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Volumn 68, Issue 3, 2004, Pages 447-456

Cleavage of desmin by cysteine proteases: Calpains and cathepsin B

Author keywords

Calpain; Cathepsin B; Cytoskeleton; Desmin; Pork

Indexed keywords

CALPAINS; CATHEPSIN; CYTOSKELETONS; DESMIN; PORK; PROTEOLYSIS;

EID: 9644291525     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2004.03.019     Document Type: Article
Times cited : (57)

References (54)
  • 1
    • 0023821279 scopus 로고
    • Cysteine proteases: The S2P2 hydrogen bond is more important for catalysis than is the analogous S1P1 bond
    • Asboth, B., Majer, Z., & Polgar, L. (1988). Cysteine proteases: The S2P2 hydrogen bond is more important for catalysis than is the analogous S1P1 bond. FEBS Letters, 233, 339-341.
    • (1988) FEBS Letters , vol.233 , pp. 339-341
    • Asboth, B.1    Majer, Z.2    Polgar, L.3
  • 2
    • 0024509811 scopus 로고
    • Amino acid analysis: Determination of cysteine plus half-cystine in proteins after hydrochloric acid hydrolysis with a disulfide compound as additive
    • Barkholt, V., & Jensen, A. (1989). Amino acid analysis: Determination of cysteine plus half-cystine in proteins after hydrochloric acid hydrolysis with a disulfide compound as additive. Analytical Biochemistry, 177, 318-322.
    • (1989) Analytical Biochemistry , vol.177 , pp. 318-322
    • Barkholt, V.1    Jensen, A.2
  • 3
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H, and cathepsin L.
    • Barett, A. J., & Kirschke, H. (1981). Cathepsin B, cathepsin H, and cathepsin L. Methods in Eznymology, 80, 535-561.
    • (1981) Methods in Eznymology , vol.80 , pp. 535-561
    • Barett, A.J.1    Kirschke, H.2
  • 4
    • 0025011384 scopus 로고
    • Properties of the desmin tail domain: Studies using synthetic peptides and antipeptide antibodies
    • Birkenberger, L., & Ip, W. (1990). Properties of the desmin tail domain: Studies using synthetic peptides and antipeptide antibodies. The Journal of Cell Biology, 111, 2063-2075.
    • (1990) The Journal of Cell Biology , vol.111 , pp. 2063-2075
    • Birkenberger, L.1    Ip, W.2
  • 7
    • 0030770449 scopus 로고    scopus 로고
    • Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis
    • Caulin, C., Salvesen, G. S., & Oshima, R. G. (1997). Caspase cleavage of keratin 18 and reorganization of intermediate filaments during epithelial cell apoptosis. The Journal of Cell Biology, 138, 1379-1394.
    • (1997) The Journal of Cell Biology , vol.138 , pp. 1379-1394
    • Caulin, C.1    Salvesen, G.S.2    Oshima, R.G.3
  • 8
    • 0037470243 scopus 로고    scopus 로고
    • Caspase proteolysis off desmin produces a dominant-negative inhibitor of intermediate filaments and promotes apoptosis
    • Chen, F., Chang, R., Trivedi, M., Capetanaki, Y., & Cryns, V. L. (2003). Caspase proteolysis off desmin produces a dominant-negative inhibitor of intermediate filaments and promotes apoptosis. The Journal of Biological Chemistry, 278, 6848-6853.
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 6848-6853
    • Chen, F.1    Chang, R.2    Trivedi, M.3    Capetanaki, Y.4    Cryns, V.L.5
  • 9
    • 0347622365 scopus 로고    scopus 로고
    • Effect of muscle type on the rate of post-mortem proteolysis in pig
    • Christensen, M., Henckel, P., & Purslow, P. P. (2004). Effect of muscle type on the rate of post-mortem proteolysis in pig. Meat Science, 66, 595-601.
    • (2004) Meat Science , vol.66 , pp. 595-601
    • Christensen, M.1    Henckel, P.2    Purslow, P.P.3
  • 10
    • 0025831476 scopus 로고
    • Calcium-activated neutral protease (calpain) system: Structure, function, and regulation
    • Croall, D., & DeMartino, G. (1991). Calcium-activated neutral protease (calpain) system: Structure, function, and regulation. Physiological Reviews, 71, 813-847.
    • (1991) Physiological Reviews , vol.71 , pp. 813-847
    • Croall, D.1    Demartino, G.2
  • 14
    • 0020171992 scopus 로고
    • Protein-chemical characterization of three structurally distinct domains along the protofilament unit of desmin 10 nm filaments
