Ca2+ transport mediated by a synthetic neutral Ca2+-ionophore in biological membranes

Caroni, Pierenrico; Gazzotti, Paolo; Vuilleumier, Paul; Simon, W.; Carafoli, Ernesto

doi:10.1016/0005-2736(77)90134-1

Cited by 31 publications

(10 citation statements)

References 19 publications

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“…Anti-IgE antibody-dependent stimulation is known to induce influx of extracellular calcium in a voltage-dependent manner by increasing the permeability of the cell membrane [27,44]. On the other hand, calcium ionophore A23187 forms a neutral complex with the calcium ion and promotes transmembrane translocation driven by a concentration gradient of calcium [28]. On the other hand, calcium ionophore A23187 forms a neutral complex with the calcium ion and promotes transmembrane translocation driven by a concentration gradient of calcium [28].…”

Section: Discussionmentioning

confidence: 99%

Inhibitory effect of 1α,25-dihydroxyvitamin D3 on mast cell proliferation and A23187-induced histamine release, also accompanied by a decreased c-kit receptor

et al. 1996

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Using mouse peritoneal mast cells, we investigated the effects of 1 alpha,25-dihydroxyvitamin D3 (calcitriol) on mast cell proliferation and histamine release. Calcitriol did not affect IL-3/IL-4-dependent mast cell proliferation, but it selectively inhibited stem cell factor-dependent mast cell proliferation and colony formation. Immunohistochemical and immunoblot analyses revealed that calcitriol treatment reduced expression of purified peritoneal mast cell c-kit protein. Using a mast cell line, MC/9, both c-kit protein and c-kit mRNA transcript were seen to be reduced following calcitriol treatment. Calcitriol also reduced histamine release induced by calcium ionophore A23187. In contrast, anti-IgE antibody-dependent histamine release was not affected by calcitriol. Our results indicate that calcitriol inhibits mast cell proliferation and A23187-induced histamine release that might be associated with a decreased expression of c-kit receptor.

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Section: Discussionmentioning

confidence: 99%

Inhibitory effect of 1α,25-dihydroxyvitamin D3 on mast cell proliferation and A23187-induced histamine release, also accompanied by a decreased c-kit receptor

et al. 1996

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“…The substantial decrease in Ca2+ uptake by brush-border vesicles in the presence of the hexavalent cation, Ruthenium Red, may have been due to an accumulation of positive charges on the external surface of the membrane, or to a specific interaction with Ca2+ binding or transporting sites (Caroni et al, 1977). In rat liver mitochondria, Ruthenium Red reacts specifically with mucopolysaccharides, mucoproteins or muco-or glyco-lipids (Moore & Korey, 1971).…”

Section: Discussionmentioning

confidence: 99%

Calcium uptake in isolated brush-border vesicles from rat small intestine

Miller¹,

Bronner²

1981

Biochemical Journal

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Ca2+ uptake in brush-border vesicles isolated from rat duodena was studied by a rapid-filtration technique. Ca2+ uptake showed saturation kinetics, was dependent on the pH and ionic strength of the medium and was independent of metabolic energy. Uptake activity was readily inhibited by Ruthenium Red, La3+, tetracaine, EGTA, choline chloride and Na+ or K+. The effect of variations in medium osmolarity on Ca2+ uptake and the ionophore A23 187-induced efflux of the cation from preloaded vesicles indicated that the Ca2+-uptake process involved binding to membrane components, as well as transport into an osmotically active space. Scatchard-plot analyses of the binding data suggested at least two classes of Ca2+-binding sites. The high-affinity sites, Ka = (2.7 + 1.1) x 104M-1 (mean + S.D.) bound 3.2 + 0.8 nmol of Ca2+/mg of protein, whereas the low-affinity sites (Ka = 60 ± 6 mF1) bound 1 10 + 17 nmol of Ca2+/mg of protein. In the presence of l10mM-NaCl, 1.7 and 53nmol of Ca2+/mg of protein were bound to the high-and low-affinity sites respectively. Decreased Ca2+-uptake activity was observed in vesicles isolated from vitamin D-deficient as compared with vitamin D-replete animals and intraperitoneal administration of 1,25-dihydroxycholecalciferol to vitamin D-deficient rats 16h before membrane isolation stimulated the initial rate of Ca2+ uptake significantly. The data indicated that Ca2+ entry and/or binding was passive and may involve a carrier-mediated Ca2+-uptake component that is associated with the brush-border membrane. Altering the electrochemical potential difference across the membrane by using anions of various permeability and selected ionophores appeared to increase primarily binding to the membrane rather than transport into the intravesicular space. Since there is considerable binding of Ca2+ to the vesicle interior, a comprehensive analysis of the transport remains difficult at present.

