Identification of μ-, m-Calpains and Calpastatin and capture of μ- calpain activation in endothelial cells

Journal of Cellular Biochemistry

Volumn 66, Issue 2, 1997, Pages 197-209

  Fujitani, Kazumasa ^a   Kambayashi, Jun Ichi ^a   Sakon, Masato ^a   Ohmi, Shinobu I ^b   Kawashima, Sei Ichi ^c   Yukawa, Masao ^a   Yano, Yoshiko ^a   Miyoshi, Hideyuki ^a   Ikeda, Masataka ^a   Shinoki, Nobutoshi ^a   Monden, Morito ^a  

^a OSAKA UNIVERSITY MEDICAL SCHOOL   (Japan)

^b THE UNIVERSITY OF TOKYO   (Japan)

^c TOKYO METROPOLITAN INSTITUTE OF MEDICAL SCIENCE   (Japan)

Author keywords

calpain; calpain activation in endothelial cells; Autolytic intermediate form of calpain; Calpeptin; Cytoskeletal proteolysis; Filamin; Fully autolyzed postautolysis form of calpain; M calpain; Talin

Indexed keywords

CALCIMYCIN; CALCIUM; CALPAIN; CALPASTATIN; CALPEPTIN; CYTOSKELETON PROTEIN; MESSENGER RNA;

ARTICLE; CONTROLLED STUDY; CYTOSKELETON; ENDOTHELIUM CELL; ENZYME ACTIVATION; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN DEGRADATION; UMBILICAL VEIN;

ANTIBODY SPECIFICITY; BLOTTING, WESTERN; CALCIMYCIN; CALCIUM; CALCIUM-BINDING PROTEINS; CALPAIN; CELLS, CULTURED; CHROMATOGRAPHY, DEAE-CELLULOSE; CYTOSKELETAL PROTEINS; DIPEPTIDES; ENDOTHELIUM, VASCULAR; ENZYME ACTIVATION; ENZYME PRECURSORS; EXTRACELLULAR SPACE; HUMANS; HYDROLYSIS; RNA, MESSENGER; UMBILICAL VEINS;

EID: 0030811551     PISSN: 07302312     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4644(19970801)66:2<197::AID-JCB7>3.0.CO;2-L     Document Type: Article

References (71)