    • Geisler, N., Kaufmann, E., & Weber, K. (1982). Protein-chemical characterization of three structurally distinct domains along the protofilament unit of desmin 10 nm filaments. Cell, 30, 277-286.
    • (1982) Cell , vol.30 , pp. 277-286
    • Geisler, N.1    Kaufmann, E.2    Weber, K.3
  • 15
    • 0019133440 scopus 로고
    • Purification of smooth-muscle desmin and a protein-chemical comparison of desmins from chicken gizzard and hog stomach
    • Geisler, N., & Weber, K. (1980). Purification of smooth-muscle desmin and a protein-chemical comparison of desmins from chicken gizzard and hog stomach. European Journal of Biochemistry, 111, 425-433.
    • (1980) European Journal of Biochemistry , vol.111 , pp. 425-433
    • Geisler, N.1    Weber, K.2
  • 16
    • 0033457374 scopus 로고    scopus 로고
    • Intermediate filaments: Dynamic processes regulating their assembly, motility, and interactions with other cytoskeletal systems
    • Goldman, R. D., Chou, Y. H., Prahlad, V., & Yoon, M. (1999). Intermediate filaments: Dynamic processes regulating their assembly, motility, and interactions with other cytoskeletal systems. The FASEB Journal, 2, S261-S265.
    • (1999) The FASEB Journal , vol.2
    • Goldman, R.D.1    Chou, Y.H.2    Prahlad, V.3    Yoon, M.4
  • 18
    • 0019195947 scopus 로고
    • Synemin: A new high molecular weight protein associated with desmin and vimentin filament in muscle
    • Granger, B. L., & Lazarides, E. (1980). Synemin: A new high molecular weight protein associated with desmin and vimentin filament in muscle. Cell, 22, 727-738.
    • (1980) Cell , vol.22 , pp. 727-738
    • Granger, B.L.1    Lazarides, E.2
  • 21
    • 0033571776 scopus 로고    scopus 로고
    • The behavior of calpain-generated N- And C-terminal fragment of talin in integrin-mediated signaling pathways
    • Hayashi, M., Suzuki, H., Kawashima, S., & Saido, T. (1999). The behavior of calpain-generated N- and C-terminal fragment of talin in integrin-mediated signaling pathways. Archives of Biochemistry and Biophysics, 371, 133-141.
    • (1999) Archives of Biochemistry and Biophysics , vol.371 , pp. 133-141
    • Hayashi, M.1    Suzuki, H.2    Kawashima, S.3    Saido, T.4
  • 22
    • 0036198178 scopus 로고    scopus 로고
    • Factors contributing to proteolysis and disruption of myofibrillar proteins and the impact on tenderization in beef and sheep meat
    • Hopkins, D. L., & Thompson, J. M. (2002). Factors contributing to proteolysis and disruption of myofibrillar proteins and the impact on tenderization in beef and sheep meat. Australian Journal of Agricultural Research, 53, 149-166.
    • (2002) Australian Journal of Agricultural Research , vol.53 , pp. 149-166
    • Hopkins, D.L.1    Thompson, J.M.2
  • 23
    • 0030141091 scopus 로고    scopus 로고
    • Proteolysis of specific muscle structural proteins by calpains at low pH and temperature is similar to degradation in post mortem bovine muscle
    • Huff-Lonergan, E., Mitsushahi, T., Beekman, D. D., Parrish, F. C., Jr., Olson, G., & Robson, R. M. (1996). Proteolysis of specific muscle structural proteins by calpains at low pH and temperature is similar to degradation in post mortem bovine muscle. Journal of Animal Science, 74, 993-1008.
    • (1996) Journal of Animal Science , vol.74 , pp. 993-1008
    • Huff-Lonergan, E.1    Mitsushahi, T.2    Beekman, D.D.3    Parrish Jr., F.C.4    Olson, G.5    Robson, R.M.6
  • 24
    • 84987369453 scopus 로고
    • Studies of desmin and a actinin degradation in bovine semitendinosous muscle
    • Hwan, S. F., & Bandman, E. (1989). Studies of desmin and a actinin degradation in bovine semitendinosous muscle. Journal of Food Science, 54, 1426-1430.
    • (1989) Journal of Food Science , vol.54 , pp. 1426-1430
    • Hwan, S.F.1    Bandman, E.2
  • 27
    • 0035606922 scopus 로고    scopus 로고
    • The effect of ageing on the water-holding capacity of pork: Role of cytoskeletal proteins
    • Kristensen, L., & Purslow, P. P. (2001). The effect of ageing on the water-holding capacity of pork: Role of cytoskeletal proteins. Meat Science, 58, 17-23.
    • (2001) Meat Science , vol.58 , pp. 17-23
    • Kristensen, L.1    Purslow, P.P.2
