Vanadate inhibition of the Ca<sup>2+</sup>‐dependent conformational change of the sarcoplasmic reticulum Ca<sup>2+</sup>‐ATPase

Dupont, Yves; Bennett, Nelly

doi:10.1016/0014-5793(82)80860-0

Cited by 70 publications

(40 citation statements)

References 18 publications

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“…This hypothesis for K ÷ or Na + exchange comes from the observation of a fast EGTA-induced K+/Na + efflux from SR vesicles, which is sensitive to the concentration of protons, calcium and vanadate, an inhibitor of P-type ATPases [11]. This kind of study using native SR vesicles is generally complicated by the existence of a number of passive permeabilities in the native membrane.…”

Section: Discussionmentioning

confidence: 99%

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Evidence for direct involvement of the sarcoplasmic reticulum Ca²⁺‐ATPase in a passive monovalent cation (K⁺/Na⁺) exchange

1995

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A specific inhibitor of SERCA-pumps, thapsigargin (TG) was used to demonstrate the direct involvement of the SR Ca2+-ATPase in passive K+/Na + exchange. The K+-potential variations across vesicle membranes were measured in the absence of ATP with a fluorescent probe: 3,3'-dipropylthiodicarbocyanine iodide. Addition of EGTA dissipates the K÷-potential whereas the presence of TG abolishes this effect. Our data prove that the CaZ+-ATPase translocates monovalent cations at a rate similar to the E2-~Et conformational change.

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Section: Discussionmentioning

confidence: 99%

“…Furthermore, a passive monovalent cation exchange (K + or Na ÷) has been observed in native SR vesicles in the absence of ATE This exchange is inhibited by vanadate and seems to be regulated by pH and the extravesicular calcium concentration [9,11 ]. Consequently the authors have postulated *Corresponding author.…”

Section: Methodsmentioning

confidence: 99%

Evidence for direct involvement of the sarcoplasmic reticulum Ca²⁺‐ATPase in a passive monovalent cation (K⁺/Na⁺) exchange

1995

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“…Vanadate and phosphate compete in a number of systems, such as the red blood cell anion exchange pathway (Cantley et al, 1978b) and the Ca-ATPase from skeletal sarcoplasmic reticulum (Dupont & Bennett, 1982). Phosphate inhibited contractions elicited by vanadate in a reversible manner but did not affect responses to ACh, suggesting a common site of action of these analogues on or within the smooth muscle cell.…”

Section: )mentioning

confidence: 99%

“…It also inhibits several phosphate hydrolysing enzymes in vitro, including Na,K-ATPase (Cantley, Josephson, Warner, Yanagisawa, Lechene & Guidotti, 1977;Cantley, Cantley & Josephson, 1978a;Cantley, Resh & Guidotti, 1978b) and Ca-ATPase (O'Neal, Rhoads & Racker, 1979;Vincenzi & Ashleman, 1980;Dupont & Bennett, 1982). The presence of vanadium in trace concentrations of 0.1-11 M in animal tissues (Underwood, 1977) has led to the i) The Macmillan Press Ltd 1983 suggestion of a regulatory role for vanadium in some of these enzyme systems.…”

Section: Introductionmentioning

confidence: 99%

Mechanism of vanadate‐induced contraction of airways smooth muscle of the guinea‐pig

