메뉴 건너뛰기




Volumn 385, Issue 6, 2004, Pages 465-472

Interaction of calpastatin with calpain: A review

Author keywords

Binding; Calcium; Inhibitor; Proteases; Structure

Indexed keywords

AMINO ACID; CALPAIN; CALPASTATIN;

EID: 3242798339     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2004.054     Document Type: Review
Times cited : (187)

References (46)
  • 1
    • 0037424522 scopus 로고    scopus 로고
    • Structural determinants of the calpain inhibitory activity of calpastatin peptide B27-WT
    • Betts, R., Weinsheimer, S., Blouse, G.E., and Anagli, J. (2003). Structural determinants of the calpain inhibitory activity of calpastatin peptide B27-WT. J. Biol. Chem. 278, 7800-7809.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7800-7809
    • Betts, R.1    Weinsheimer, S.2    Blouse, G.E.3    Anagli, J.4
  • 2
    • 0031962266 scopus 로고    scopus 로고
    • The bovine calpastatin gene promoter and a new N-terminal region of the protein are targets for cAMP dependent protein kinase activity
    • Cong, M., Thompson, V.F., Goll, D.E., and Antin, P.B. (1998). The bovine calpastatin gene promoter and a new N-terminal region of the protein are targets for cAMP dependent protein kinase activity. J. Biol. Chem. 273, 660-666.
    • (1998) J. Biol. Chem. , vol.273 , pp. 660-666
    • Cong, M.1    Thompson, V.F.2    Goll, D.E.3    Antin, P.B.4
  • 3
    • 0027360303 scopus 로고
    • Studies of the active site of m-calpain and the interaction with calpastatin
    • 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.
    • (1993) Biochem. J. , vol.296 , pp. 135-142
    • Crawford, C.1    Brown, N.R.2    Willis, A.C.3
  • 4
    • 0027940509 scopus 로고
    • Domain structure of calpain: Mapping the binding site for calpastatin
    • Croall, D.E., and McGrody, K.S. (1994). Domain structure of calpain: mapping the binding site for calpastatin. Biochemistry 33, 13223-13230.
    • (1994) Biochemistry , vol.33 , pp. 13223-13230
    • Croall, D.E.1    McGrody, K.S.2
  • 5
    • 0017101439 scopus 로고
    • 2+-activated protease possibly involved in myofibrillar protein turnover. Purification from porcine muscle
    • 2+-activated protease possibly involved in myofibrillar protein turnover. Purification from porcine muscle. Biochemistry 15, 2150-2158.
    • (1976) Biochemistry , vol.15 , pp. 2150-2158
    • Dayton, W.R.1    Goll, D.E.2    Zeece, M.G.3    Robson, R.M.4    Reville, W.J.5
  • 6
    • 0038057187 scopus 로고
    • Endogenous inhibitor for calcium-dependent cysteine protease contains four internal repeats that could be responsible for its multiple reactive sites
    • Emori, Y, Kawasaki, H., Imajoh, S., Imahori, K., and Suzuki, K. (1987). Endogenous inhibitor for calcium-dependent cysteine protease contains four internal repeats that could be responsible for its multiple reactive sites. Proc. Natl. Acad. Sci. 84, 3590-3594.
    • (1987) Proc. Natl. Acad. Sci. , vol.84 , pp. 3590-3594
    • Emori, Y.1    Kawasaki, H.2    Imajoh, S.3    Imahori, K.4    Suzuki, K.5
  • 7
    • 0023835174 scopus 로고
    • All four repeating domains of the endogenous inhibitor for calcium-dependent protease independently retain inhibitory activity. Expression of the cDNA fragments in Escherichia coli
    • Emori, Y., Kawasaki, H., Imajoh, S., Minami, Y., and Suzuki, K. (1988). All four repeating domains of the endogenous inhibitor for calcium-dependent protease independently retain inhibitory activity. Expression of the cDNA fragments in Escherichia coli. J. Biol. Chem. 263, 2364-2370.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2364-2370
    • Emori, Y.1    Kawasaki, H.2    Imajoh, S.3    Minami, Y.4    Suzuki, K.5
  • 9
    • 0023650901 scopus 로고
    • A fragment of an endogenous inhibitor produced in Escherichia coli for calcium-activated neutral protease (CANP) retains an inhibitory activity
    • Imajoh, S., Kawasaki, H., Emori, Y., Ishiura, S., Minami, Y., Sugita, H., Imahori, K., and Suzuki, K. (1987a). A fragment of an endogenous inhibitor produced in Escherichia coli for calcium-activated neutral protease (CANP) retains an inhibitory activity. FEBS Lett. 215, 274-278.