  • 28
    • 0020512030 scopus 로고
    • Activity of lysosomal cysteine proteinase during differentiation of rat skeletal-muscle
    • Kirschke, H., Wood, L., Roisen, F. J., & Bird, J. W. C. (1983). Activity of lysosomal cysteine proteinase during differentiation of rat skeletal-muscle. The Biochemical Journal, 214, 871-877.
    • (1983) The Biochemical Journal , vol.214 , pp. 871-877
    • Kirschke, H.1    Wood, L.2    Roisen, F.J.3    Bird, J.W.C.4
  • 29
    • 0000805516 scopus 로고
    • Effect of postmortem storage on Ca++-dependant proteases, their inhibitor and myofibril fragmentation
    • Koohmaraie, M., Seideman, S. C., Schollmeyer, J. E., Dutson, T. R., & Crouse, J. D. (1987). Effect of postmortem storage on Ca++-dependant proteases, their inhibitor and myofibril fragmentation. Meat Science, 19, 187-196.
    • (1987) Meat Science , vol.19 , pp. 187-196
    • Koohmaraie, M.1    Seideman, S.C.2    Schollmeyer, J.E.3    Dutson, T.R.4    Crouse, J.D.5
  • 30
    • 0036013229 scopus 로고    scopus 로고
    • Changes in immunolelectron microscopic localisation of cathepsin D in muscle induced by conditioning or high-pressure treatment
    • Kubo, T., Gerelt, O. D., Han, T., Sugiyama, T., Nishiumi, T., & Suzuki, A. (2002). Changes in immunolelectron microscopic localisation of cathepsin D in muscle induced by conditioning or high-pressure treatment. Meat Science, 61, 415-418.
    • (2002) Meat Science , vol.61 , pp. 415-418
    • Kubo, T.1    Gerelt, O.D.2    Han, T.3    Sugiyama, T.4    Nishiumi, T.5    Suzuki, A.6
  • 32
    • 0037409612 scopus 로고    scopus 로고
    • In vitro proteolysis of myofibrillar and sarcoplasmic proteins of white muscle of sea bass (Dicentrarchus labrax L.): Effects of cathepsins B, D and L
    • Ladrat, C., Verrez-Bagnis, V., Noel, J., & Fleurence, J. (2003). In vitro proteolysis of myofibrillar and sarcoplasmic proteins of white muscle of sea bass (Dicentrarchus labrax L.): Effects of cathepsins B, D and L. Food Chemistry, 81, 517-525.
    • (2003) Food Chemistry , vol.81 , pp. 517-525
    • Ladrat, C.1    Verrez-Bagnis, V.2    Noel, J.3    Fleurence, J.4
  • 33
    • 0018842868 scopus 로고
    • Intermediate filaments as mechanical integrator of cellular space
    • Lazarides, E. (1980). Intermediate filaments as mechanical integrator of cellular space. Nature, 283, 249-256.
    • (1980) Nature , vol.283 , pp. 249-256
    • Lazarides, E.1
  • 36
    • 0030347894 scopus 로고    scopus 로고
    • Activity of μ- And m-calpain in regenerating fast and slow twitch skeletal muscles
    • Moraczewski, J., Piekarska, E., Zimowska, M., & Sobolewska, M. (1996). Activity of μ- and m-calpain in regenerating fast and slow twitch skeletal muscles. Acta Biochimica Polonica, 43, 693-700.
    • (1996) Acta Biochimica Polonica , vol.43 , pp. 693-700
    • Moraczewski, J.1    Piekarska, E.2    Zimowska, M.3    Sobolewska, M.4
  • 37
    • 0032220313 scopus 로고    scopus 로고
    • Immunolocalisation of intermediate filaments proteins in porcine meat. Fibre type and muscle-specificity variations during conditioning
    • Morrisson, E., Mielche, M., & Purslow, P. P. (1998). Immunolocalisation of intermediate filaments proteins in porcine meat. Fibre type and muscle-specificity variations during conditioning. Meat Science, 50, 91-104.
    • (1998) Meat Science , vol.50 , pp. 91-104
    • Morrisson, E.1    Mielche, M.2    Purslow, P.P.3
  • 38
    • 0020490635 scopus 로고
    • 2+ activated proteinase specific for the intermediate filament proteins vimentin and desmin
    • 2+ activated proteinase specific for the intermediate filament proteins vimentin and desmin. The Journal of Biological Chemistry, 257, 5544-5553.
    • (1982) The Journal of Biological Chemistry , vol.257 , pp. 5544-5553
    • Nelson, W.J.1    Traub, P.2
  • 39
    • 0020965175 scopus 로고
    • 2+-activated proteinase specific for these intermediate filament proteins
    • 2+-activated proteinase specific for these intermediate filament proteins. Molecular and Cellular Biology, 3, 1146-1156.
    • (1983) Molecular and Cellular Biology , vol.3 , pp. 1146-1156
    • Nelson, W.J.1    Traub, P.2
