Some Properties of the Ca2+-stimulated ATPase of a Rat Liver Microsomal Fraction

Overview

Journal Biochem J

Specialty Biochemistry

Date 1983 Feb 15

PMID 6222732

Citations 12

Authors

A P Dawson

D V Fulton

Affiliations

Soon will be listed here.

Abstract

1. The heavy microsomal fraction from rat liver apparently has very little Ca2+-stimulated ATPase activity, although it has an active, ATP-driven Ca2+ accumulation system. 2. The addition of ionophore A23187 to the ATPase assay, to allow continuous Ca2+ recycling during the assay time, reveals the presence of a substantial Ca2+-stimulated ATPase with Vmax. 160 nmol of Pi/10 min per mg of protein and Km for Ca2+ 0.19 microM. 3. The Ca2+-stimulated ATPase, but not the basal Mg2+-stimulated ATPase, is potently inhibited by orthovanadate. Both the Ca2+-stimulated ATPase and the vanadate inhibition are enhanced by the presence of Mg2+. 4. Ca2+-stimulated ATPase activity is not responsive to calmodulin or the calmodulin antagonist trifluoperazine.

Citing Articles

CYP2E1 overexpression inhibits microsomal Ca2+-ATPase activity in HepG2 cells.

Caro A, Evans K, Cederbaum A Toxicology. 2008; 255(3):171-6.

PMID: 19028543 PMC: 2650832. DOI: 10.1016/j.tox.2008.10.020.

Characterization of Ca Transport in Purified Endoplasmic Reticulum Membrane Vesicles from Lepidium sativum L. Roots.

Buckhout T Plant Physiol. 1984; 76(4):962-7.

PMID: 16663981 PMC: 1064416. DOI: 10.1104/pp.76.4.962.

Effects of paraquat on Mg(2+)-ATPase activity in rat liver.

Noguchi N, Yamamoto H, Misawa S Arch Environ Contam Toxicol. 1993; 24(4):483-6.

PMID: 8507103 DOI: 10.1007/BF01146166.

A steady-state mechanism can account for the properties of inositol 2,4,5-trisphosphate-stimulated Ca2+ release from permeabilized L1210 cells.

Dawson A Biochem J. 1993; 289 ( Pt 3):861-6.

PMID: 8382056 PMC: 1132255. DOI: 10.1042/bj2890861.

A procedure for the rapid isolation from rat liver of plasma membrane vesicles exhibiting Ca2+-transport and Ca2+-ATPase activities.

Epping R, Bygrave F Biochem J. 1984; 223(3):733-45.

PMID: 6239615 PMC: 1144357. DOI: 10.1042/bj2230733.

References

Moore L, Chen T, Knapp Jr H, Landon E . Energy-dependent calcium sequestration activity in rat liver microsomes. J Biol Chem. 1975; 250(12):4562-8. View

Gopinath R, VINCENZI F . Phosphodiesterase protein activator mimics red blood cell cytoplasmic activator of (Ca2+-Mg2+)ATPase. Biochem Biophys Res Commun. 1977; 77(4):1203-9. DOI: 10.1016/s0006-291x(77)80107-1. View

Jarrett H, Penniston J . Partial purification of the Ca2+-Mg2+ ATPase activator from human erythrocytes: its similarity to the activator of 3':5' - cyclic nucleotide phosphodiesterase. Biochem Biophys Res Commun. 1977; 77(4):1210-6. DOI: 10.1016/s0006-291x(77)80108-3. View

Josephson L, Cantley Jr L . Isolation of a potent (Na-K)ATPase inhibitor from striated muscle. Biochemistry. 1977; 16(21):4572-8. DOI: 10.1021/bi00640a006. View

Bygrave F . Properties of energy-dependent calcium transport by rat liver microsomal fraction as revealed by initial-rate measurements. Biochem J. 1978; 170(1):87-91. PMC: 1183864. DOI: 10.1042/bj1700087. View

Wang T, Tsai L, Solaro R, Grassi de Gende A, Schwartz A . Effects of potassium on vanadate inhibition of sarcoplasmic reticulum Ca2+-ATPase from dog cardiac and rabbit skeletal muscle. Biochem Biophys Res Commun. 1979; 91(1):356-61. DOI: 10.1016/0006-291x(79)90626-0. View

Lam A, Hummel L, Friedmann N . Characterization of the hormone-sensitive Ca2+ uptake activity of the hepatic endoplasmic reticulum. Biochim Biophys Acta. 1980; 630(2):165-75. DOI: 10.1016/0304-4165(80)90418-3. View

Bond G, Hudgins P . Inhibition of red cell Ca2+-ATPase by vanadate. Biochim Biophys Acta. 1980; 600(3):781-90. DOI: 10.1016/0005-2736(80)90480-0. View

Caroni P, Carafoli E . The Ca2+-pumping ATPase of heart sarcolemma. Characterization, calmodulin dependence, and partial purification. J Biol Chem. 1981; 256(7):3263-70. View

10.

Carafoli E, Niggli V, Malmstrom K, Caroni P . Calmodulin in natural and reconstituted calcium transporting systems. Ann N Y Acad Sci. 1980; 356:258-66. DOI: 10.1111/j.1749-6632.1980.tb29616.x. View

11.

Lotersztajn S, Hanoune J, Pecker F . A high affinity calcium-stimulated magnesium-dependent ATPase in rat liver plasma membranes. Dependence of an endogenous protein activator distinct from calmodulin. J Biol Chem. 1981; 256(21):11209-15. View

12.

Reinhart P, Bygrave F . Glucagon stimulation of ruthenium red-insensitive calcium ion transport in developing rat liver. Biochem J. 1981; 194(2):541-9. PMC: 1162778. DOI: 10.1042/bj1940541. View

13.

Wibo M, Morel N, GODFRAIND T . Differentiation of Ca2+ pumps linked to plasma membrane and endoplasmic reticulum in the microsomal fraction from intestinal smooth muscle. Biochim Biophys Acta. 1981; 649(3):651-60. DOI: 10.1016/0005-2736(81)90170-x. View

14.

Berthon B, POGGIOLI J, Capiod T, Claret M . Effect of the alpha-agonist noradrenaline on total and 45Ca2+ movements in mitochondria of rat liver cells. Biochem J. 1981; 200(1):177-80. PMC: 1163517. DOI: 10.1042/bj2000177. View

15.

Pick U . The interaction of vanadate ions with the Ca-ATPase from sarcoplasmic reticulum. J Biol Chem. 1982; 257(11):6111-9. View

16.

Iwasa Y, Higashi K, Matsui K, Miyamoto E . Demonstration of a high affinity Ca2+ ATPase in rat liver plasma membranes. Biochem Biophys Res Commun. 1982; 105(2):488-94. DOI: 10.1016/0006-291x(82)91461-9. View

17.

Kanagasuntheram P, Teo T . Calmodulin-sensitive ATP-dependent calcium transport by the rat parotid endoplasmic reticulum. FEBS Lett. 1982; 141(2):233-6. DOI: 10.1016/0014-5793(82)80055-0. View

18.

Dawson A . Kinetic properties of the Ca2+-accumulation system of a rat liver microsomal fraction. Biochem J. 1982; 206(1):73-9. PMC: 1158551. DOI: 10.1042/bj2060073. View