Nayler

Sparrow

1983

British J Pharmacology

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The characteristics of vanadate‐induced contraction of airways smooth muscle are described in isolated preparations of guinea‐pig central and peripheral airways. Vanadate (1–1000 μM) induced sustained contractions of trachea and lung parenchymal strips within 1 min of challenge. It was more potent (P < 0.001) on the lung strip (EC50 = 63 μM) than on the trachea (EC50 =123 μM). The lung strip also developed greater maximum isometric tension (P < 0.001) than the trachea. The efficacy on the lung strip was 2 and the trachea 0.6, relative to the response to acetylcholine (efficacy = 1). Vanadate‐induced contractions of the trachea were not inhibited by atropine, mepyramine, phentolamine or indomethacin, nor after mast cell depletion by compound 48/80, showing that contractions were not mediated via specific receptors or by release of endogenous mediators of tone. Inorganic phosphate specifically inhibited vanadate responses in a dose‐dependent and reversible manner, suggesting a common site of action. Contractions could be elicited in depolarized muscle and after treatment with ouabain plus propranolol, showing that membrane depolarization and inhibition of the Na, K‐ATPase system were not involved in the contractile action of vanadate. Pretreatment of tracheal smooth muscle with verapamil had no influence on contractions elicited by vanadate. After removal of extracellular calcium, vanadate‐induced contractions declined slowly with time, indicating that influx of extracellular calcium was not giving rise to contractions elicited by vanadate. Vanadate markedly increased the rate of calcium efflux from trachealis muscle loaded with 45Ca into both Ca2+‐free and normal Krebs solutions; this is compatible with vanadate mobilizing an intracellular store of Ca2+. Such a store involving sites with Ca‐ATPase activity would be consistent with the action of vanadate in isolated membrane preparations. Membrane‐skinned tracheal fibres contracted by micromolar Ca2+ were relaxed by vanadate in a reversible dose‐related manner, indicating that the contractile action of vanadate was not related to its interaction with proteins at the cross‐bridge level.

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“…Several kinetic studies have suggested that, in the absence of ATP, orthovanadate can bind to the SR ATPase and form a transition state analog of the phosphorylated intermediate (3)(4)(5). On the other hand, decavanadate has been very useful in stabilizing bidimensional crystals of the SR ATPase (6), thereby rendering possible electron crystallographic studies (7,8).…”

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confidence: 99%

Distinct Topologies of Mono- and Decavanadate Binding and Photo-oxidative Cleavage in the Sarcoplasmic Reticulum ATPase

Hua

Inesi

Toyoshima

2000

Journal of Biological Chemistry

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Vanadate inhibition of the Ca²⁺‐dependent conformational change of the sarcoplasmic reticulum Ca²⁺‐ATPase

Cited by 70 publications

References 18 publications

Evidence for direct involvement of the sarcoplasmic reticulum Ca²⁺‐ATPase in a passive monovalent cation (K⁺/Na⁺) exchange

Evidence for direct involvement of the sarcoplasmic reticulum Ca²⁺‐ATPase in a passive monovalent cation (K⁺/Na⁺) exchange

Mechanism of vanadate‐induced contraction of airways smooth muscle of the guinea‐pig

Distinct Topologies of Mono- and Decavanadate Binding and Photo-oxidative Cleavage in the Sarcoplasmic Reticulum ATPase

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Vanadate inhibition of the Ca2+‐dependent conformational change of the sarcoplasmic reticulum Ca2+‐ATPase

Cited by 70 publications

References 18 publications

Evidence for direct involvement of the sarcoplasmic reticulum Ca2+‐ATPase in a passive monovalent cation (K+/Na+) exchange

Evidence for direct involvement of the sarcoplasmic reticulum Ca2+‐ATPase in a passive monovalent cation (K+/Na+) exchange

Mechanism of vanadate‐induced contraction of airways smooth muscle of the guinea‐pig

Distinct Topologies of Mono- and Decavanadate Binding and Photo-oxidative Cleavage in the Sarcoplasmic Reticulum ATPase

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Resources

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Vanadate inhibition of the Ca²⁺‐dependent conformational change of the sarcoplasmic reticulum Ca²⁺‐ATPase

Evidence for direct involvement of the sarcoplasmic reticulum Ca²⁺‐ATPase in a passive monovalent cation (K⁺/Na⁺) exchange

Evidence for direct involvement of the sarcoplasmic reticulum Ca²⁺‐ATPase in a passive monovalent cation (K⁺/Na⁺) exchange