Calpains: Intact and active?

BioEssays

Volumn 19, Issue 11, 1997, Pages 1011-1018

  Johnson, Gail V W ^a   Guttmann, Rodney P ^a  

^a UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0031281945     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.950191111     Document Type: Review

References (70)

1. Sorimachi, H., Saldo, T.C. and Suzuki, K. (1994). New era of calpain research. Discovery of tissue-specific calpains. FEBS Lett. 343, 1-5.
2. Mellgren, R.L. (1987). Calcium-dependent proteases: an enzyme system active at cellular membranes? FASEB J. 1, 110-115.
3. Kawasaki, H. and Kawashima, S. (1996). Regulation of the calpain-calpastatin system by membranes (review). Mol. Membr. Biol. 13, 217-224.
4. Murachi, T. (1984). Calcium-dependent proteinases and specific inhibitors: calpain and calpastatin. Biochem. Soc. Symp. 49, 149-167.
5. Suzuki, K. (1987). Calcium activated neutral protease: domain structure and activity regulation. Trends Biochem. Sci. 12, 103-105.
6. Goll, D.E., Thompson, V.F., , Taylor, R.G. and Zalewska, T. (1992). Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin? BioEssays 14, 549-556.
7. Kubbatat, M.H. and Vousden, K.H. (1997). Proteolytic cleavage of human p53 by calpain: a potential regulator of protein stability. Mol. Cell. Biol. 17, 460-468.
8. Cooray, P., Yuan, Y., Schoenwaelder, S.M., Mitchell, C.A., Salem, H.H. and Jackson, S.P. (1996). Focal adhesion kinase (pp125FAK) cleavage and regulation by calpain. Biochem. J. 318, 41-47.
9. Johnson, G.V., Jope, R.S. and Binder L.I. (1989). Proteolysis of tau by calpain. Biochem. Biophys. Res. Comm. 163, 1505-1511.
10. Seubert, P., Lee, K. and Lynch, G. (1989) Ischemia triggers NMDA receptor-linked cytoskeletal proteolysis in hippocampus. Brain Res. 492, 366-370.
11. 2+)-induced suppression of neurite outgrowth in isolated hippocampal pyramidal neurons. J. Neurosci. Res. 39, 474-481.
12. Faddis, B.T., Hasbani, M.J. and Goldberg, M.P. (1997). Calpain activation contributes to dendritic remodeling after brief excititoxic injury in vitro. J. Neurosci. 17,951-959.
13. Blomgren, K., Kawashima, S., Saido, T.C., Karlsson, J.O., Elmered, A. and Hagberg, H. (1995). Fodrin degradation and subcellular distribution of calpains after neonatal rat cerebral hypoxic-ischemia. Brain Res. 684, 143-149.
14. Kampfl A. et al. (1996). Calpain inhibitors protect against depolarization-induced neurofilament protein loss of septo-hippocampal neurons in culture. Euro. J. Neurosci. 8, 344-352.
15. Saido, T.C. et al. (1992). Autolytic transition of mu-calpain upon activation as resolved by antibodies distinguishing between the pre-and post-autolysis forms. J. Biochem. 111, 81-86.
16. 2+)-activated neutral protease is active in the erythrocyte membrane in its nonautolyzed 80-kDa form. J. Biol. Chem. 269, 27992-27995.
17. 2+-dependent proteinases (μ-calpain and m-calpain). J. Biol. Chem. 264, 10096-10103.
18. Guttmann, R.P., Elce, J.S., Bell, P.D, Isbell, J.C and Johnson, G.V.W. (1997). Oxidation inhibits substrate proteolysis by calpain I but not autolysis. J. Biol. Chem. 272, 2005-2012.
19. 2+ requirement and heterodimer stability in m-calpain. J. Biol. Chem. 272, 11268-11275.
20. Sorimachi, H. et al. (1995). Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence. J. Biol. Chem. 270, 31158-31162.
21. Melloni, E. and Pontremoli, S. (1989). The calpains. Trends Neurosci. 12, 438-444
22. Kawasaki, H., Imajoh, S., Kawashima, S., Hayashi, H. and Suzuki, K. (1986). The small subunits of calcium dependent proteases with different calcium sensitivities are identical. J. Biochem. 99, 1525-1532.
23. Suzuki, K., Sorimachi, H., Yoshizawa, T., Kinbara, K. and Ishiura, S. (1995). Calpain: novel family members, activation and physiologic function. Biol. Chem. Hoppe-Seyler 376, 523-529.