1. 2+-activated neutral protease (μCANP) deduced from its cDNA sequence. FEBS Lett 205:313-317.
2. Ariyoshi H, Shiba E, Kambayashi J, Sakon M, Tsujinaka T, Uemura Y, Mori T (1991): Characteristics of various synthetic peptide calpain inhibitors and their application for the analysis of platelet reaction. Biochem Int 23:1019-1033.
3. Ariyoshi H, Shiba E, Sakon M, Kambayashi J, Yoshida K, Kawashima S, Mori T (1993): Translocation of human platelet calpain-I. Biochem Mol Biol Int 30:63-72.
4. 2+ homeostasis in Ehrlich and Yoshida carcinomas. J Biol Chem 260:2719-2727.
5. Asada K, Ishino Y, Shimada M, Shimojo T, Endo M, Kimizuka F, Kato I, Maki M, Hatanaka M, Murachi T (1989): cDNA cloning of human calpastatin: Sequence homology among human, pig, and rabbit calpastatins. J Enz Inhibition 3:49-56.
6. Beckerle MC, Halloran TO, Burridge K (1986): Demonstration of a relationship between talin and P235, a major substrate of the calcium-dependent protease in platelets. J Cell Biochem 30:259-270.
7. Beckerle MC, Burridge K, DeMartino GN, Croall DE (1987): Colocalization of calcium-dependent protease II and one of its substrates at sites of cell adhesion. Cell 51:569-577.
8. 2+-stimulated proteolysis of mouse lung cAMP-dependent protein kinases. Arch Biochem Biophys 228:207-219.
9. Bradford MM (1976): A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
10. Bronk SF, Gores GJ (1993): pH-dependent nonlysosomal proteolysis contributes to lethal anoxic injury of rat hepatocytes. Am J Physiol 264:G744-G751.
11. Burridge K, Fath K, Kelly T, Nuckolls G, Turner C (1988): Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton. Ann Rev Cell Biol 4:487-525.
12. Cassel D, Glaser L (1982): Proteolytic cleavage of epidermal growth factor receptor. J Biol Chem 257:9845-9848.
13. Covault J, Liu QY, El-Deeb S (1991): Calcium-activated proteolysis of intracellular domains in the cell adhesion molecules NCAM and N-cadherin. Mol Brain Res 11: 11-16.
14. 2+ -dependent thiol protease. Eur J Biochem 155:409-413.
15. Garcia JGN, Birnboim AS, Bizios R, Del Vecchio PJ, Fenton JW, Malik AB (1986): Thrombin-induced increase in albumin permeability across the endothelium. J Cell Physiol 128:96-104.
16. 2+ and proteolysis in lethal oxidative injury in endothelial cells. Am J Physiol 261:C889-C896.
17. Giancotti FG, Stepp MN, Suzuki S, Engvall E, Ruoslahti E (1992): Proteolytic processing of endogeneous and recombinant β4integrin subunit. J Cell Biol 118:951-959.
18. Harafuji H, Ogawa Y (1980): Re-examination of the apparent binding constant of ethylene glycol bis (β-aminoetyl ether)-N,N,N′,N′-tetraacetic acid with calcium around neutral pH. J Biochem 87:1305-1312.
19. Hayashi M, Kasai Y, Kawashima S (1987): Preferential localization of calcium-activated neutral protease in epithelial tissues. Biochem Biophys Res Commun 148:567-574.
20. 2+-activated neutral protease. Biochemistry 27:8122-8128.
21. Inomata M, Kasai Y, Nakamura M, Kawashima S (1988): Activation mechanism of calcium-activated neutral protease. J Biol Chem 263:19783-19787.
22. Inomata M, Hayashi M, Nakamura M, Saito Y, Kawashima S (1989): Properties of erythrocyte membrane binding and autolytic activation of calcium-activated neutral protease. J Biol Chem 264:18838-18843.
23. Kambayashi J, Sakon M (1989): Calcium-dependent proteases and their inhibitors in human platelets. In Hawiger J (ed): "Methods in Enzymology." San Diego: Academic Press, vol. 169, pp 442-454.
24. Kasai Y, Inomata M, Hayashi M, Imahori K, Kawashima S (1986): Isolation and characterization of monoclonal antibodies against calcium-activated neutral protease with low calcium sensitivity. J Biochem 100:183-190.
25. Kawashima S, Hayashi M, Saito Y, Kasai Y, Imahori K (1988): Tissue distribution of calcium-activated neutral proteinases in rat. Biochim Biophys Acta 965:130-135.
26. Kikuchi H, Imajoh-Ohmi S (1995a): Activation and possible involvement of calpain, a calcium-activated cysteine protease, in down-regulation of apoptosis of human monoblast U937 cells. Cell Death Differ 2:195-199.