    • (1987) FEBS Lett. , vol.215 , pp. 274-278
    • Imajoh, S.1    Kawasaki, H.2    Emori, Y.3    Ishiura, S.4    Minami, Y.5    Sugita, H.6    Imahori, K.7    Suzuki, K.8
  • 10
    • 0023669255 scopus 로고
    • Calcium-activated neutral protease inhibitor from rabbit erythrocytes lacks the N-terminal region of the liver inhibitor but retains three inhibitory units
    • Imajoh, S., Kawasaki, H., Emori, Y., and Suzuki, K. (1987b). Calcium-activated neutral protease inhibitor from rabbit erythrocytes lacks the N-terminal region of the liver inhibitor but retains three inhibitory units. Biochem. Biophys. Res. Comm. 146, 630-637.
    • (1987) Biochem. Biophys. Res. Comm. , vol.146 , pp. 630-637
    • Imajoh, S.1    Kawasaki, H.2    Emori, Y.3    Suzuki, K.4
  • 11
    • 0021741893 scopus 로고
    • A 107-kDa inhibitor for calcium-activated neutral protease (CANP): Purification from the human liver
    • Imajoh, S., Kawasaki, H., Kisaragi, M., Mukai, M., Sugita, H., and Suzuki, K. (1984). A 107-kDa inhibitor for calcium-activated neutral protease (CANP): purification from the human liver. Biomed. Res. 5, 481-488.
    • (1984) Biomed. Res. , vol.5 , pp. 481-488
    • Imajoh, S.1    Kawasaki, H.2    Kisaragi, M.3    Mukai, M.4    Sugita, H.5    Suzuki, K.6
  • 12
    • 0022271492 scopus 로고
    • 2+-activated neutral protease (CANP) and its endogenous inhibitor
    • 2+-activated neutral protease (CANP) and its endogenous inhibitor. FEBS Lett. 187, 47-50.
    • (1985) FEBS Lett. , vol.187 , pp. 47-50
    • Imajoh, S.1    Suzuki, K.2
  • 14
    • 0024473080 scopus 로고
    • 2+ on binding of the calpains to calpastatin
    • 2+ on binding of the calpains to calpastatin. J. Biol. Chem. 264, 17888-17896.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17888-17896
    • Kapprell, H.-P.1    Goll, D.E.2
  • 15
    • 0024346641 scopus 로고
    • Identification and characterization of inhibitory sequences in four repeating domains of the endogenous inhibitor for calcium-dependent protease
    • Kawasaki, H., Emori, Y., Imajoh-Ohmi, S., Minami, Y., and Suzuki, K. (1989). Identification and characterization of inhibitory sequences in four repeating domains of the endogenous inhibitor for calcium-dependent protease. J. Biochem. 106, 274-281.
    • (1989) J. Biochem. , vol.106 , pp. 274-281
    • Kawasaki, H.1    Emori, Y.2    Imajoh-Ohmi, S.3    Minami, Y.4    Suzuki, K.5
  • 16
    • 0030699525 scopus 로고    scopus 로고
    • A circular dichroism study of preferential hydration and alcohol effects on a denatured protein, pig calpastatin domain I
    • Konno, T., Tanaka, N., Kataoka, M., Takano, E., and Maki, M. (1997). A circular dichroism study of preferential hydration and alcohol effects on a denatured protein, pig calpastatin domain I. Biochim. Biophys. Acta 1342, 73-82.
