메뉴 건너뛰기




Volumn 386, Issue 7, 2005, Pages 609-612

Digestive versus regulatory proteases: On calpain action in vivo

Author keywords

Calpain; Calpastatin; Cleavage specificity; Enzyme targeting

Indexed keywords

CALPAIN; CALPASTATIN; PROTEINASE; REGULATOR PROTEIN;

EID: 26844461079     PISSN: 14316730     EISSN: 14316730     Source Type: Journal    
DOI: 10.1515/BC.2005.071     Document Type: Short Survey
Times cited : (36)

References (35)
  • 2
    • 0037447227 scopus 로고    scopus 로고
    • Bioinformatic design of A-kinase anchoring protein-in silico: A potent and selective peptide antagonist of type II protein kinase A anchoring
    • Alto, N.M., Soderling, S.H., Hoshi, N., Langeberg, L.K., Fayos, R., Jennings, P.A., and Scott, J.D. (2003). Bioinformatic design of A-kinase anchoring protein-in silico: a potent and selective peptide antagonist of type II protein kinase A anchoring. Proc. Natl. Acad. Sci. USA 100, 4445-4450.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4445-4450
    • Alto, N.M.1    Soderling, S.H.2    Hoshi, N.3    Langeberg, L.K.4    Fayos, R.5    Jennings, P.A.6    Scott, J.D.7
  • 3
    • 0028219939 scopus 로고
    • Peptide bond specificity of calpain: Proteolysis of human myelin basic protein
    • Banik, N.L., Chou, C.H., Deibler, G.E., Krutzch, H.C., and Hogan, E.L. (1994). Peptide bond specificity of calpain: proteolysis of human myelin basic protein. J. Neurosci. Res. 37, 489-496.
    • (1994) J. Neurosci. Res. , vol.37 , pp. 489-496
    • Banik, N.L.1    Chou, C.H.2    Deibler, G.E.3    Krutzch, H.C.4    Hogan, E.L.5
  • 4
    • 0033553483 scopus 로고    scopus 로고
    • Calpastatin is up-regulated in response to hypoxia and is a suicide substrate to calpain after neonatal cerebral hypoxia-ischemia
    • Blomgren, K., Hallin, U., Andersson, A.L., Puka-Sundvall, M., Bahr, B.A., McRae, A., Saido, T.C., Kawashima, S., and Hagberg, H. (1999). Calpastatin is up-regulated in response to hypoxia and is a suicide substrate to calpain after neonatal cerebral hypoxia-ischemia. J. Biol. Chem. 274, 14046-14052.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14046-14052
    • Blomgren, K.1    Hallin, U.2    Andersson, A.L.3    Puka-Sundvall, M.4    Bahr, B.A.5    McRae, A.6    Saido, T.C.7    Kawashima, S.8    Hagberg, H.9
  • 8
    • 1642406178 scopus 로고    scopus 로고
    • Autolytic activation and localization in Schneider cells (S2) of calpain B from Drosophila
    • Farkas, A., Tompa, P., Schad, E., Sinka, R., Jekely, G., and Friedrich, P. (2004). Autolytic activation and localization in Schneider cells (S2) of calpain B from Drosophila. Biochem. J. 378, 299-305.
    • (2004) Biochem. J. , vol.378 , pp. 299-305
    • Farkas, A.1    Tompa, P.2    Schad, E.3    Sinka, R.4    Jekely, G.5    Friedrich, P.6
  • 11
    • 7044240676 scopus 로고    scopus 로고
    • The calpain-system of Drosophila melanogaster: Coming of age
    • Friedrich, P., Tompa, P., and Farkas, A. (2004). The calpain-system of Drosophila melanogaster: coming of age. Bioessays 26, 1088-1096.
    • (2004) Bioessays , vol.26 , pp. 1088-1096
    • Friedrich, P.1    Tompa, P.2    Farkas, A.3
  • 14
    • 0033573028 scopus 로고    scopus 로고
    • 2+-dependent protease activity and a novel mode of enzyme activation
    • 2+-dependent protease activity and a novel mode of enzyme activation. EMBO J. 18, 6880-6889.
    • (1999) EMBO J. , vol.18 , pp. 6880-6889
    • Hosfield, C.M.1    Elce, J.S.2    Davies, P.L.3    Jia, Z.4
  • 16
    • 5144233203 scopus 로고    scopus 로고
    • 2+: Roles of the large subunit N-terminal and domain III-IV linker peptides
    • 2+: roles of the large subunit N-terminal and domain III-IV linker peptides. J. Mol. Biol. 343, 1049-1053.
    • (2004) J. Mol. Biol. , vol.343 , pp. 1049-1053
    • Hosfield, C.M.1    Elce, J.S.2    Jia, Z.3
  • 17
    • 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
  • 18
    • 0028148057 scopus 로고