  • 41
    • 0026539218 scopus 로고
    • Proteolytic and physicochemical mechanisms involved in meat texture development
    • Ouali, A. (1992). Proteolytic and physicochemical mechanisms involved in meat texture development. Biochimie, 74, 251-265.
    • (1992) Biochimie , vol.74 , pp. 251-265
    • Ouali, A.1
  • 42
    • 0032860769 scopus 로고    scopus 로고
    • Calpain cleavage of integrin beta cytoplasmic domains
    • Pfaff, M., Du, X. P., & Ginsberg, M. H. (1999). Calpain cleavage of integrin beta cytoplasmic domains. FEBS Letters, 460, 17-22.
    • (1999) FEBS Letters , vol.460 , pp. 17-22
    • Pfaff, M.1    Du, X.P.2    Ginsberg, M.H.3
  • 43
    • 0024348987 scopus 로고
    • Determination of amino acid compositions and NH2-terminal sequences of peptides electroblotted onto PVDF membranes from tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis: Application to peptide mapping of human complement component C3
    • Ploug, M., Jensen, A. L., & Barkholt, V. (1989). Determination of amino acid compositions and NH2-terminal sequences of peptides electroblotted onto PVDF membranes from tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis: Application to peptide mapping of human complement component C3. Analytical Biochemistry, 181, 33-39.
    • (1989) Analytical Biochemistry , vol.181 , pp. 33-39
    • Ploug, M.1    Jensen, A.L.2    Barkholt, V.3
  • 45
    • 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., & Murashi, T. (1984). Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates. The Journal of Biological Chemistry, 259, 12489-12494.
    • (1984) The Journal of Biological Chemistry , vol.259 , pp. 12489-12494
    • Sasaki, T.1    Kikuchi, T.2    Yumoto, N.3    Yoshimura, N.4    Murashi, T.5
  • 46
    • 0036706535 scopus 로고    scopus 로고
    • Physiological and structural events post mortem of importance for drip loss in pork
    • Schäfer, A., Rosenvold, K., Purslow, P. P., Andersen, H. J., & Henckel, P. (2002). Physiological and structural events post mortem of importance for drip loss in pork. Meat Science, 61, 355-366.
    • (2002) Meat Science , vol.61 , pp. 355-366
    • Schäfer, A.1    Rosenvold, K.2    Purslow, P.P.3    Andersen, H.J.4    Henckel, P.5
  • 48
    • 0033595636 scopus 로고    scopus 로고
    • The PEST domain of IkappaBalpua is necessary and sufficient for in vitro degradation by mu-calpain
    • Shumway, S. D., Maki, M., & Miyamoto, S. (1999). The PEST domain of IkappaBalpua is necessary and sufficient for in vitro degradation by mu-calpain. The Journal of Biological Chemistry, 274, 30874-30881.
    • (1999) The Journal of Biological Chemistry , vol.274 , pp. 30874-30881
    • Shumway, S.D.1    Maki, M.2    Miyamoto, S.3
  • 50
    • 0020825122 scopus 로고
    • Involvement of the N-terminal polypeptide of vimentin in the formation of intermediate filaments
    • Traub, P., & Vorgias, C. E. (1983). Involvement of the N-terminal polypeptide of vimentin in the formation of intermediate filaments. Journal of Cell Science, 63, 43-67.
    • (1983) Journal of Cell Science , vol.63 , pp. 43-67
    • Traub, P.1    Vorgias, C.E.2
  • 51
    • 0028435234 scopus 로고
    • Effect of exogenous protease effectors on beef tenderness development and myoflbrillar degradation and solubility
    • Uytterhaegen, L., Claeys, E., & Demeyer, D. (1994). Effect of exogenous protease effectors on beef tenderness development and myoflbrillar degradation and solubility. Journal of Animal Science, 72, 1209-1223.
    • (1994) Journal of Animal Science , vol.72 , pp. 1209-1223
    • Uytterhaegen, L.1    Claeys, E.2    Demeyer, D.3
  • 54
    • 0026248168 scopus 로고
    • Degradation of myofibrillar proteins by extractable lysosomal enzymes and m-calpain, and the effect of zinc chloride
    • Whipple, G., & Koohmaraie, M. (1991). Degradation of myofibrillar proteins by extractable lysosomal enzymes and m-calpain, and the effect of zinc chloride. Journal of Animal Science, 69, 4449-4460.
    • (1991) Journal of Animal Science , vol.69 , pp. 4449-4460
    • Whipple, G.1    Koohmaraie, M.2


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