Chapter 7 Biosynthesis of Na+, K+-ATPase in Amphibian Epithelial Cells

Rossjer, B.C.

doi:10.1016/s0070-2161(08)60874-6

Cited by 18 publications

(9 citation statements)

References 76 publications

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“…The biosynthesis [536][537][538][539][540], intraccllularsortingand polarized delivery' [541], and pretranslational regula tion [542] of Na.K-ATPase was studied in MDCK, and in A6 and TB-M cells. A6 cells, which are responsive to mineralocorticoids, further provided a useful model to correlate the induction of transcription of Na.KATPase mRNA, and translation of a-and (3-subunit proteins with the increased sodium transport upon stimulation by aldosterone [315.…”

Section: The Cell and Molecular Biological Approachmentioning

confidence: 99%

Epithelial Cells in Tissue Culture

Gstraunthaler

1988

Kidney Blood Press Res

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In this review the characteristics of established renal and intestinal epithelial cell lines are described by summarizing the accumulated literature about specific properties retained by the cells in tissue culture. Furthermore, brief examples are given for the use of cultured epithelia as model systems to study epithelial transport and metabolic functions, epithelial cell polarity, and aspects of the differentiation and maturation of epithelia by physiological, biochemical and genetic, or cell and molecular biological approaches.

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Section: The Cell and Molecular Biological Approachmentioning

confidence: 99%

Epithelial Cells in Tissue Culture

Gstraunthaler

1988

Kidney Blood Press Res

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“…We have previously shown that the synthesis of both a-and [3-subunit of Na+,K+-ATPase is remarkably coordinated. A parallel change in the rate of synthesis of each subunit is observed whether the system is up-or down-regulated by hormones or drugs (6,7,28,40). This is a rather striking observation since each subunit is coded for by distinct species of mRNAs (2.6 kb vs. 3.9 kb) which can be translated in a cellfree system and inserted independently into endoplasmic reticulum (8).…”

Section: The Coordinate Control Of a And ~ Mrna Accumulation And The mentioning

confidence: 99%

Regulation by aldosterone of Na+,K+-ATPase mRNAs, protein synthesis, and sodium transport in cultured kidney cells.

Verrey¹,

Schaerer²,

Zoerkler³

et al. 1987

The Journal of Cell Biology

151

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Abstract. Transepithelial Na ÷ reabsorption across tight epithelia is regulated by aldosterone. Mineralocorticoids modulate the expression of a number of proteins. Na+,K+-ATPase has been identified as an aldosteroneinduced protein (Geering, K., M. Girardet, C. Bron, J. P. Kraehenbuhl, and B. C. Rossier, 1982, J. Biol. Chem., 257:10338-10343). Using A6 cells (kidney of Xenopus laevis) grown on filters we demonstrated by Northern blot analysis that the induction of Na+,K ÷-ATPase was mainly mediated by a two-to fourfold accumulation of both a-and 13-subunit mRNAs. The specific competitor spironolactone decreased basal Na + transport, Na+,K+-ATPase mRNA, and the relative rate of protein biosynthesis, and it blocked the response to aldosterone. Cycloheximide inhibited the aldosteronedependent sodium transport but did not significantly affect the cytoplasmic accumulation of Na+,K+-ATPase mRNA induced by aldosterone.

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“…This enzyme contains two subunits, o(M r=96,000) and /2(Mr=45,000-65,000) [11]. Several authors [for review see ref .…”

Section: Resultsmentioning

confidence: 99%

“…Since cells in general devote a large fraction of the ATP they produce to transport Na+ and K+ ions across their plasma membrane [11], we wondered whether an abnormally high activ ity of the Na+, K+-ATPase in trembler nerves could account for this increased 0 2 consumption. Our finding of slightly reduced activities in mutant nerves does not support this hypothesis and is in fair agreement with values previously reported by Bourre et al [12], On the other hand, during the course of these experiments, unexpected high levels of ouabain-insensitive Mg2+-ATPase were measured in adult trembler nerves.…”

Section: Introductionmentioning

confidence: 99%

Three ATPase Activities Have an Abnormal Developmental Time Course in Trembler Sciatic Nerves

Bürgisser¹,

Geering²,

Rossier³

et al. 1987

Dev Neurosci

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Trembler mutant mice are affected by a peripheral neuropathy characterized by hypomyelination, demyelination, and Schwann cell proliferation. In adult mutants, supernumerary Schwann cells form membranous structures known as ''onion-bulb'' formations. The activities of the Na⁺, K⁺-ATPase and of two ouabain-insensitive Mg²⁺-ATPases were investigated in sciatic nerves of young and adult mutants. The Na⁺, K⁺-ATPase activities were 92 and 76% of the control values in young and adult mutants, respectively. By immunoblot analysis, the α-subunit of the Na⁺, K⁺-ATPase had an identical apparent molecular weight in controls at both ages and in young mutants. In adult mutants, on the contrary, the α-subunit appeared smaller by about 2 kd, similar to that in kidney, indicating that the Na⁺, K⁺-ATPase was localized mainly on supernumerary Schwann cells. In addition, in the mutants, the developmental increase of both the mitochondrial and the nonmitochondrial Mg²⁺-ATPase was abnormally high. We suggest that the abnormal increase of the nonmitochondrial Mg²⁺-ATPase activity during development reflects an enrichment of that enzyme in ''onion-bulb'' formations.

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Chapter 7 Biosynthesis of Na+, K+-ATPase in Amphibian Epithelial Cells

Cited by 18 publications

References 76 publications

Epithelial Cells in Tissue Culture

Epithelial Cells in Tissue Culture

Regulation by aldosterone of Na+,K+-ATPase mRNAs, protein synthesis, and sodium transport in cultured kidney cells.

Three ATPase Activities Have an Abnormal Developmental Time Course in Trembler Sciatic Nerves

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