Foxj1 is required for apical localization of ezrin in airway epithelial cells

Huang, Tao; You, Yingjian; Spoor, Melanie S.; Richer, Edward J.; Kudva, Vrinda. V.; Paige, Renee C.; Seiler, Michael P.; Liebler, Janice M.; Zabner, Joseph; Plopper, Charles G.; Brody, Steven L.

doi:10.1242/jcs.00830

Cited by 89 publications

(80 citation statements)

References 65 publications

(82 reference statements)

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“…These cells most probably represented the ciliated cell type of the ductuli efferentes. Apical ezrin expression had previously been observed in ciliated airway epithelial cells (Huang et al 2003). In the male genital tract, however, different from the airway epithelium, ezrin appeared to be present also in the nonciliated cells (compare also Höfer & Drenckhahn 1996).…”

Section: Association Of He6/gpr64 With the Apical F-actin-ezrin Scaffoldmentioning

confidence: 61%

“…An apical area immediately below the ciliated tufts was positive for F-actin and ezrin, but was completely devoid of HE6/GPR64. Indeed, ezrin has been found in the apical domain of specialized ciliated cells of the airway epithelium (Huang et al 2003) and may thus also be expressed in the ciliated cell type of the ductuli efferentes. A profilin-like protein that was previously suggested to link HE6/GPR64 to the actin cytoskeleton (Kirchhoff et al 2006), however, could not be verified by co-localization studies (data not shown).…”

Section: Discussionmentioning

confidence: 99%

“…Ezrin, a minor component of microvilli in the male excurrent ducts (Hö fer & Drenckhahn 1996), is considered to be an organizer of the brush border and/or actin terminal web. More recently, ezrin was also found in the apical domain of specialized ciliated cells (Huang et al 2003).…”

Section: Association Of He6/gpr64 With the Apical F-actin-ezrin Scaffoldmentioning

confidence: 97%

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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: Association Of He6/gpr64 With the Apical F-actin-ezrin Scaffoldmentioning

confidence: 61%

Section: Discussionmentioning

confidence: 99%

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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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“…However, it has recently been suggested that scaffolding proteins of the ezrin-radixin-moesin (ERM) family must be correctly localized at the PM for proper CFTR trafficking and function (Short et al, 1998;Mohler et al, 1999;Huang et al, 2003). Epithelial inflammation and remodeling have been reported to alter ERM protein expression (Laoukili et al, 2001), which could impair localization of ⌬F508 protein to the apical PM.…”

Section: Introductionmentioning

confidence: 99%

Characterization of Wild-Type and ΔF508 Cystic Fibrosis Transmembrane Regulator in Human Respiratory Epithelia

Kreda

Mall

Mengos

et al. 2005

MBoC

233

210

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Previous studies in native tissues have produced conflicting data on the localization and metabolic fate of WT and ⌬F508 cystic fibrosis transmembrane regulator (CFTR) in the lung. Combining immunocytochemical and biochemical studies utilizing new high-affinity CFTR mAbs with ion transport assays, we examined both 1) the cell type and region specific expression of CFTR in normal airways and 2) the metabolic fate of ⌬F508 CFTR and associated ERM proteins in the cystic fibrosis lung. Studies of lungs from a large number of normal subjects revealed that WT CFTR protein localized to the apical membrane of ciliated cells within the superficial epithelium and gland ducts. In contrast, other cell types in the superficial, gland acinar, and alveolar epithelia expressed little WT CFTR protein. No ⌬F508 CFTR mature protein or function could be detected in airway specimens freshly excised from a large number of ⌬F508 homozygous subjects, despite an intact ERM complex. In sum, our data demonstrate that WT CFTR is predominantly expressed in ciliated cells, and ⌬F508 CFTR pathogenesis in native tissues, like heterologous cells, reflects loss of normal protein processing.

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“…We used primary epithelial layers differentiated from murine (mouse) tracheal epithelia on permeable supports in culture as previously described. 17 The support is the plastic "insert" of the Ussing chamber (EC8225 Warner Instruments, Inc.) and is shown in panel a of Fig. 1.…”

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confidence: 99%

A synthetic, chloride-selective channel that alters chloride transport in epithelial cells

et al. 2006

Self Cite

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An Ussing chamber was used to demonstrate that synthetic amphiphilic anion transporters function as chloride transporters in mammalian airway epithelial cells.Proteins are generally required for the transport of ionic and molecular species through bilayer membranes. Because these proteins are both critical and complex, bioorganic chemists have devised a variety of functional model systems. Two decades ago, synthetic ion channels were virtually unknown, but several worthy examples have emerged recently. 1 In our laboratory, we have designed and characterized structurally different families of synthetic cation-2 and anion-selective 3 channels. We refer to the former as hydraphiles; 4 this family of cation channels is now well characterized. The cation channels incorporate macrocyclic "crown" polyethers and are thought to function as monomers within the bilayer. In contrast, the anion channels developed in our laboratory are amphiphilic peptides 3,5,6,7 that function, at least in some cases, as dimers. 8 The active molecules have the general structure (R 1 ) 2 NCOCH 2 OCH 2 CO-(Gly) 3 Pro(Gly) 3 -OR 2 . Extensive structural variation 5-7 and selectivity studies 9 have been conducted in liposomes.Vectorial ion transport across lung epithelial cell layers is essential for homeostasis in multicellular organisms and disruption of this process is pathological. 10,11 Epithelial cell layers control mass transport of water and solutes in alimentary, pulmonary, renal, and a variety of secretory organs. Anion regulation is critical in the function of epithelial layers. We now report that a synthetic anion channel, based on the general structure shown above, mediates anion regulation in airway epithelial cells.The preparation of (H 37 C 18 ) 2 NCOCH 2 OCH 2 CO-(Gly) 3 -Pro(Gly) 3 -OCH 2 Ph, 1, has been reported. 5 The ca. six-fold less effective variant, (H 37 C 18 ) 2 NCOCH 2 OCH 2 CO-(Gly) 3 Leu (Gly) 3 -OCH 2 Ph, 2 ,3 was chosen as a control. When 1 was added to DOPC-DOPA (7 : 3) liposomes containing chloride ion, an increase in Cl -permeability was observed. Compound

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Foxj1 is required for apical localization of ezrin in airway epithelial cells

Cited by 89 publications

References 65 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

Characterization of Wild-Type and ΔF508 Cystic Fibrosis Transmembrane Regulator in Human Respiratory Epithelia

A synthetic, chloride-selective channel that alters chloride transport in epithelial cells

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