The induction of (Na++K+)-ATPase in the salt gland of the duck

Lingham, Russell B.; Sen, Amar K.

doi:10.1016/0005-2736(80)90527-1

Cited by 24 publications

(5 citation statements)

References 18 publications

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“…6). These observations taken in conjunction with SDS-PAGE studies by other investigators (Hopkins et al, 1976;Stewart et al, 1976;Lingham et al, 1980) Biosynthetic events associated with the first 12 hy of salt stress. The top graph represents increased levels of Na,K-ATPase as measured by 'H-ouabain binding and ATP hydrolysis.…”

Section: Sds-page and Fluorographic Analysis Ofsupporting

confidence: 66%

“…Stewart et al (1976) have found that Na,K-ATPase makes up as much as 27-44% of total plasma membrane protein in salt stressed glands. Using a double-label technique, Lingham et al (1980) have reported an increased rate of synthesis of Na,KATPase after 24 hr of salt stress. In addition, Mazurkiewicz and Barrnett (1981) have reported that in primary cultures of secretory cells isolated from 3-day salt stressed glands, 8-10% of the total 3H-leucine incorporation could be attributed to uptake into Na,K-ATPase as monitored by immunoprecipitation.…”

Section: Discussionmentioning

confidence: 98%

“…Only a limited number of studies of the salt gland, however, have focused on early biosynthetic events associated with salt-stress. Increases in the level of the plasma membrane marker Na,K-ATPase (ATP phosphohydrolase, EC 3.6.1.3) have been measured after 24-hr of treatment (Ernst and Mills, 1977;Hossler et al, 1978a;Lingham et al, 1980). In addition, increases in acyltransferase activity (Levine et al, 19721, in total DNA and RNA content (Holmes and Stewart, 1968;Hossler, 1982), and in the number of free polysomes have been detected after 24 hr of salt-stress (Stewart and Holmes, 1970).…”

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confidence: 99%

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Plasma membrane biogenesis in the avian salt gland: A biochemical and quantitative electron microscopic autoradiographic study

et al. 1985

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The avian salt gland provides an ideal system for the study of plasma membrane (PM) biogenesis. Feeding ducklings 1% sodium chloride (salt stress) induces the secretory cells of the gland to synthesize large amounts of PM, which forms an extensive basolateral PM domain after 7-9 days of treatment. In the present study, the initial biosynthetic events following salt stress were investigated. In vivo studies using 3H-uridine indicated that increased rates of RNA synthesis could be detected by 2 hr after the beginning of salt stress and continued through at least 12 hr. Under in vitro conditions, increased rates of protein and glycoprotein synthesis (as monitored by 3H-leucine and 3H-fucose incorporation, respectively) were also detected after 2 hr and continued through 7-9 days. Increased levels of Na,K-ATPase, a specific secretory cell PM marker, were detected after 8 hr of treatment as monitored by specific activity and 3H-ouabain binding. Sodium dodecyl sulfate-polyacrylamide slab gel electrophoresis coupled with fluorography indicated that both 3H-leucine and 3H-fucose were incorporated into partially purified preparations of Na,K-ATPase isolated after 12 hr. Light microscopic autoradiographic analysis of pulse-chase experiments indicated that in secretory cells of 12-hr salt-stressed glands, 3H-leucine- and 3H-fucose-labelled products reached the cell periphery by 1-2 hr after the initial pulse. The incorporation of both tritiated precursors was predominantly associated with the secretory cells. Quantitative electron microscopic autoradiography indicated that 3H-leucine is initially taken up by elements of the rough endoplasmic reticulum (RER) and cytoplasm (5 min postpulse), subsequently transported to and concentrated within components of the Golgi apparatus (10 min of chase), and ultimately incorporated into all domains of the plasma membrane of secretory cells by 1-2 hr of chase. The data is consistent with a flow of newly synthesized membrane components from RER to Golgi to plasma membrane and is analogous to the pattern previously found for the synthesis and processing of PM proteins in a wide variety of cell types.

