Na,K-ATPase α- and β-isoforms in the developing cochlea of the mouse

Erichsen, Susan; Zuo, Jian; Curtis, Lisa M.; Rarey, Kyle E.; Hultcrantz, Malou

doi:10.1016/0378-5955(96)00105-0

Cited by 56 publications

(43 citation statements)

References 20 publications

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“…Thus, there does not seem to be a particular subcellular compartment to which NKAα3 expression is restricted in either the central or peripheral nervous system. Our findings are consistent with earlier research using immunocytochemistry that identified the NKAα3 in the SGNs and cochlear nerve in the gerbil (Schulte and Adams 1989;McGuirt and Schulte 1994;Nakazawa et al 1995), rat (ten Cate et al 1994;Peters et al 2001), and mouse (Erichsen et al 1996). NKAα immunoreactivity was localized to the nerve terminals underlying the IHCs and OHCs in the human cochlea (Weber et al 2001).…”

Section: Discussionsupporting

confidence: 92%

“…We found no NKAα1 immunoreactivity in the afferent terminals. Previous studies have reported weak to moderate NKAα1 immunoreactivity in the SGNs and cochlear nerve of the rat (ten Cate et al 1994;Peters et al 2001;Delprat et al 2007) and mouse (Erichsen et al 1996), and one study reports expression of the NKAα in the afferent terminals underlying the OHCs in the gerbil (Nakazawa et al 1995). Although we did not find NKAα1 immunoreactivity in either type I or II afferent terminals, we did see NKAα1 labeling in the spiral ganglion (data not shown) but were unable to identify unequivocally the NKAα1-expressing cells as either the SGNs or ensheathing satellite cells.…”

Section: Discussionmentioning

confidence: 92%

“…We were unable to detect NKAα2 immunoreactivity in the organ of Corti or spiral ganglion with either of two antibodies used (data not shown). While some groups have reported exclusive expression of the NKAα2 in the supralimbal fibrocytes (McGuirt and Schulte 1994;Schulte and Steel 1994;Peters et al 2001), others have reported additional weak or transient NKAα2 immunoreactivity in the cochlear nerve (ten Cate et al 1994;Erichsen et al 1996).…”

Section: Discussionmentioning

confidence: 99%

“…Nonetheless, earlier work also reported expression of the NKAα in the neuronal elements of the mammalian cochlea using a variety of techniques, including enzyme cytochemistry (Kerr et al 1982), in situ hybridization (Ryan and Watts 1991), and immunohistochemistry (Schulte and Adams 1989;Iwano et al 1990;McGuirt and Schulte 1994;Schulte and Steel 1994;ten Cate et al 1994;Nakazawa et al 1995;Zuo et al 1995;Erichsen et al 1996;Peters et al 2001;Weber et al 2001).…”

Section: Introductionmentioning

confidence: 99%

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Distribution of the Na,K-ATPase α Subunit in the Rat Spiral Ganglion and Organ of Corti

McLean

Smith

Glowatzki

et al. 2008

JARO

107

105

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Processing of sound in the cochlea involves both afferent and efferent innervation. The Na,K-ATPase (NKA) is essential for cells that maintain hyperpolarized membrane potentials and sodium and potassium concentration gradients. Heterogeneity of NKA subunit expression is one mechanism that tailors physiology to particular cellular demands. Therefore, to provide insight into molecular differences that distinguish the various innervation pathways in the cochlea, we performed a variety of double labeling experiments with antibodies against three of the α isoforms of the NKA (NKAα1-3) and markers identifying particular subsets of neurons or supporting cells in whole mount preparations of the organ of Corti and spiral ganglion. We found that the NKAα3 is abundantly expressed within the membranes of the spiral ganglion somata, the type I afferent terminals contacting the inner hair cells, and the medial efferent terminals contacting the outer hair cells. We also found expression of the NKAα1 in the supporting cells that neighbor the inner hair cells and express the glutamate transporter GLAST. These findings suggest that both the NKAα1 and NKAα3 are poised to play an essential role in the regulation of the type I afferent synapses, the medial efferent synapses, and also glutamate transport from the afferent-inner hair cell synapse.

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Section: Discussionsupporting

confidence: 92%

Section: Discussionmentioning

confidence: 92%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Distribution of the Na,K-ATPase α Subunit in the Rat Spiral Ganglion and Organ of Corti

