The Ca(2+)-transporting ATPases of Rabbit and Trout Exhibit Different PH- and Temperature-dependences

Overview

Journal Biochem J

Specialty Biochemistry

Date 1993 Jul 15

PMID 8343126

Citations 1

Authors

E N Chini

F G de Toledo

M C Albuquerque

L De Meis

Affiliations

Soon will be listed here.

Abstract

The phosphorylation of the trout sarcoplasmic-reticulum Ca(2+)-ATPase by Pi differs in its temperature- and pH-dependence from the rabbit ATPase. In the trout enzyme, the apparent affinity for Pi and maximum phosphoenzyme values do not vary over a pH and temperature ranges that have a pronounced effect on the rabbit enzyme. The lack of temperature-dependence for phosphorylation is observed at pH 6.8. At pH 8.0, the temperature profile for phosphorylation of the trout enzyme resembles that of the rabbit at pH 6.8. The rabbit ATPase is no longer phosphorylated by Pi after solubilization with the detergent C12E9. In contrast, the trout enzyme can be phosphorylated by Pi after solubilization with C12E9, and the same levels of phosphoenzyme were obtained with the soluble and membrane-bound ATPase at both 0 degrees and 25 degrees C. In the range of 0-20 degrees C, the rates of ATP synthesis and of Ca2+ uptake by the trout ATPase are less temperature-dependent than for the rabbit enzyme. However, both isoenzymes catalyse ATP hydrolysis with similar temperature-dependences. The results raise the possibility that protonation of specific amino acid residues may contribute to the lack of temperature-dependence for phosphorylation of the trout Ca(2+)-ATPase.

Citing Articles

Effects of acute warming on cardiac and myotomal sarco(endo)plasmic reticulum ATPase (SERCA) of thermally acclimated brown trout (Salmo trutta).

Vornanen M J Comp Physiol B. 2020; 191(1):43-53.

PMID: 32980918 PMC: 7819936. DOI: 10.1007/s00360-020-01313-1.

References

De Meis L, Tume R . A new mechanism by which an H+ concentration gradient drives the synthesis of adenosine triphosphate, pH jump, and adenosine triphosphate synthesis by the Ca2+-dependnet adenosine triphosphatase of sarcoplasmic reticulum. Biochemistry. 1977; 16(20):4455-63. DOI: 10.1021/bi00639a020. View

De Meis L, Inesi G . Effects of organic solvents, methylamines, and urea on the affinity for Pi of the Ca2+-ATPase of sarcoplasmic reticulum. J Biol Chem. 1988; 263(1):157-61. View

De Meis L . Approaches to studying the mechanisms of ATP synthesis in sarcoplasmic reticulum. Methods Enzymol. 1988; 157:190-206. DOI: 10.1016/0076-6879(88)57075-1. View

Inesi G, Lewis D, Murphy A . Interdependence of H+, Ca2+, and Pi (or vanadate) sites in sarcoplasmic reticulum ATPase. J Biol Chem. 1984; 259(2):996-1003. View

Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

De Meis L, Suzano V, Inesi G . Functional interactions of catalytic site and transmembrane channel in the sarcoplasmic reticulum ATPase. J Biol Chem. 1990; 265(31):18848-51. View

Champeil P, Guillain F, Venien C, Gingold M . Interaction of magnesium and inorganic phosphate with calcium-deprived sarcoplasmic reticulum adenosinetriphosphatase as reflected by organic solvent induced perturbation. Biochemistry. 1985; 24(1):69-81. DOI: 10.1021/bi00322a012. View

Gould G, Colyer J, East J, Lee A . Silver ions trigger Ca2+ release by interaction with the (Ca2+-Mg2+)-ATPase in reconstituted systems. J Biol Chem. 1987; 262(16):7676-9. View

Masuda H, De Meis L . Phosphorylation of the sarcoplasmic reticulum membrane by orthophosphate. Inhibition by calcium ions. Biochemistry. 1973; 12(23):4581-5. DOI: 10.1021/bi00747a006. View

10.

Chini E, Meyer-Fernandes J, Sola-Penna M . Monosaccharides and disaccharides decrease the Km for phosphorylation of a membrane-bound enzyme ATPase. Z Naturforsch C J Biosci. 1991; 46(7-8):644-6. DOI: 10.1515/znc-1991-7-822. View

11.

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

12.

Michelangeli F, Grimes E, East J, Lee A . Effects of phospholipids on the function of (Ca2(+)-Mg2+)-ATPase. Biochemistry. 1991; 30(2):342-51. DOI: 10.1021/bi00216a006. View

13.

De Meis L . Fast efflux of Ca2+ mediated by the sarcoplasmic reticulum Ca2(+)-ATPase. J Biol Chem. 1991; 266(9):5736-42. View

14.

Gerdes U, MOLLER J . The Ca2+ permeability of sarcoplasmic reticulum vesicles. II. Ca2+ efflux in the energized state of the calcium pump. Biochim Biophys Acta. 1983; 734(2):191-200. DOI: 10.1016/0005-2736(83)90117-7. View

15.

MAKINOSE M, Hasselbach W . ATP synthesis by the reverse of the sarcoplasmic calcium pump. FEBS Lett. 1971; 12(5):271-272. DOI: 10.1016/0014-5793(71)80196-5. View

16.

Vrbjar N, Simatos G, Keough K . Temperature dependence of kinetic parameters of (Ca2+ + Mg2+)-ATPase in rabbit and winter flounder sarcoplasmic reticulum. Biochim Biophys Acta. 1990; 1030(1):94-100. DOI: 10.1016/0005-2736(90)90243-h. View

17.

Inesi G, Millman M, Eletr S . Temperature-induced transitions of function and structure in sarcoplasmic reticulum membranes. J Mol Biol. 1973; 81(4):483-504. DOI: 10.1016/0022-2836(73)90518-4. View

18.

Masuda H, De Meis L . Effect of temperature on the Ca2+ transport ATPase of sarcoplasmic reticulum. J Biol Chem. 1977; 252(23):8567-71. View

19.

Kanazawa T . Phosphorylation of solubilized sarcoplasmic reticulum by orthophosphate and its thermodynamic characteristics. The dominant role of entropy in the phosphorylation. J Biol Chem. 1975; 250(1):113-9. View

20.

De Meis L, Martins O, Alves E . Role of water, hydrogen ion, and temperature on the synthesis of adenosine triphosphate by the sarcoplasmic reticulum adenosine triphosphatase in the absence of a calcium ion gradient. Biochemistry. 1980; 19(18):4252-61. DOI: 10.1021/bi00559a017. View