidis1

Cited by 49 publications

References 52 publications

Expression of ion transport-associated proteins in human efferent and epididymal ducts

Expression of ion transport-associated proteins in human efferent and epididymal ducts

G protein-coupled receptor 48 upregulates estrogen receptor α expression via cAMP/PKA signaling in the male reproductive tract

Cross‐reactivity of acid‐sensing ion channel and Na⁺–H⁺ exchanger antagonists with nicotinic acetylcholine receptors

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Expression of Multiple Na+/H+ Exchanger Isoforms in Cultured Epithelial Cells from Rat Efferent Duct and Cauda Epididymidis1

Cited by 49 publications

References 52 publications

Expression of ion transport-associated proteins in human efferent and epididymal ducts

Expression of ion transport-associated proteins in human efferent and epididymal ducts

G protein-coupled receptor 48 upregulates estrogen receptor α expression via cAMP/PKA signaling in the male reproductive tract

Cross‐reactivity of acid‐sensing ion channel and Na+–H+ exchanger antagonists with nicotinic acetylcholine receptors

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Cross‐reactivity of acid‐sensing ion channel and Na⁺–H⁺ exchanger antagonists with nicotinic acetylcholine receptors