24. Lin, G. et al. (1997). Crystal structure of calcium bound domain VI of calpain at 1.9A resolution and its role in enzyme assembly, regulation and inhibitor binding. Nature Struct. Biol. 4, 539-547.
25. Inomata, M., Kasai, Y., Nakamura, M. and Kawashima, S. (1988). Activation mechanism of calcium-activated neutral protease. Evidence for the existence of intramolecular and intermolecular autolyses. J. Biol. Chem. 263, 19783-19787.
26. Michetti, M., Viotti, P.L., Melloni, E. and Pontremoli, S. (1991). Mechanism of action of the calpain activator protein in rat skeletal muscle. Eur. J. Biochem. 202, 1177-1180.
27. Zimmerman, U.P. and Schlaepfer, W.W. (1991). Two-stage autolysis of the catalytic subunit initiates activation of calpain I. Biochim. Biophys. Acta. 1078, 192-198.
28. Melloni, E., Michetti, M., Salamino, F., Minafra, R. and Pontremoli, S. (1996). Modulation of the clapin autoproteolysis by calpastatin and phospholipids. Biochem. Biophy. Res. Commun. 229, 193-197.
29. Dayton, W.R. (1982). Comparison of low-and high-calcium-requiring forms of the calcium-activated protease with their autocatalytic breakdown products. Biochim. Biophys. Acta. 709, 166-172.
30. Tompa, P., Baki, A., Schad, E. and Friedrich, P. (1996). The calpain cascade. J. Biol. Chem. 271, 31612-33164.
31. 2+. J. Biol. Chem. 260, 2719-2727.
32. 2+ pool and of neuropeptide secretion. Nature 385, 343-346.
33. Takano, E. et al. (1988). Pig heart calpastatin: identification of repetitive domain structures and anomalous behavior in polyacrylamide gel electrophoresis. Biochem. 27, 1964-1972.
34. Uemori, T. et al. (1990). Characterization of a functional domain of human calpastatin. Biochem. Biophys. Res. Comm. 166, 1485-1493.
35. Croall, D.E and DeMartino, G.N. (1991). Calcium-activated neutral protease (calpain) system: structure, function and regulation. Physiol. Rev. 71, 813-847.
36. Croall, D.E. and McGrody, K.S. (1994). Domain structure of calpain: mapping the binding site for calpastatin. Biochem. 33, 13223-13230.
37. Harris, A.S., Croall, D.E. and Morrow, J.S. (1989). Calmodulin regulates fodrin susceptibility to cleavage by calcium-dependent protease I. J. Biol. Chem. 264, 177401-17408.
38. Litersky, J.M. and Johnson, G.V. (1992). Phosphorylation by cAMP-dependent protein kinase inhibits the degradation of tau by calpain. J. Biol. Chem. 267, 1563-1568.
39. Elvira, M., Diez, J.A., Wang, K.K. and Villalobo, A. (1993). Phosphorylation of connexin-32 by protein kinase C prevents its proteolysis by mu-calpain and m-calpain. J. Biol. Chem. 268, 14294-14300.
40. Rogers, S., Wells, R. and Rechsteiner M. (1986). Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234,364-368.
41. Carillo, S. et al. (1996). PEST motifs are not required for rapid calpain-mediated proteolysis of c-fos protein. Biochem. J. 313, 245-251.
42. B-binding pocket but does not prevent rapid turnover of D1. J. Biol. Chem. 270, 14919-14927.
43. Saido, T.C., Shibata, M., Takenawa, T., Murofushi, H. and Suzuki, K. (1992). Positive regulation of mu-calpain action by polyphosphoinositides. J. Biol. Chem. 267, 24585-24590.
44. 2+. Proc. Natl Acad. Sci. USA 85, 1740-1743
45. Imajoh, S., Kawasaki, H. and Suzuki, K. (1986) The amino-terminal hydrophobic region of the small subunit of calcium-activated neutral protease (CANP) is essential for its activation by phosphatidylinositol. J. Biochem. 99, 1281-1284.
46. 2+ ions. J. Biochem. (Tokyo) 101, 889-895.
47. Takano, E., Ma, H., Yang, H.Q., Maki ,M. and Hatanaka, M. (1995). Preference of calcium-dependent interactions between calmodulin-like domains of calpain and calpastatin subdomains. FEBS Lett. 362,93-97.
