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Query: UNIPROT:P20020 (
adenosine triphosphatase
)
3,299
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The effect of the calcium-binding protein
regucalcin
on the Ca2+ transport system in rat liver mitochondria was investigated. Ca2+ transport was assayed by the method of Millipore filtration to estimate mitochondrial 45Ca2+ accumulation. 45Ca2+ uptake was stimulated by the presence of
regucalcin
(1.0 and 2.0 microM). This stimulation was remarkable during 1.0 min after 45Ca2+ addition, while appreciable stimulation was no longer seen at 3 min.
Regucalcin
(2.0 microM)-induced stimulation of 45Ca2+ uptake was prevented by the presence of ruthenium red (1.0 microM) and lanthanum chloride (0.1 mM).
Regucalcin
(2.0 microM) did not increase the mitochondrial
adenosine triphosphatase
(
ATPase
) activity during 3.0 min after Ca2+ addition. Meanwhile, 45Ca2+, which accumulated in the mitochondria during 5.0 min after 45Ca2+ addition, was not released by the addition of
regucalcin
.
Regucalcin
may stimulate Ca2+ uptake in rat liver mitochondria independently of the energy.
...
PMID:Calcium-binding protein regucalcin stimulates the uptake of Ca2+ by rat liver mitochondria. 204 6
The effect of
regucalcin
, a calcium-binding protein isolated from rat liver cytosol, on Ca2+-
adenosine triphosphatase
(
ATPase
) activity in hepatic microsomes was investigated. Mg2+-ATPase activity was clearly increased by the presence of 50 microM Ca2+.
Regucalcin
(1.0-4.0 microM) caused a remarkable elevation (about 3-fold) of Ca2+-ATPase activity. Also, Mg2+-ATPase activity was increased (about 1.6-fold) by the presence of
regucalcin
(2.0 and 4.0 microM). Guanosine-5'-O-(3-thiotriphosphate) (GTPrs; 10(-5) and 10(-4) M) and nicotinamide adenine dinucleotide phosphate oxidized form (NADP+; 10(-5) to 10(-3) M) or reduced form (NADPH; 10(-4) and 10(-3) M) significantly increased Ca2+-ATPase activity. These increases were not enhanced by the presence of
regucalcin
(2.0 microM). Of various metal ions, a comparatively low concentration of V5+ (10(-5) M) or Cd2+ (10(-6) M) significantly increased Ca2+-ATPase activity, while Hg2+, Zn2+, Cu2+ and Mn2+ did not have such an effect.
Regucalcin
(2.0 microM) did not enhance the effect of V5+ and Cd2+ on Ca2+-ATPase activity. The present finding, that
regucalcin
activates hepatic microsomal Ca2+-ATPase, suggests a cell physiological role of
regucalcin
as an activator in the microsomal Ca2+-pump activity. This action of
regucalcin
may not be influenced by other regulators.
...
PMID:Activation of hepatic microsomal Ca2+-adenosine triphosphatase by calcium-binding protein regucalcin. 252 22