    • (1997) Biochim. Biophys. Acta , vol.1342 , pp. 73-82
    • Konno, T.1    Tanaka, N.2    Kataoka, M.3    Takano, E.4    Maki, M.5
  • 17
    • 0026644784 scopus 로고
    • Molecular diversity in amino-terminal domains of human calpastatin by exon skipping
    • Lee, W.J., Ma, H., Takano, E., Yang, H.Q., Hatanaka, M., and Maki, M. (1992). Molecular diversity in amino-terminal domains of human calpastatin by exon skipping. J. Biol. Chem. 267, 8437-8442.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8437-8442
    • Lee, W.J.1    Ma, H.2    Takano, E.3    Yang, H.Q.4    Hatanaka, M.5    Maki, M.6
  • 18
    • 0021964351 scopus 로고
    • Purification of a high-molecular-weight inhibitor of the calcium-activated proteinase
    • Lepley, R.A., Pampusch, M., and Dayton, W.R. (1985). Purification of a high-molecular-weight inhibitor of the calcium-activated proteinase. Biochim. Biophys. Acta 828, 95-103.
    • (1985) Biochim. Biophys. Acta , vol.828 , pp. 95-103
    • Lepley, R.A.1    Pampusch, M.2    Dayton, W.R.3
  • 19
    • 0028148057 scopus 로고
    • Amino-terminal conserved region in proteinase inhibitor domain of calpastatin potentiates its calpain inhibitory activity by interacting with the calmodulin-like domain of the proteinase
    • Ma, H., Yang, H.Q., Takano, E., Hatanaka, M., and Maki, M. (1994). Amino-terminal conserved region in proteinase inhibitor domain of calpastatin potentiates its calpain inhibitory activity by interacting with the calmodulin-like domain of the proteinase. J. Biol. Chem. 269, 24430-24436.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24430-24436
    • Ma, H.1    Yang, H.Q.2    Takano, E.3    Hatanaka, M.4    Maki, M.5
  • 20
    • 0027252107 scopus 로고
    • Requirement of different subdomains of calpastatin for calpain inhibition and for binding to calmodulin-like domains
    • Ma, H., Yang, H.Q., Takano, E., Lee, W.J., Hatanaka, M., and Maki, M. (1993). Requirement of different subdomains of calpastatin for calpain inhibition and for binding to calmodulin-like domains. J. Biochem. 113, 591-599.
    • (1993) J. Biochem. , vol.113 , pp. 591-599
    • Ma, H.1    Yang, H.Q.2    Takano, E.3    Lee, W.J.4    Hatanaka, M.5    Maki, M.6
  • 22
    • 0023659729 scopus 로고
    • All four internally repetitive domains of pig calpastatin possess inhibitory activities against calpains I and II
    • Maki, M., Takano, E., Mori, H., Sato, A., Murachi, T., and Hatanaka, M. (1987b). All four internally repetitive domains of pig calpastatin possess inhibitory activities against calpains I and II. FEBS Lett. 223, 174-180.
    • (1987) FEBS Lett. , vol.223 , pp. 174-180
    • Maki, M.1    Takano, E.2    Mori, H.3    Sato, A.4    Murachi, T.5    Hatanaka, M.6
  • 23
    • 0023677846 scopus 로고
    • Analysis of structure-function relationship of pig calpastatin by expression of mutated cDNAs in Escherichia coli
    • Maki, M., Takano, E., Osawa, T., Ooi, T., Murachi, T., and Hatanaka, M. (1988). Analysis of structure-function relationship of pig calpastatin by expression of mutated cDNAs in Escherichia coli. J. Biol. Chem. 263, 10254-10261.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10254-10261
    • Maki, M.1    Takano, E.2    Osawa, T.3    Ooi, T.4    Murachi, T.5    Hatanaka, M.6
  • 24
    • 0024844775 scopus 로고
    • Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene
    • Maki, M., Baǧci, H., Hamaguchi, K., Ueda, M., Murachi, T., and Hatanaka, M. (1989). Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene. J. Biol. Chem. 264, 18866-18869.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18866-18869
    • Maki, M.1    Baǧci, H.2    Hamaguchi, K.3    Ueda, M.4    Murachi, T.5    Hatanaka, M.6
  • 26
    • 0020552823 scopus 로고
    • The protein inhibitor of calcium-dependent proteases: Purification from bovine heart and possible mechanisms of regulation
    • Mellgren R.L., and Carr, T.C. (1983). The protein inhibitor of calcium-dependent proteases: purification from bovine heart and possible mechanisms of regulation. Arch. Biochem. Biophys. 225, 779-786.