27. Kikuchi H, Imajoh-Ohmi S (1995b): Antibodies specific for proteolyzed forms of protein kinase Cα. Biochim Biophys Acta 1269:253-259.
28. Kikuchi H, Imajoh-Ohmi S, Kanegasaki S (1993): Novel antibodies specific for proteolyzed forms of protein kinase C: Production of anti-peptide antibodies available for in situ analysis of intracellular limited proteolysis. Biochim Biophys Acta 1162:171-176.
29. King LE Jr., Gates RE (1985): Calcium-activated neutral protease purified from beef lung: Properties and use in defining structure of epidermal growth factor receptors. Arch Biochem Biophys 242:146-156.
30. Kishimoto A, Kajikawa N, Shiota M, Nishizuka Y (1983): Proteolytic activation of calcium-activated, phospholipid-dependent protein kinase by calcium-dependent neutral protease. J Biol Chem 258:1156-1164.
31. Kishimoto A, Mikawa K, Hashimoto K, Yasuda I, Tanaka S, Tominaga M, Kuroda T, Nishizuka Y (1989): Limited proteolysis of protein kinase C subspecies by calcium-dependent neutral protease (calpain). J Biol Chem 264: 4088-4092.
32. Laemmli UK (1970): Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
33. Lee KS, Frank S, Vanderklish P, Arai A, Lynch G (1991): Inhibition of proteolysis protects hippocampal neurons from ischemia. Proc Natl Acad Sci USA 88:7233-7237.
34. Low MG, Carroll RC, Weglicki WB (1984): Multiple forms of phosphoinositide-specific phospholipase C of different relative molecular masses in animal tissues. Biochem J 221:813-820.
35. Lynch JJ, Ferro TJ, Blumenstock FA, Brockenauer AM, Malik AB (1990): Increased endothelial albumin permeability mediated by protein kinase C activation. J Clin Invest 85:1991-1998.
36. McCord JM (1985): Oxygen-derived free radicals in postischemic tissue injury. N Engl J Med 312:159-163.
37. Mellgren RL, Song K, Mericle MT (1993): m-Calpain requires DNA for activity on nuclear proteins at low calcium concentrations. J Biol Chem 268:653-657.
38. Murachi T (1983a): Calpain and calpastatin. Trends Biochem Sci 8:167-169.
39. 2+ protease and its inhibitor protein: Calpain and calpastatin. In Cheung WY (ed): "Calcium and Cell Function." New York: Academic Press, vol 4, pp 377-410.
40. Murachi T (1989): Intracellular regulatory system involving calpain and calpastatin. Biochem Int 18:263-294.
41. Nagao S, Saido TC, Akita Y, Tsuchiya T, Suzuki K, Kawashima S (1994): Calpain-calpastatin interactions in epidermoid carcinoma KB cells. J Biochem 115:1178-1184.
42. Nakamura M, Inomata M, Hayashi M, Imahori K, Kawashima S (1984): Purification and characterization of an inhibitor of calcium-activated neutral protease from rabbit skeletal muscle: Purification of 50,000-dalton inhibitor. J Biochem 96:1399-1407.
43. Nakamura M, Inomata M, Hayashi M, Imahori K, Kawashima S (1985): Purification and characterization of 210,000-dalton inhibitor of calcium-activated neutral protease from rabbit skeletal muscle and its relation to 50,000-dalton inhibitor. J Biochem 98:757-765.
44. 2+ -requiring forms of calcium-activated neutral proteases. Biochemistry 28:449-455.
45. Oda A, Druker BJ, Ariyoshi H, Smith M, Salzman EW (1993): pp60src is an endogenous substrate for calpain in human platelets. J Biol Chem 268:12603-12608.
46. Phillips PG, Tsan MF (1988): Hyperoxia causes increased albumin permeability of cultured endothelial monolayers. J Appl Physiol 64:1196-1202.
47. Remold-O'Donnell E, Brooklyn JV, Kenney DM (1992): Effect of platelet calpain on normal T-lymphocyte CD43: hypothesis of events in the Wiskott-Aldrich syndrome. Blood 79:1754-1762.
48. Rodgers GM, Cong J, Goll DE, Kane WH (1987): Activation of coagulation factor V by calcium-dependent proteinase. Biochim Biophys Acta 929:263-270.
49. Rotrosen D, Gallin JI (1986): Histamine type I receptor occupancy increases endothelial cytosolic calcium, reduces F-actin, and promotes albumin diffusion across cultured endothelial monolayers. J Cell Biol 103:2379-2387.
