Regulation of the Phosphorylation of Calpain II and Its Inhibitor

Overview

Journal Mol Cell Biochem

Publisher Springer

Specialty Biochemistry

Date 1994 Jul 27

PMID 7845369

Citations 3

Authors

W N Kuo

U Ganesan

D L Davis

D L Walbey

Affiliations

Soon will be listed here.

Abstract

Phosphorylation of calpain II (or its inhibitor) by the catalytic subunit of cyclic AMP-dependent protein kinase (A-PK), cyclic GMP-dependent protein kinase (G-PK), and protein kinase C (PK-C) was analyzed by SDS-polyacrylamide gel electrophoresis and autoradiography. Among these protein kinases, the catalytic subunit of A-PK exhibited the strongest phosphorylations of both calpain II and its inhibitor. Arachidonic acid and staurosporine effectively inhibited phosphorylation regardless the type of kinase tested. Despite its lack of effect on the phosphorylation of calpain II by the catalytic subunit of A-PK, sphingosine moderately enhanced the phosphorylation of calpain II by G-PK. Other agents, including phosphatidylethanolamine, phosphatidylinositol and 1, 2-dioleoyl-sn-glycerol, had no significant effect.

Citing Articles

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Activation of m-calpain (calpain II) by epidermal growth factor is limited by protein kinase A phosphorylation of m-calpain.

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Protein nitration.

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References

Nakamura M, Inomata M, Hayashi M, Imahori K, Kawashima S . Purification and characterization of an inhibitor of calcium-activated neutral protease from rabbit skeletal muscle: purification of 50,000-dalton inhibitor. J Biochem. 1984; 96(5):1399-407. DOI: 10.1093/oxfordjournals.jbchem.a134968. 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

Hathaway D, Werth D, Haeberle J . Limited autolysis reduces the Ca2+ requirement of a smooth muscle Ca2+-activated protease. J Biol Chem. 1982; 257(15):9072-7. View

Tsujinaka T, Ariyoshi H, Uemura Y, Sakon M, Kambayashi J, Mori T . Potential participation of calpain in platelet activation studied by use of a cell penetrating calpain inhibitor (calpeptin). Life Sci. 1990; 46(15):1059-66. DOI: 10.1016/0024-3205(90)90414-m. View

Kuo J, Kuo W, Shoji M, Davis C, Seery V, Donnelly Jr T . Purification and general properties of guanosine 3':5'-monophosphate-dependent protein kinase from guinea pig fetal lung. J Biol Chem. 1976; 251(6):1759-66. View

Nishiura I, Tanaka K, Yamato S, Murachi T . The occurrence of an inhibitor of Ca2+-dependent neutral protease in rat liver. J Biochem. 1978; 84(6):1657-9. DOI: 10.1093/oxfordjournals.jbchem.a132296. View

Hincke M, Tolnai S . Phosphorylation of bovine cardiac calcium-activated neutral protease by protein kinase-C. Biochem Biophys Res Commun. 1986; 137(1):559-65. DOI: 10.1016/0006-291x(86)91247-7. View

Zimmerman U, SCHLAEPFER W . Kinase activities associated with calcium-activated neutral proteases. Biochem Biophys Res Commun. 1984; 120(3):767-74. DOI: 10.1016/s0006-291x(84)80173-4. View

NISHIZUKA Y . Turnover of inositol phospholipids and signal transduction. Science. 1984; 225(4668):1365-70. DOI: 10.1126/science.6147898. View

10.

Corbin J, Brostrom C, King C, KREBS E . Studies on the adenosine 3',5'-monophosphate-dependent protein kinases of rabbit skeletal muscle. J Biol Chem. 1972; 247(23):7790-8. View

11.

Hannun Y, Bell R . Rat brain protein kinase C. Kinetic analysis of substrate dependence, allosteric regulation, and autophosphorylation. J Biol Chem. 1990; 265(5):2962-72. View

12.

Kawashima S, Nomoto M, Hayashi M, Inomata M, Nakamura M, Imahori K . Comparison of calcium-activated neutral proteases from skeletal muscle of rabbit and chicken. J Biochem. 1984; 95(1):95-101. DOI: 10.1093/oxfordjournals.jbchem.a134608. View

13.

Beer D, Butley M, Malkinson A . Developmental changes in the endogenous Ca2+-stimulated proteolysis of mouse lung cAMP-dependent protein kinases. Arch Biochem Biophys. 1984; 228(1):207-19. DOI: 10.1016/0003-9861(84)90062-6. View

14.

Kuo J, Krueger B, Sanes J, Greengard P . Cyclic nucleotide-dependent protein kinases. V. Preparation and properties of adenosine 3',5'-monophosphate-dependent protein kinase from various bovine tissues. Biochim Biophys Acta. 1970; 212(1):79-91. DOI: 10.1016/0005-2744(70)90180-4. View

15.

Melloni E, Salamino F, Sparatore B, Michetti M, Pontremoli S, HORECKER B . Regulation of the Ca2+-dependent neutral proteinases from rabbit liver by an endogenous inhibitor. Arch Biochem Biophys. 1984; 232(2):513-9. DOI: 10.1016/0003-9861(84)90568-x. View

16.

Kikkawa U, Takai Y, Minakuchi R, Inohara S, NISHIZUKA Y . Calcium-activated, phospholipid-dependent protein kinase from rat brain. Subcellular distribution, purification, and properties. J Biol Chem. 1982; 257(22):13341-8. View

17.

Greengard P . Phosphorylated proteins as physiological effectors. Science. 1978; 199(4325):146-52. DOI: 10.1126/science.22932. View

18.

Waxman L, KREBS E . Identification of two protease inhibitors from bovine cardiac muscle. J Biol Chem. 1978; 253(17):5888-91. View

19.

NISHIZUKA Y . Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science. 1992; 258(5082):607-14. DOI: 10.1126/science.1411571. View

20.

Kuo W, Ganesan U, Walbey D, Davis D, Allen K, McCall L . Modulation of the activity of calpain II by phosphorylation--changes in the proteolysis of cyclic AMP-dependent protein kinase (peak II, DEAE). Appl Theor Electrophor. 1993; 3(6):317-20. View