48. Yang, H.Q., Ma, H., Takano, E., Hatanaka, M. and Maki, M. (1994) Analysis of calcium-dependent interaction between amino-terminal conserved region of calpastatin functional domain and calmodulin-like domain of mu-calpain large subunit. J. Biol. Chem. 269, 18977-18984.
49. Cottin, P., Poussard, S., Desmazes, J.P., Georgescauld, D. and Ducastaing, A. (1991). Free calcium and calpain I activity. Biochim. Biophys. Acta. 1079, 139-145.
50. 2+ level. J. Neurosci. Res. 44, 374-380.
51. Michetti, M. et al. (1996). Autolysis of human erythrocyte calpain produces two active enzyme forms with different cell localization. FEBS Lett. 392, 11-15.
52. Inomata, M., Saito, Y., Kon, K. and Kawashima, S. (1990) Binding sites for calcium-activated neutral protease on erythrocyte membranes are not membrane phospholipids. Biochem. Biophys. Res. Comm. 171,625-632.
53. Inomata, M. and Kawashima S. (1995). The possible self-down-regulation of calpain triggered by cell membranes. Biochim. Biophys. Acta. 1235, 107-114.
54. Meyer, S.L. et al. (1996). Biologically active monomeric and heterodimeric recombinant human calpain I produced using the baculovirus expression system. Biochem. J. 314, 511-519.
55. Yoshizawa, T., Sorimachi, H., Tomioka, S., Ishiura, S. and Suzuki, K. (1995). A catalytic subunit of calpain possesses full proteolytic activity. FEBS Lett. 358, 101-103.
56. Zhang, W. and Mellgren, R.L. (1996). Calpain subunits remain associated during catalysis. Biochem. Biophys. Res. Comm. 227, 891-896.
57. Mellgren, R.L., Shaw, E. and Mericle, M.T. (1994). Inhibition of growth of human TE2 and C-33A cells by the cell-permeant calpain inhibitor benzyloxycarbonyl-Leu-Leu-Tyr diazomethyl ketone. Exp. Cell Res. 215, 164-171.
58. Mellgren, R.L., Lu, Q., Zhang, W., Lakkis, M., Shaw, E. and Mericle, M.T. (1996). Isolation of a Chinese hamster ovary cell clone possessing decreased mu-calpain content and a reduced proliferative growth rate. J. Biol. Chem. 271, 15568-15574.
59. Samis, J.A., Zboril, G. and Elce, U.S., (1987). Calpain I remains intact and intracellular during platelet activation. Immunochemical measurements with monoclonal and polyclonal antibodies. Biochem. J. 246, 481-488.
60. Zhang, W., Lane, R.D. and Mellgren, R.L. (1996). The major calpain isozymes are long-lived proteins. Design of an antisense strategy for calpain depletion in cultured cells. J. Biol. Chem. 271, 18825-18830.
61. Crawford, C., Brown, N.R. and Willis, A.C. (1993). Studies of the active site of m-calpain and the interaction with calpastatin. Biochem. J. 296, 135-142.
62. Neumann, N. P. (1972). Oxidation with hydrogen peroxide. Meth. Enzymol. 25, 393-400
63. Azuma, M. and Shearer, T.R. (1992). Involvement of calpain in diamide-induced cataract in cultured lenses. FEBS Lett. 307, 313-317.
64. Bartus, R.T. et al. (1994). Postischemic administration of AK275, a calpain inhibitor, provides substantial protection against focal ischemic brain damage. J. Cereb. Blood Flow Met. 14, 537-544,
65. Richard, I. et al. (1995). Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A. Cell 81,27-40.
66. Bartus, R.T. et al. (1995). Calpain as a novel target for treating acute neurodegenerative disorders. Neurol. Res. 17, 249-258.
67. Saito, K., Elce, J.S., Hamos, J.E. and Nixon, R.A. (1993). Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration. Proc. Natl Acad. Sci. USA 90, 2628-2632.
68. Saatman, K.E. et al. (1996). Calpain inhibitor AK295 attenuates motor and cognitive deficits following experimental brain injury in the rat. Proc. Natl Acad. Sci. USA 93, 3428-3433.
69. Smith, M.A., Sayre, L. and Pery, G. (1996) Is Alzheimer's a disease of oxidative stress? Alz. Dis. Rev. 1, 63-67.
70. Arthur, J.S., Gauthier, S. and Elce, J.S. (1995). Active site residues in m-calpain: dentification by site-directed mutagenesis. FEBS Lett. 368, 397-400.