Identification of a novel gene of the X,K‐ATPase β‐subunit family that is predominantly expressed in skeletal and heart muscles<sup>1</sup>

Pestov, Nikolay B.; Adams, Gail; Shakhparonov, M. I.; Modyanov, Nikolaï N.

doi:10.1016/s0014-5793(99)00954-0

Cited by 34 publications

(51 citation statements)

References 36 publications

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“…Transcripts of all known Na-K-ATPase ␤-subunits (␤ 1 , ␤ 2 , and ␤ 3 ) are readily detectable, whereas no signal can be observed in the case of ␤ g . The absence of ␤ m in these glands has been reported before (44). Considering the number of cycles, it appears that ␤ 1 transcripts are more abundant than ␤ 2 or ␤ 3 in all tissues studied, and ␤ 3 is more abundant than ␤ 2 .…”

Section: Analysis Of Lobe-specific Expression Of the X-k-atpasesupporting

confidence: 69%

“…Five closely related genes encoding ␤-subunits have been identified in mammals encoding three Na-K-ATPase ␤-isoforms (␤ 1 , ␤ 2 , ␤ 3 ), gastric H-K-ATPase ␤-subunit (␤ g ), and muscle-specific (␤ m ) protein. All five members of the family share a common transmembrane structure of type II membrane proteins but exhibit a much lower degree of sequence similarity (ϳ32-48%) than ␣-subunits (13, 24, 44). …”

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confidence: 99%

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Identification of the β-subunit for nongastric H-K-ATPase in rat anterior prostate

Pestov

Korneenko²,

Radkov³

et al. 2004

American Journal of Physiology-Cell Physiology

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The structural organization of nongastric H-K-ATPase, unlike that of closely related Na-K-ATPase and gastric H-K-ATPase, is not well characterized. Recently, we demonstrated that nongastric H-K-ATPase α-subunit (αng) is expressed in apical membranes of rodent prostate. Its highest level, as well as relative abundance, with respect to α1-isoform of Na-K-ATPase, was observed in anterior lobe. Here, we aimed to determine the subunit composition of nongastric H-K-ATPase through the detailed analysis of the expression of all known X-K-ATPase β-subunits in rat anterior prostate (AP). RT-PCR detects transcripts of β-subunits of Na-K-ATPase only. Measurement of absolute protein content of these three β-subunit isoforms, with the use of quantitative Western blotting of AP membrane proteins, indicates that the abundance order is β1 > β3 ≫ β2. Immunohistochemical experiments demonstrate that β1 is present predominantly in apical membranes, coinciding with αng, whereas β3 is localized in the basolateral compartment, coinciding with α1. This is the first direct demonstration of the αng-β1 colocalization in situ indicating that, in rat AP, αng associates only with β1. The existence of αng-β1 complex has been confirmed by immunoprecipitation experiments. These results indicate that β1-isoform functions as the authentic subunit of Na-K-ATPase and nongastric H-K-ATPase. Putatively, the intracellular polarization of X-K-ATPase isoforms depends on interaction with other proteins.

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Section: Analysis Of Lobe-specific Expression Of the X-k-atpasesupporting

confidence: 69%

mentioning

confidence: 99%

Identification of the β-subunit for nongastric H-K-ATPase in rat anterior prostate

Pestov

Korneenko²,

Radkov³

et al. 2004

American Journal of Physiology-Cell Physiology

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“…The functional Na ϩ pump consists of an association of one ␣-catalytic subunit and one ␤-glycoprotein subunit of Na ϩ -K ϩ -ATPase. Some isoforms are expressed ubiquitously, whereas some are expressed in a tissue-specific manner (2,39,40,52).…”