50. Saido TC, Shibata M, Takenawa T, Murofushi H, Suzuki K (1992a): Positive regulation of μ-calpain action by polyphosphoinositides. J Biol Chem 267:24585-24590.
51. Saido TC, Nagao S, Shiramine M, Tsukaguchi M, Sorimachi H, Murofushi H, Tsuchiya T, Ito H, Suzuki K (1992b): Autolytic transition of μ-calpain upon activation as resolved by antibodies distinguishing between the pre-and post-autolysis forms. J Biochem 111:81-86.
52. Saido TC, Suzuki H, Yamazaki H, Tanoue K, Suzuki K (1993a): In situ capture of μ-calpain activation in platelets. J Biol Chem 268:7422-7426.
53. Saido TC, Yokota M, Nagao S, Yamaura I, Tani E, Tsuchiya T, Suzuki K, Kawashima S (1993b): Spatial resolution of fodrin proteolysis in postischemic brain. J Biol Chem 268:25239-25243.
54. Sambrook J, Fritsch EF, Maniatis T (1989): Northern Hybridization. In Ford N, Nolan C, Ferguson M (eds): "Molecular Cloning." New York: Cold Spring Harbor Laboratory Press, pp 7.39-7.52.
55. Shasby DM, Lind SE, Shasby SS, Goldsmith JC, Hunninghake, KW (1985): Reversible oxidant-induced increases in albumin transfer across cultured endothelium: Alterations in cell shape and calcium hemostasis. Blood 65: 605-614.
56. Sheppard A, Wu J, Rutishauser U, Lynch G (1991): Proteolytic modification of neural cell adhesion molecule (NCAM) by the intracellular proteinase calpain. Biochim Biophys Acta 1076:156-160.
57. Stasek JE, Garcia JGN (1992): The role of protein kinase C in α-thrombin-mediated endothelial cell activation. Semin Thromb Hemost 18:117-125.
58. 2+-activated protease. In Ebashi S, Endo M, Imahori K, Kakiuchi S, Nishizuka Y (eds): "Calcium Regulation in Biological Systems." New York: Academic Press, pp 213-226.
59. Suzuki K, Imajoh S, Emori Y, Kawasaki H, Minami Y, Ohno S (1987): Calcium-activated neutral protease and its endogenous inhibitor. FEBS Lett 220:271-277.
60. Takano E, Kitahara A, Sasaki T, Kannagi R, Murachi T (1986): Two different molecular species of pig calpastatin. Biochem J 235:97-102.
61. Tolnai S, Korecky B (1986): Calcium-dependent proteolysis and its inhibition in the ischemic rat myocardium. Can J Cardiol 2:42-47.
62. Towbin H, Staehelin T, Gordon J (1979): Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci USA 76:4350-4354.
63. Truglia JA, Stracher A (1981): Purification and characterization of a calcium dependent sulfhydryl protease from human platelets. Biochem Biophys Res Commun 100: 814-822.
64. Tsujinaka T, Kajiwara Y, Kambayashi J, Sakon M, Mori T (1988a): Studies on myosin light chain phosphorylation in intact platelets, utilizing a cell-penetrating thiol protease inhibitor. Thromb Res 51:365-372.
65. Tsujinaka T, Kajiwara Y, Kambayashi J, Sakon M, Higuchi N, Tanaka T, Mori T (1988b): Synthesis of a new cell penetrating calpain inhibitor (calpeptin). Biochem Biophys Res Commun 153:1201-1208.
66. Verhallen PFJ, Bevers EM, Comfurius P, Zwaal RFA (1987): Correlation between calpain-mediated cytoskeletal degradation and expression of platelet procoagulant activity. Biochim Biophys Acta 903:206-217.
67. Wysolmerski RB, Lagunoff D (1990): Involvement of myosin light-chain kinase in endothelial cell retraction. Proc Natl Acad Sci USA 87:16-20.
68. Yano Y, Shiba E, Kambayashi J, Sakon M, Kawasaki T, Fujitani K, Kang J, Mori T (1993): The effects of calpeptin (a calpain specific inhibitor) on agonist induced microparticle formation from the platelet plasma membrane. Thromb Res 71:385-396.
69. Yokota H, Katayama M, Hino F, Kato I, Takano E, Maki M, Hatanaka M, Murachi T (1991): Direct measurement of calpastatin subtypes by sandwich enzyme immunoassay using monoclonal antibodies. Mol Cell Probes 5:261-269.
70. Yoshimura N, Ohtsuki H, Hamakubo T, Kitahara A, Kannagi R, Murachi T (1984a): Distribution of calpain in various organs of the rat: An immunohistochemical study. Biomed Res 5:419-424.
71. 2+-proteases (Calpain I and Calpain II) as demonstrated by using discriminative antibodies. J Biol Chem 259:9847-9852.