Characteristics of β-adrenergic-activated Na-proton transport in red blood cells

Motais, R; Scheuring, Uwe; Borgèse, Franck; Garcia-Romeu, F

doi:10.1016/b978-0-444-81125-7.50022-0

Cited by 15 publications

(10 citation statements)

References 17 publications

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“…5), suggests that the truncated Na+/H+ antiporter (TA559) is no longer activated by cAMP. As the trout red cell exchanger is activated by phorbol esters (19), we also examined whether PKC activators (a-thrombin and phorbol esters) stimulate both the wild-type antiporter and the deletion mutant (Fig. 5).…”

Section: Resultsmentioning

confidence: 99%

“…The antiporter cDNA clone described here will be a valuable tool for answering other important questions related to the peculiar regulatory properties of the cAMP-dependent Na+/H+ exchanger. Indeed, it has been shown previously that,8NHE is desensitized despite the continued presence of cAMP (38) and that desensitization leads to refractoriness (19). Moreover, the activity of,NHE is controlled by molecular oxygen through a change in the quaternary structure of hemoglobin (39).…”

Section: Discussionmentioning

confidence: 99%

“…It was of interest to consider the Na+/H+ exchanger found in nucleated trout red cells (termed f3NHE) since, in contradistinction to NHE1 and to the apical antiporter, it is activated by cAMP and other cAMP-dependent protein kinase (protein kinase A; PKA) activators such as catecholamines or forskolin (16)(17)(18)(19). Thus, it is likely to represent an additional form of antiporter.…”

mentioning

confidence: 99%

“…Thus, it is likely to represent an additional form of antiporter. The trout red cell exchanger is also activated by a distinct signaling pathway involving protein kinase C (PKC) (19 Fig. 1).…”

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confidence: 99%

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Cloning and expression of a cAMP-activated Na+/H+ exchanger: evidence that the cytoplasmic domain mediates hormonal regulation.

Borgèse¹,

Sardet²,

Cappadoro³

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

136

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The ubiquitous plasma membrane Na+/H+ exchanger (termed NHE1) is activated by diverse hormonal signals, with the notable exception of hormones acting through cAMP as second messenger. Therefore, the Na+/H+ exchanger found in the nucleated trout red cell is of particular interest since it is activated by catecholamines, forskolin, and cAMP analogues. We report here that a cloned cDNA encoding the red cell exchanger restores functional Na+/H+ activity when transfected into Na+/H+ antiporter-deficient fibroblasts (i.e., it regulates intracellular pH in a Na-dependent and amiloridesensitive manner). This red cell exchanger represents an ad-

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Cloning and expression of a cAMP-activated Na+/H+ exchanger: evidence that the cytoplasmic domain mediates hormonal regulation.

Borgèse¹,

Sardet²,

Cappadoro³

et al. 1992

Proc. Natl. Acad. Sci. U.S.A.

136

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“…This Na+-H+ exchanger cannot significantly regulate cell volume after cell shrinkage (Motais, Scheuring, Borgese & Garcia-Romeu, 1990;Motais, Borgese, Fievet & Garcia-Romeu, 1992) as others do, but its activation promotes an enlargement of cells suspended in an isotonic medium (i.e. it induces a perturbation of the steady-state cell volume).…”

Section: Discussionmentioning

confidence: 99%

Evidence for a K(+)‐H+ exchange in trout red blood cells.

Fiévet

Guizouarn

Pellissier

et al. 1993

The Journal of Physiology

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SUMMARY1. Exposure of trout red blood cells to ,-adrenergic agonist isoprenaline activates a cAMP-dependent Na+-H+ antiport, the movements of protons being compensated by a Cl--OH-(or HCO3) exchange mediated by band 3 protein. The absorption of water osmotically linked to sodium and chloride induces cell swelling.2. In the presence of acetazolamide, anionic exchange is inhibited and activation of cationic exchange resulted in the first 2 min in a strong external acidification and a large internal alkalinization leading to a reversal of the transmembrane pH gradient. Then, for at least 1 h and despite the inhibition of Cl-entry, a net Na+ uptake occurred which was balanced by an equivalent K+ loss, with the result that cell volume and pH gradient remained unchanged.3. In such conditions, the inactivation of the Na+-H+ exchanger by a /8-antagonist, propanolol, blocked Na+ entry while K+ continued to be lost. This volume-independent K+ efflux, which is thus independent of the Na+-H+ exchanger, was not accompanied by a Cl-efflux but was associated with large internal and external pH changes consistent with K+-H+ exchange.4. The K+ loss and the related pH changes are inhibited by compounds which are known to inhibit the K+-anion co-transporter in trout red cells, i.e. 4,4'-diisothiocyanatostilbene-2,2'-disulphonic acid (Dids) and niflumic acid.

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Adrenergic Control of Red Cell pH, Organic Phosphate Concentrations and Haemoglobin Function in Teleost Fish

Nikinmaa

Boutilier

1995

Mechanisms of Systemic Regulation

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Characteristics of β-adrenergic-activated Na-proton transport in red blood cells

Cited by 15 publications

References 17 publications

Cloning and expression of a cAMP-activated Na+/H+ exchanger: evidence that the cytoplasmic domain mediates hormonal regulation.

Cloning and expression of a cAMP-activated Na+/H+ exchanger: evidence that the cytoplasmic domain mediates hormonal regulation.

Evidence for a K(+)‐H+ exchange in trout red blood cells.

Adrenergic Control of Red Cell pH, Organic Phosphate Concentrations and Haemoglobin Function in Teleost Fish

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