    • Amino-terminal conserved region in proteinase inhibitor domain of calpastatin potentiates its calpain inhibitory activity by interacting with 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 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
  • 21
    • 0141634346 scopus 로고    scopus 로고
    • Binding-induced folding transitions in calpastatin subdomains A and C
    • Mucsi, Z., Hudecz, F., Hollosi, 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    Hollosi, M.3    Tompa, P.4    Friedrich, P.5
  • 23
    • 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
  • 24
    • 0028274544 scopus 로고
    • Anchoring of protein kinase A is required for modulation of AMPA/kainate receptors on hippocampal neurons
    • Rosenmund, C., Carr, D.W., Bergeson, S.E., Nilaver, G., Scott, J.D., and Westbrook, G.L. (1994). Anchoring of protein kinase A is required for modulation of AMPA/kainate receptors on hippocampal neurons. Nature 368, 853-856.
    • (1994) Nature , vol.368 , pp. 853-856
    • Rosenmund, C.1    Carr, D.W.2    Bergeson, S.E.3    Nilaver, G.4    Scott, J.D.5    Westbrook, G.L.6
  • 25
    • 0023323994 scopus 로고
    • A unique specificity of a calcium activated neutral protease indicated in histone hydrolysis
    • Sakai, K., Akanuma, H., Imahori, K., and Kawashima, S. (1987). A unique specificity of a calcium activated neutral protease indicated in histone hydrolysis. J. Biochem. (Tokyo) 101, 911-918.
    • (1987) J. Biochem. (Tokyo) , vol.101 , pp. 911-918
    • Sakai, K.1    Akanuma, H.2    Imahori, K.3    Kawashima, S.4
  • 26
    • 0021683468 scopus 로고
    • Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates
    • Sasaki, T., Kikuchi, T., Yumoto, N., Yoshimura, N., and Murachi, T. (1984). Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates. J. Biol. Chem. 259, 12489-12494.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12489-12494
    • Sasaki, T.1    Kikuchi, T.2    Yumoto, N.3    Yoshimura, N.4    Murachi, T.5
  • 27
    • 0031031730 scopus 로고    scopus 로고
    • Site-directed mutagenesis of aΙI spectrin at codon 1175 modulates its μ-calpain susceptibility
    • Stabach, P.R., Cianci, C.D., Glantz, S.B., Zhang, Z., and Morrow, J.S. (1997). Site-directed mutagenesis of aΙI spectrin at codon 1175 modulates its μ-calpain susceptibility. Biochemistry 36, 57-65.
    • (1997) Biochemistry , vol.36 , pp. 57-65
    • Stabach, P.R.1    Cianci, C.D.2    Glantz, S.B.3    Zhang, Z.4    Morrow, J.S.5
  • 29
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P. (2002). Intrinsically unstructured proteins. Trends Biochem. Sci. 27, 527-533.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 527-533
    • Tompa, P.1
  • 31
    • 0037088661 scopus 로고    scopus 로고
    • Calpastatin subdomains A and C are activators of calpain
    • Tompa, P., Mucsi, Z., Orosz, G., and Friedrich, P. (2002). Calpastatin subdomains A and C are activators of calpain. J. Biol. Chem. 277, 9022-9026.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9022-9026
    • Tompa, P.1    Mucsi, Z.2    Orosz, G.3    Friedrich, P.4
  • 33
    • 3242798339 scopus 로고    scopus 로고
    • Interaction of calpastatin with calpain: A review
    • Wendt, A., Thompson, V.F., and Goll, D.E. (2004). Interaction of calpastatin with calpain: a review. Biol. Chem. 385, 465-472.
    • (2004) Biol. Chem. , vol.385 , pp. 465-472
    • Wendt, A.1    Thompson, V.F.2    Goll, D.E.3
  • 34
    • 10044253425 scopus 로고    scopus 로고
    • AKAP signalling complexes: Focal points in space and time
    • Wong, W. and Scott, J.D. (2004). AKAP signalling complexes: focal points in space and time. Nat. Rev. Mol. Cell Biol. 5, 959-970.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 959-970
    • Wong, W.1    Scott, J.D.2
  • 35
    • 0029763766 scopus 로고    scopus 로고
    • The major calpain isozymes are long-lived proteins. Design of an antisense strategy for calpain depletion in cultured cells
    • 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.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18825-18830
    • Zhang, W.1    Lane, R.D.2    Mellgren, R.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.