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

Kujala, Minna; Hihnala, Satu; Tienari, Jukka; Kaunisto, Kari; Hästbacka, Johanna; Holmberg, Christer; Kere, Juha; Höglund, Pia

doi:10.1530/rep.1.00964

Cited by 62 publications

(65 citation statements)

References 48 publications

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“…These apparently human-specific structures that had no obvious counterpart in the mouse were remotely reminiscent of crypts in the intestine. Similar structures were shown in a recent publication on the localization of ion transport-associated proteins in the human ductuli efferentes (Kujala et al 2007). Although not explicitly mentioned by the authors, the putative anion transporter-1 (SLC26A6) and the Na C /H C exchanger NHE3 (SLC9A3) seemed to be specifically enriched in cryptlike grooves.…”

Section: Discussionsupporting

confidence: 82%

HE6/GPR64 adhesion receptor co-localizes with apical and subapical F-actin scaffold in male excurrent duct epithelia

Kirchhoff¹,

Osterhoff²,

Samalecos³

2008

Reproduction

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A role for HE6/GPR64 in male excurrent ducts in the regulation of water balance was suggested from targeted gene mutation in the mouse. Results of the present immunolocalization study strengthen this hypothesis. Employing monospecific antibodies and laser confocal microscopy, we studied the localization of the receptor protein in the human and wild-type mouse ductuli efferentes and epididymis. We show that HE6/GPR64 is specifically associated with cell types and subcellular domains involved in the process of fluid reabsorption. In the mouse, dual labelling with anti-tubulin antibodies revealed that HE6/GPR64 was absent from the (kino-) cilia of ciliated cells. Instead, the receptor protein accumulated in the non-ciliated principal cells. Specifically, strong immunofluorescence was observed in the apical compartment of these cells. Dual labelling with phalloidin and anti-ezrin antibodies revealed that in the mouse the bulk amount of HE6/GPR64 protein co-localized with the F-actin-ezrin scaffold in brush border-like microvilli of ductuli efferentes and long stereocilia of the epididymis proper. In the ductuli efferentes, HE6/GPR64 also co-localized with the subapical F-actin network immediately below the microvilli. Comparable immunostaining patterns were observed in human and mouse; however, a specific feature of the human ductuli efferentes was an intense HE6/GPR64-related labelling of crypt-like grooves or furrows of hitherto unknown function. Reproduction (2008) 136 235-245

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Section: Discussionsupporting

confidence: 82%

HE6/GPR64 adhesion receptor co-localizes with apical and subapical F-actin scaffold in male excurrent duct epithelia

Kirchhoff¹,

Osterhoff²,

Samalecos³

2008

Reproduction

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“…Four genes in the latter category encode isoforms of the H + v-ATPase that localize to the plasma membrane, including atp6v1c2 (112-fold change), atp6v0a4 (100-fold change), atp6v0d2 (55-fold change) and atp6v1b1 (32-fold change) (Wagner et al, 2004;Pietrement et al, 2006;Kujala et al, 2007). Three genes on the list encode isoforms of carbonic anhydrase (ca): ca2a (64-fold change), ca2b (43-fold change) and ca12 (81-fold change), enzymes that are highly expressed by PSCs in order to catalyze the production of H + and HCO 3 -from carbon dioxide and water (Breton, 2001).…”

Section: Resultsmentioning

confidence: 99%

Specification of ion transport cells in theXenopuslarval skin

2011

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SUMMARYSpecialized epithelial cells in the amphibian skin play important roles in ion transport, but how they arise developmentally is largely unknown. Here we show that proton-secreting cells (PSCs) differentiate in the X. laevis larval skin soon after gastrulation, based on the expression of a 'kidney-specific' form of the H + v-ATPase that localizes to the plasma membrane, orthologs of the Cl -/HCO 3 -antiporters ae1 and pendrin, and two isoforms of carbonic anhydrase. Like PSCs in other species, we show that the expression of these genes is likely to be driven by an ortholog of foxi1, which is also sufficient to promote the formation of PSC precursors. Strikingly, the PSCs form in the skin as two distinct subtypes that resemble the alpha-and beta-intercalated cells of the kidney. The alpha-subtype expresses ae1 and localizes H + v-ATPases to the apical plasma membrane, whereas the beta-subtype expresses pendrin and localizes the H + v-ATPase cytosolically or basolaterally. These two subtypes are specified during early PSC differentiation by a binary switch that can be regulated by Notch signaling and by the expression of ubp1, a transcription factor of the grainyhead family. These results have implications for how PSCs are specified in vertebrates and become functionally heterogeneous.

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“…SLC26A7 expression has been identified in high endothelial venules, kidney, stomach, nasal epithelium, and epididymal ducts (7,54,83,117). SLC26A7 has been localized to the basolateral membrane of the gastric parietal cells, the renal outer medullary collecting duct and the thick ascending limb (8,20,82,83,131), the apical membrane of the proximal tubule (20), and in endosomes in MDCK cells when grown under isotonic conditions (131 (50).…”

Section: Groupmentioning

confidence: 99%

The Solute Carrier 26 Family of Proteins in Epithelial Ion Transport

et al. 2008

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Transepithelial Cl− and HCO3− transport is critically important for the function of all epithelia and, when altered or ablated, leads to a number of diseases, including cystic fibrosis, congenital chloride diarrhea, deafness, and hypotension ( 78 , 111 , 119 , 126 ). HCO3− is the biological buffer that maintains acid-base balance, thereby preventing metabolic and respiratory acidosis ( 48 ). HCO3− also buffers the pH of the mucosal layers that line all epithelia, protecting them from injury ( 2 ). Being a chaotropic ion, HCO3− is essential for solubilization of ions and macromolecules such as mucins and digestive enzymes in secreted fluids. Most epithelia have a Cl−/HCO3 exchange activity in the luminal membrane. The molecular nature of this activity remained a mystery for many years until the discovery of SLC26A3 and the realization that it is a member of a new family of Cl− and HCO3− transporters, the SLC26 family ( 73 , 78 ). This review will highlight structural features, the functional diversity, and several regulatory aspects of the SLC26 transporters.

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

Cited by 62 publications

References 48 publications

HE6/GPR64 adhesion receptor co-localizes with apical and subapical F-actin scaffold in male excurrent duct epithelia

HE6/GPR64 adhesion receptor co-localizes with apical and subapical F-actin scaffold in male excurrent duct epithelia

Specification of ion transport cells in theXenopuslarval skin

The Solute Carrier 26 Family of Proteins in Epithelial Ion Transport

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