    • (1983) Arch. Biochem. Biophys. , vol.225 , pp. 779-786
    • Mellgren, R.L.1    Carr, T.C.2
  • 27
    • 0028868307 scopus 로고
    • Purification and properties of high molecular weight calpastatin from bovine brain
    • Mohan, P.S., and Nixon, R.A. (1995). Purification and properties of high molecular weight calpastatin from bovine brain. J. Neurochem. 64, 859-866.
    • (1995) J. Neurochem. , vol.64 , pp. 859-866
    • Mohan, P.S.1    Nixon, R.A.2
  • 28
    • 0141634346 scopus 로고    scopus 로고
    • Binding-induced folding transitions in calpastatin subdomains A and C
    • Mucsi, Z., Hudecz, F., Hollósi, M., Tompa, P., and Friedrich, P. (2003). Binding-induced folding transitions in calpastatin subdomains A and C. Protein Sci. 12, 2327-2336.
    • (2003) Protein Sci. , vol.12 , pp. 2327-2336
    • Mucsi, Z.1    Hudecz, F.2    Hollósi, M.3    Tompa, P.4    Friedrich, P.5
  • 29
    • 0024561590 scopus 로고
    • Intracellular regulatory system involving calpain and calpastatin
    • Murachi, T. (1989). Intracellular regulatory system involving calpain and calpastatin. Biochem. Int. 18, 263-294.
    • (1989) Biochem. Int. , vol.18 , pp. 263-294
    • Murachi, T.1
  • 30
    • 0021714076 scopus 로고
    • Purification and characterization of an inhibitor of calcium-activated neutral protease from rabbit skeletal muscle: Purification of 50,000 dalton inhibitor
    • Nakamura, M., Inomata, M., Hayashi, M., Imahori, K., and 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.
    • (1984) J. Biochem. , vol.96 , pp. 1399-1407
    • Nakamura, M.1    Inomata, M.2    Hayashi, M.3    Imahori, K.4    Kawashima, S.5
  • 31
    • 0026079729 scopus 로고
    • Binding of calpain fragments to calpastatin
    • Nishimura, T., and Goll, D.E. (1991). Binding of calpain fragments to calpastatin. J. Biol. Chem. 266, 11842-11850.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11842-11850
    • Nishimura, T.1    Goll, D.E.2
  • 34
    • 0035499860 scopus 로고    scopus 로고
    • Calpastatin expression in porcine cardiac and skeletal muscle and partial gene structure
    • Parr, T., Sensky, P.L., Bardsley, R.G., and Buttery, P.J. (2001). Calpastatin expression in porcine cardiac and skeletal muscle and partial gene structure. Arch. Biochem. Biophys. 395, 1-13.
    • (2001) Arch. Biochem. Biophys. , vol.395 , pp. 1-13
    • Parr, T.1    Sensky, P.L.2    Bardsley, R.G.3    Buttery, P.J.4
  • 35
    • 0034769614 scopus 로고    scopus 로고
    • The structure of calcium-free human m-calpain. Implications for calcium activation and function
    • Reverter, D. Sorimachi, H., and Bode, W. (2001). The structure of calcium-free human m-calpain. Implications for calcium activation and function. Trends Cardiovasc. Med. 11, 222-229.
    • (2001) Trends Cardiovasc. Med. , vol.11 , pp. 222-229
    • Reverter, D.1    Sorimachi, H.2    Bode, W.3
  • 36
    • 0021779754 scopus 로고
    • 2+-dependent proteinase
    • E.A. Khairallah, J.S. Bond, and J.W.S. Bird, eds. (New York, USA: Alan R. Liss, Inc.)
    • 2+-dependent proteinase. In: Intracellular Protein Catabolism, E.A. Khairallah, J.S. Bond, and J.W.S. Bird, eds. (New York, USA: Alan R. Liss, Inc.), pp. 257-259.