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Section: Sds-page and Fluorographic Analysis Ofsupporting

confidence: 66%

Section: Discussionmentioning

confidence: 98%

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confidence: 99%

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Plasma membrane biogenesis in the avian salt gland: A biochemical and quantitative electron microscopic autoradiographic study

et al. 1985

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“…The increase in plasma osmolality results in a rapid increase in the rate of NaCl secretion by the gland by means of a cholinergic mechanism, and a slower increase in the Na + ,K + -ATPase content of the gland because of both an increase in its size and a 4-fold increase in its Na + ,K + -ATPase specific activity (Na + ,K + -ATPase activity per milligram of protein) (53). The increased Na + ,K + -ATPase activity results from an increase in the rate of enzyme synthesis (54,55). Stewart et al (54) prepared Na + ,K + -ATPase from salt glands of salt-adapted ducks which had a specific activity of 17 EU; the preparation was not pure, and contamination of the Na + ,K + -ATPase with the other proteins no doubt contributed to the low specific activity.…”

Section: Discussionmentioning

confidence: 99%

Preparation of Na⁺,K⁺-ATPase with Near Maximal Specific Activity and Phosphorylation Capacity: Evidence That the Reaction Mechanism Involves All of the Sites

Martin

Sachs

1999

Biochemistry

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The phosphorylation capacity of Na+,K+-ATPase preparations in common use is much less than expected on the basis of the molecular weight of the enzyme deduced from cDNA sequences. This has led to the popularity of half-of-the-sites or flip-flop models for the enzyme reaction mechanism. We have prepared Na+,K+-ATPase from nasal salt glands of salt-adapted ducks which has a phosphorylation capacity and specific activity near the theoretical maxima. Preparations with specific activities of >60 micromol (mg of protein)-1 min-1 at 37 degrees C had phosphorylation capacities of >60 nmol/mg of protein, and the rate of turnover of the enzyme was 9690 min-1, within the range reported for the enzyme from other sources. The fraction of the maximal specific activity of the enzyme compared well with the fraction of the protein on SDS-PAGE which was alpha and beta chains, especially at the highest specific activity which indicates that all of the alphabeta protomers are active. The gels of the most reactive preparations contained only alpha and beta chains, but less active preparations contained a number of extraneous proteins. The major contaminant was actin. The preparation did not contain any protein which migrated in the molecular weight range of the gamma subunit. The subunit composition of the enzyme was alpha1 and beta1 only. This is the first report of a pure, homogeneous, fully active preparation of the protein. Reaction models which incorporate a half-of-the-sites or flip-flop mechanism do not apply to this enzyme.

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“…At present, relatively little is known about this topic. Concerning upregulation, it has been shown that thyroid hormones in mammals (Lo & Edelmann, 1976;Lin & Akera, 1978), aldosterone in amphibia (Geering et al, 1982(Geering et al, , 1984 or salt stress in marine ducks (Hossler et al, 1978;Lingham et al, 1980) stimulate the biosynthesis of Na,K-ATPase molecules and their insertion into the plasma membrane.…”

Section: Receptor Recyclingmentioning

confidence: 99%

The receptor function of the Na+, K+-activated adenosine triphosphatase system

Anner¹

1985

Biochemical Journal

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The induction of (Na++K+)-ATPase in the salt gland of the duck

Cited by 24 publications

References 18 publications

Plasma membrane biogenesis in the avian salt gland: A biochemical and quantitative electron microscopic autoradiographic study

Plasma membrane biogenesis in the avian salt gland: A biochemical and quantitative electron microscopic autoradiographic study

Preparation of Na⁺,K⁺-ATPase with Near Maximal Specific Activity and Phosphorylation Capacity: Evidence That the Reaction Mechanism Involves All of the Sites

The receptor function of the Na+, K+-activated adenosine triphosphatase system

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The induction of (Na++K+)-ATPase in the salt gland of the duck

Cited by 24 publications

References 18 publications

Plasma membrane biogenesis in the avian salt gland: A biochemical and quantitative electron microscopic autoradiographic study

Plasma membrane biogenesis in the avian salt gland: A biochemical and quantitative electron microscopic autoradiographic study

Preparation of Na+,K+-ATPase with Near Maximal Specific Activity and Phosphorylation Capacity: Evidence That the Reaction Mechanism Involves All of the Sites

The receptor function of the Na+, K+-activated adenosine triphosphatase system

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Product

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Preparation of Na⁺,K⁺-ATPase with Near Maximal Specific Activity and Phosphorylation Capacity: Evidence That the Reaction Mechanism Involves All of the Sites