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“…These circumstances complicate the interpretation of earlier studies that reported the absence of an obvious permeability transition in yMt exposed to Ca 2ϩ (20,21). We used the electrophoretic Ca 2ϩ ionophore ETH129 (34,35) to determine if high internal Ca 2ϩ loads trigger a permeability transition in yMt. A typical experiment is shown in Fig.…”

Section: Camentioning

confidence: 95%

Properties of a Cyclosporin-insensitive Permeability Transition Pore in Yeast Mitochondria

Jung

Bradshaw

Pfeiffer

1997

Journal of Biological Chemistry

127

123

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Yeast mitochondria (Saccharomyces cerevisiae) contain a permeability transition pore which is regulated differently than the pore in mammalian mitochondria. In a mannitol medium containing 10 mM P i and ethanol (oxidizable substrate), yeast mitochondria accumulate large amounts of Ca 2؉ (>400 nmol/mg of protein) upon the addition of an electrophoretic Ca 2؉ ionophore (ETH129). Pore opening does not occur following Ca 2؉ uptake, even though ruthenium red-inhibited rat liver mitochondria undergo rapid pore opening under analogous conditions. However, a pore does arise in yeast mitochondria when Ca 2؉ and P i are not present, as monitored by swelling, ultrastructure, and matrix solute release. Pore opening is slow unless a respiratory substrate is provided (ethanol or NADH) but also occurs rapidly in response to ATP (2 mM) when oligomycin is present. P i and ADP inhibit pore opening (EC 50 ϳ1 and 4 mM, respectively), however, cyclosporin A (7 g/ml), oligomycin (20 g/ml), or carboxyatractyloside (25 M) have no effect. The pore arising during respiration is also inhibited by nigericin or uncoupler, indicating that an acidic matrix pH antagonizes the process. P i also inhibits pore opening by lowering the matrix pH (P i / OH ؊ antiport). However, inhibition of the ATP-induced pore by P i is seen in the presence of mersalyl, suggesting a second mechanism of action. Since pore induction by ATP is not sensitive to carboxyatractyloside, ATP appears to act at an external site and P i may antagonize the interaction. Isoosmotic polyethylene glycol-induced contraction of yeast mitochondria swollen during respiration, or in the presence of ATP, is 50% effective at a solute size of 1.0 -1.1 kDa. This suggests that the same pore is induced in both cases and is comparable in size with the permeability transition pore of heart and liver mitochondria.

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Ca2+ transport mediated by a synthetic neutral Ca2+-ionophore in biological membranes

Cited by 31 publications

References 19 publications

Inhibitory effect of 1α,25-dihydroxyvitamin D3 on mast cell proliferation and A23187-induced histamine release, also accompanied by a decreased c-kit receptor

Inhibitory effect of 1α,25-dihydroxyvitamin D3 on mast cell proliferation and A23187-induced histamine release, also accompanied by a decreased c-kit receptor

Calcium uptake in isolated brush-border vesicles from rat small intestine

Properties of a Cyclosporin-insensitive Permeability Transition Pore in Yeast Mitochondria

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