Stimulation of Ca2+ Efflux from Sarcoplasmic Reticulum by Preincubation with ATP and Inorganic Phosphate

Overview

Journal Biochem J

Specialty Biochemistry

Date 1987 Nov 1

PMID 2962569

Citations 7

Authors

V Shoshan-Barmatz

Affiliations

Soon will be listed here.

Abstract

Preincubation of sarcoplasmic reticulum with 1 mM-ATP completely inhibits Ca2+ accumulation and stimulates ATPase activity by over 2-fold. This effect of ATP is obtained only when the preincubation is carried out in the presence of Pi, but not with arsenate, chloride or sulphate. The inhibition by ATP of Ca2+ accumulation is pH-dependent, increasing as the pH is increased above 7.5. Inhibition of Ca2+ accumulation is observed on preincubation with ATP, but not with CTP, UTP, GTP, ADP, adenosine 5'-[beta gamma-methylene]triphosphate or adenosine 5'-[beta gamma-imido]triphosphate. The presence of Ca2+, but not Mg2+, during the preincubation, prevents the effect of ATP + Pi on Ca2+ accumulation. The ATP + Pi inhibition of Ca2+ accumulation is not due to modification of the ATPase catalytic cycle, but rather to stimulation of a rapid Ca2+ efflux from actively or passively loaded vesicles. This Ca2+ efflux is inhibited by dicyclohexylcarbodi-imide. Photoaffinity labelling of sarcoplasmic-reticulum membranes with 8-azido-[alpha-32P]ATP resulted in specific labelling of two proteins, of approx. 160 and 44 kDa. These proteins were labelled in the presence of Pi, but not other anions.

Citing Articles

Chemical modification of an arginine residue in the ATP-binding site of Ca2+ -transporting ATPase of sarcoplasmic reticulum by phenylglyoxal.

Yamamoto H, Kawakita M Mol Cell Biochem. 1999; 190(1-2):169-77.

PMID: 10098984

ATP-dependent interaction of propranolol and local anaesthetic with sarcoplasmic reticulum. Stimulation of Ca2+ efflux.

Shoshan-Barmatz V Biochem J. 1988; 256(3):733-9.

PMID: 2975944 PMC: 1135477. DOI: 10.1042/bj2560733.

Activation of Ca2+ release in isolated sarcoplasmic reticulum.

Shoshan-Barmatz V J Membr Biol. 1988; 103(1):67-77.

PMID: 2846845 DOI: 10.1007/BF01871933.

Antibodies to junctional sarcoplasmic reticulum proteins: probes for the Ca2+-release channel.

Zorzato F, Chu A, Volpe P Biochem J. 1989; 261(3):863-70.

PMID: 2552993 PMC: 1138910. DOI: 10.1042/bj2610863.

Involvement of protein phosphorylation in activation of Ca2+ efflux from sarcoplasmic reticulum.

Gechtman Z, ORR I, Shoshan-Barmatz V Biochem J. 1991; 276 ( Pt 1):97-102.

PMID: 2039485 PMC: 1151148. DOI: 10.1042/bj2760097.

References

MAKINOSE M, The R . [Calcium accumulation and cleavage of nucleoside triphosphate cleavage by vesicles of sacroplasmic reticulum]. Biochem Z. 1965; 343(4):383-93. View

Shoshan V, Maclennan D, Wood D . Tetraphenylboron causes Ca2+ release in isolated sarcoplasmic reticulum and in skinned muscle fibers. J Biol Chem. 1983; 258(5):2837-42. View

RACKER E . Reconstitution of a calcium pump with phospholipids and a purified Ca ++ - adenosine triphosphatase from sacroplasmic reticulum. J Biol Chem. 1972; 247(24):8198-200. View

Ebashi S . Excitation-contraction coupling. Annu Rev Physiol. 1976; 38:293-313. DOI: 10.1146/annurev.ph.38.030176.001453. View

Ogawa Y, Ebashi S . Ca-releasing action of beta, gamma-methylene adenosine triphosphate on fragmented sarcoplasmic reticulum. J Biochem. 1976; 80(5):1149-57. DOI: 10.1093/oxfordjournals.jbchem.a131370. View

Endo M . Calcium release from the sarcoplasmic reticulum. Physiol Rev. 1977; 57(1):71-108. DOI: 10.1152/physrev.1977.57.1.71. View

PENEFSKY H . Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase. J Biol Chem. 1977; 252(9):2891-9. View

Millman M, Azari J . Adenosine triphosphate-induced rapid calcium release from fragmented sarcoplasmic reticulum. Biochem Biophys Res Commun. 1977; 78(1):60-6. DOI: 10.1016/0006-291x(77)91221-9. View

Tada M, Yamamoto T, Tonomura Y . Molecular mechanism of active calcium transport by sarcoplasmic reticulum. Physiol Rev. 1978; 58(1):1-79. DOI: 10.1152/physrev.1978.58.1.1. View

10.

De Meis L, Vianna A . Energy interconversion by the Ca2+-dependent ATPase of the sarcoplasmic reticulum. Annu Rev Biochem. 1979; 48:275-92. DOI: 10.1146/annurev.bi.48.070179.001423. View

11.

Ohnishi S . Calcium-induced calcium release from fragmented sarcoplasmic reticulum. J Biochem. 1979; 86(4):1147-50. DOI: 10.1093/oxfordjournals.jbchem.a132609. View

12.

Varsanyi M, Heilmeyer Jr L . Ca2+ regulation of sarcoplasmic reticular protein phosphatase activity. Biochemistry. 1979; 18(22):4869-75. DOI: 10.1021/bi00589a015. View

13.

Shoshan V, Maclennan D . Quercetin interaction with the (Ca2+ + Mg2+)-ATPase of sarcoplasmic reticulum. J Biol Chem. 1981; 256(2):887-92. View

14.

Campbell K, Shamoo A . Phosphorylation of heavy sarcoplasmic reticulum vesicles: identification and characterization of three phosphorylated proteins. J Membr Biol. 1980; 56(3):241-8. DOI: 10.1007/BF01869479. View

15.

Pick U, Karlish S . Indications for an oligomeric structure and for conformational changes in sarcoplasmic reticulum Ca2+-ATPase labelled selectively with fluorescein. Biochim Biophys Acta. 1980; 626(1):255-61. DOI: 10.1016/0005-2795(80)90216-0. View

16.

Campbell K, Maclennan D . Purification and characterization of the 53,000-dalton glycoprotein from the sarcoplasmic reticulum. J Biol Chem. 1981; 256(9):4626-32. View

17.

Shoshan V, Maclennan D, Wood D . A proton gradient controls a calcium-release channel in sarcoplasmic reticulum. Proc Natl Acad Sci U S A. 1981; 78(8):4828-32. PMC: 320264. DOI: 10.1073/pnas.78.8.4828. View

18.

Nagasaki K, Kasai M . Calcium-induced calcium release from sarcoplasmic reticulum vesicles. J Biochem. 1981; 90(3):749-55. DOI: 10.1093/oxfordjournals.jbchem.a133529. View

19.

Ikemoto N . Structure and function of the calcium pump protein of sarcoplasmic reticulum. Annu Rev Physiol. 1982; 44:297-317. DOI: 10.1146/annurev.ph.44.030182.001501. View

20.

Chiesi M, Wen Y . A phosphorylated conformational state of the (Ca2+-Mg2+)-ATPase of fast skeletal muscle sarcoplasmic reticulum can mediate rapid Ca2+ release. J Biol Chem. 1983; 258(10):6078-85. View