Section: Discussionmentioning

confidence: 99%

“…Apical Na ϩ from the endolymph enters SCCD epithelial cells through ENaC and is extruded from the cytosol into the perilymph across the basolateral membrane by Na ϩ -K ϩ -ATPase, which is a heterodimer composed of one ␣-subunit and one ␤-subunit. Four ␣-subunit (␣ l , ␣ 2 , ␣ 3 , and ␣ 4 ) and four ␤-subunit (␤ 1 , ␤ 2 , ␤ 3 , and ␤ 4 ) isoforms of Na ϩ -K ϩ -ATPase have been identified (39,40,52). Recently, a ␥-subunit was also cloned and found to regulate the function of Na ϩ -K ϩ -ATPase (2).…”

mentioning

confidence: 99%

Glucocorticoid regulation of genes in the amiloride-sensitive sodium transport pathway by semicircular canal duct epithelium of neonatal rat

Pondugula¹,

Raveendran²,

Ergönül

et al. 2006

Physiological Genomics

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, which is important for transduction processes. We have recently shown that glucocorticoid receptors (GR) stimulate absorption of Na ϩ by semicircular canal duct (SCCD) epithelia. In the present study, we sought to determine the presence of genes involved in the control of the amiloride-sensitive Na ϩ transport pathway in rat SCCD epithelia and whether their level of expression was regulated by glucocorticoids using quantitative real-time RT-PCR. Transcripts were present for ␣-, ␤-, and ␥-subunits of the epithelial sodium channel (ENaC); the ␣1-, ␣3-, ␤1-, and ␤3-isoforms of Na ϩ -K ϩ -ATPase; inwardly rectifying potassium channels [IC50 of short circuit current (Isc) for Ba 2ϩ : 210 M] Kir2

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“…Recently, a novel member of the ␤-subunit family has been identified (␤ m ) which shares common structural features and signature motifs with X-K-ATPase ␤-isoforms (355). Despite the similarities with X-K-ATPase ␤-isoforms, ␤ m has also some atypical characteristics.…”

Section: ␤-Subunit Isoformsmentioning

confidence: 99%

Cell Adhesion, Polarity, and Epithelia in the Dawn of Metazoans

Cereijido

Contreras

Shoshani

2004

Physiological Reviews

151

100

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Transporting epithelia posed formidable conundrums right from the moment that Du Bois Raymond discovered their asymmetric behavior, a century and a half ago. It took a century and a half to start unraveling the mechanisms of occluding junctions and polarity, but we now face another puzzle: lest its cells died in minutes, the first high metazoa (i.e., higher than a sponge) needed a transporting epithelium, but a transporting epithelium is an incredibly improbable combination of occluding junctions and cell polarity. How could these coincide in the same individual organism and within minutes? We review occluding junctions (tight and septate) as well as the polarized distribution of Na+-K+-ATPase both at the molecular and the cell level. Junctions and polarity depend on hosts of molecular species and cellular processes, which are briefly reviewed whenever they are suspected to have played a role in the dawn of epithelia and metazoan. We come to the conclusion that most of the molecules needed were already present in early protozoan and discuss a few plausible alternatives to solve the riddle described above.

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Identification of a novel gene of the X,K‐ATPase β‐subunit family that is predominantly expressed in skeletal and heart muscles¹

Cited by 34 publications

References 36 publications

Identification of the β-subunit for nongastric H-K-ATPase in rat anterior prostate

Identification of the β-subunit for nongastric H-K-ATPase in rat anterior prostate

Glucocorticoid regulation of genes in the amiloride-sensitive sodium transport pathway by semicircular canal duct epithelium of neonatal rat

Cell Adhesion, Polarity, and Epithelia in the Dawn of Metazoans

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Identification of a novel gene of the X,K‐ATPase β‐subunit family that is predominantly expressed in skeletal and heart muscles1

Cited by 34 publications

References 36 publications

Identification of the β-subunit for nongastric H-K-ATPase in rat anterior prostate

Identification of the β-subunit for nongastric H-K-ATPase in rat anterior prostate

Glucocorticoid regulation of genes in the amiloride-sensitive sodium transport pathway by semicircular canal duct epithelium of neonatal rat

Cell Adhesion, Polarity, and Epithelia in the Dawn of Metazoans

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Identification of a novel gene of the X,K‐ATPase β‐subunit family that is predominantly expressed in skeletal and heart muscles¹