    • (1985) Intracellular Protein Catabolism , pp. 257-259
    • Shannon, J.D.1    Goll, D.E.2
  • 37
    • 0028965234 scopus 로고
    • Preference of calcium-dependent interactions between calmodulin-like domains of calpain and calpastatin subdomains
    • 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.
    • (1995) FEBS Lett. , vol.362 , pp. 93-97
    • Takano, E.1    Ma, H.2    Yang, H.Q.3    Maki, M.4    Hatanaka, M.5
  • 38
    • 0023920362 scopus 로고
    • Pig heart calpastatin: Identification of repetitive domain structures and anomalous behavior in polyacrylamide gel electrophoresis
    • Takano, E., Maki, M., Mori, H., Hatanaka, M., Marti, T., Titani, K., Kannagi, R., Ooi, T., and Murachi, T. (1988). Pig heart calpastatin: identification of repetitive domain structures and anomalous behavior in polyacrylamide gel electrophoresis. Biochemistry 27, 1964-1972.
    • (1988) Biochemistry , vol.27 , pp. 1964-1972
    • Takano, E.1    Maki, M.2    Mori, H.3    Hatanaka, M.4    Marti, T.5    Titani, K.6    Kannagi, R.7    Ooi, T.8    Murachi, T.9
  • 39
    • 0020345877 scopus 로고
    • Purification and some properties of human erythrocyte calpastatin
    • Takano, E., and Murachi, T. (1982). Purification and some properties of human erythrocyte calpastatin. J. Biochem. 92, 2021-2028.
    • (1982) J. Biochem. , vol.92 , pp. 2021-2028
    • Takano, E.1    Murachi, T.2
  • 40
    • 0033526847 scopus 로고    scopus 로고
    • Structure of mouse calpastatin isoforms: Implications of species-common and species-specific alternative splicing
    • Takano, J., Kawamura, T., Murase, M., Hitomi, K., and Maki, M. (1999). Structure of mouse calpastatin isoforms: implications of species-common and species-specific alternative splicing. Biochem. Biophys. Res. Commun. 260, 339-345.
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 339-345
    • Takano, J.1    Kawamura, T.2    Murase, M.3    Hitomi, K.4    Maki, M.5
  • 41
    • 0033931805 scopus 로고    scopus 로고
    • Four types of calpastatin isoforms with distinct amino-terminal sequences are specified by alternative first exons and differentially expressed in mouse tissues
    • Takano, J., Watanabe, M., Hitomi, K., and Maki, M. (2000). Four types of calpastatin isoforms with distinct amino-terminal sequences are specified by alternative first exons and differentially expressed in mouse tissues. J. Biochem. 128, 83-92.
    • (2000) J. Biochem. , vol.128 , pp. 83-92
    • Takano, J.1    Watanabe, M.2    Hitomi, K.3    Maki, M.4
  • 42
    • 0037453230 scopus 로고    scopus 로고
    • A structural model for the inhibition of calpain by calpastatin: Crystal structures of the native domain VI of calpain and its complexes with calpastatin peptide and a small molecule inhibitor
    • Todd, B., Moore, D., Deivanayagam, C.C.S., Lin, G-d., Chattopadhyay, D., Maki, M., Wang, K.K.W., and Narayana, S.V.L. (2003). A structural model for the inhibition of calpain by calpastatin: crystal structures of the native domain VI of calpain and its complexes with calpastatin peptide and a small molecule inhibitor. J. Mol. Biol. 328, 131-146.
    • (2003) J. Mol. Biol. , vol.328 , pp. 131-146
    • Todd, B.1    Moore, D.2    Deivanayagam, C.C.S.3    Lin, G.-D.4    Chattopadhyay, D.5    Maki, M.6    Wang, K.K.W.7    Narayana, S.V.L.8
  • 46
    • 0028263631 scopus 로고
    • Analysis of calcium-dependent interaction between amino-terminal conserved region of calpastatin functional domain and calmodulin-like domain of μ-calpain large subunit
    • 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 μ-calpain large subunit. J. Biol. Chem. 269, 18977-18984.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18977-18984
    • Yang, H.Q.1    Ma, H.2    Takano, E.3    Hatanaka, M.4    Maki, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.