McLean

Smith

Glowatzki

et al. 2008

JARO

107

105

View full text Add to dashboard Cite

show abstract

“…The rationale for the current study comes from the finding that the cochlea contains a number of proteins known to interact with NHERFs, plus numerous other proteins that have PDZ domains that could potentially interact with NHERFs. These cochlear proteins include NHE3 (Bond et al 1998), the ERM family (Kitajiri et al 2004), actin (Geal-Dor et al 1993;Nishida et al 1998), myosin (Boeda et al 2002;Johnson et al 2003;Mburu et al 2003;Kitajiri et al 2004;Belyantseva et al 2005;Kikkawa et al 2005), NBC3 (Bok et al 2003), P2Y1 (Teixeira et al 2000), β-adrenergic receptors (Fauser et al 2004), the vacuolar proton pump v-H + -ATPase (Stankovic et al 1997), Na + -K + ATPase (Ichimiya et al 1994;Erichsen et al 1996), growth factor receptors (Pickles and van Heumen 1997), glucocorticoid receptors (Erichsen et al 1996), TASK-1 background K + channels (Kanjhan et al 2004a), inwardly rectifying K + channels Kir1.1 (ROMK1) (Glowatzki et al 1995), Kir4.1 and Kir5.1 (Hibino et al 2004), aquaporin-4 (Mhatre et al 2002), glutamate transporter GLAST (Furness and Lehre 1997), and plasma membrane Ca 2+ -ATPase (Ichimiya et al 1994;Dumont et al 2001). …”

Section: Discussionmentioning

confidence: 99%

Postnatal developmental expression of the PDZ scaffolds Na+-H+ exchanger regulatory factors 1 and 2 in the rat cochlea

et al. 2005

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Sensory transduction in the mammalian cochlea requires the maintenance of specialized fluid compartments with distinct ionic compositions. This is achieved by the concerted action of diverse ion channels and transporters, some of which can interact with the PDZ scaffolds, Na + -H + exchanger regulatory factors 1 and 2 (NHERF-1, NHERF-2). Here, we report that NHERF-1 and NHERF-2 are widely expressed in the rat cochlea, and that their expression is developmentally regulated. Reverse transcription/polymerase chain reaction (RT-PCR) and Western blotting initially confirmed the RNA and protein expression of NHERFs. We then performed immunohistochemistry on cochlea during various stages of postnatal development. Prior to the onset of hearing (P8), NHERF-1 immunolabeling was prominently polarized to the apical membrane of cells lining the endolymphatic compartment, including the stereocilia and cuticular plates of the inner and outer hair cells, marginal cells of the stria vascularis, Reissner's epithelia, and tectorial membrane. With maturation (P21, P70), NHERF-1 immunolabeling was reduced in the above structures, whereas labeling increased in the apical membrane of the interdental cells of the spiral limbus and the inner and outer sulcus cells, Hensen's cells, the inner and outer pillar cells, Deiters cells, the inner border cells, spiral ligament fibrocytes, and spiral ganglion neurons (particularly type II). NHERF-1 expression in strial basal and intermediate cells was persistent. NHERF-2 immunolabeling was similar to that for NHERF-1 during postnatal development, with the exception of expression in the synaptic regions beneath the outer hair cells. NHERF-1 and NHERF-2 co-localized with glial fibrillary acidic protein and vimentin in glia. The cochlear localization of NHERF scaffolds suggests that they play important roles in the developmental regulation of ion transport, homeostasis, and auditory neurotransmission.

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Human Corneal Endothelial Cell Expression of Na+, K+–Adenosine Triphosphatase Isoforms

Huang

Blanco²,

Mercer³

et al. 2003

Arch Ophthalmol

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To determine the expression of ␣ subunits and different isozymes of Na + ,K + -adenosine triphosphatase (ATPase) in human corneal endothelial cells (HCECs).Methods: Immunoblot and RNA analysis of Na + ,K + -ATPase ␣ subunit expression were performed in preparations from HCECs that had been immortalized by transformation with simian virus 40. Na + ,K + -ATPase activity was determined by constructing dose-response curves for the ouabain inhibition of Na + ,K + -ATPase activity in human corneal endothelial cells.Results: Both messenger RNA analysis and immunoblot studies indicated that HCECs express ATPase catalytic ␣1 and ␣3, but not ␣2 and ␣4, subunits. A limited amount of ␣3 subunit was expressed in HCECs compared with the ␣1 subunit. Biochemical analyses of Na + ,K + -ATPase activity revealed 2 independently active Na + ,K + -ATPase isoenzymes, a low-affinity site with a kinetic parameter for ouabain inhibition constant (K i ) in the micromolar range and a high-affinity site with a constant K i in the nanomolar range. These 2 sites may be associated with ␣1 and ␣3 isoforms, respectively, expressed in HCECs.Conclusions: Human corneal endothelial cells express ␣1 and ␣3 isoforms of Na + ,K + -ATPase, and both polypeptides are catalytically competent in these cells. Defining the components of Na + ,K + -ATPase in HCECs is an important step toward elucidating the mechanisms that regulate corneal endothelial ionic pump function as well as the pathogenesis of corneal diseases associated with corneal edema.

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Na,K-ATPase α- and β-isoforms in the developing cochlea of the mouse

Cited by 56 publications

References 20 publications

Distribution of the Na,K-ATPase α Subunit in the Rat Spiral Ganglion and Organ of Corti

Distribution of the Na,K-ATPase α Subunit in the Rat Spiral Ganglion and Organ of Corti

Postnatal developmental expression of the PDZ scaffolds Na+-H+ exchanger regulatory factors 1 and 2 in the rat cochlea

Human Corneal Endothelial Cell Expression of Na+, K+–Adenosine Triphosphatase Isoforms

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