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Volumn 456, Issue 1, 2006, Pages 48-57

Characterization of the calpain/calpastatin system in human hemopoietic cell lines

Author keywords

Calcium; Calpain; Calpastatin; Enzyme regulation; Hemopoietic cell lines; Proteolysis

Indexed keywords

CALCIUM; CALPAIN; CALPASTATIN; ISOENZYME; MONOCLONAL ANTIBODY; PROTEINASE;

EID: 33751409819     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2006.09.022     Document Type: Article
Times cited : (13)

References (57)
  • 1
    • 0025831476 scopus 로고
    • Calcium-activated neutral protease (calpain) system: structure, function and regulation
    • Croall D.E., and DeMartino G.N. Calcium-activated neutral protease (calpain) system: structure, function and regulation. Physiol. Rev. 71 (1991) 813-847
    • (1991) Physiol. Rev. , vol.71 , pp. 813-847
    • Croall, D.E.1    DeMartino, G.N.2
  • 3
    • 0031452173 scopus 로고    scopus 로고
    • Structure and physiological function of calpains
    • Sorimachi H., Ishiura S., and Suzuki K. Structure and physiological function of calpains. Biochem. J. 328 (1997) 721-732
    • (1997) Biochem. J. , vol.328 , pp. 721-732
    • Sorimachi, H.1    Ishiura, S.2    Suzuki, K.3
  • 5
    • 0036436859 scopus 로고    scopus 로고
    • Domain V of m-calpain shows the potential to form an oblique-orientated α-helix, which may modulate the enzyme's activity via interaction with anionic lipid
    • Brandenburg K., Harris F., Dennison S., Seydel U., and Phoenix D. Domain V of m-calpain shows the potential to form an oblique-orientated α-helix, which may modulate the enzyme's activity via interaction with anionic lipid. Eur. J. Biochem. 269 (2002) 5414-5422
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5414-5422
    • Brandenburg, K.1    Harris, F.2    Dennison, S.3    Seydel, U.4    Phoenix, D.5
  • 7
    • 0032543442 scopus 로고    scopus 로고
    • Calpain: a protease in search of a function? Biochem
    • Carafoli E., and Molinari M. Calpain: a protease in search of a function? Biochem. Biophys. Res. Commun. 247 (1998) 193-203
    • (1998) Biophys. Res. Commun. , vol.247 , pp. 193-203
    • Carafoli, E.1    Molinari, M.2
  • 8
    • 33745829449 scopus 로고    scopus 로고
    • Spatial localization of m-calpain to the plasma membrane by phosphoinositide biphosphate binding during epidermal growth factor receptor-mediated activation
    • Shao H., Chou J., Baty C.J., Burke N.A., Watkins S.C., Stolz D.B., and Wells A. Spatial localization of m-calpain to the plasma membrane by phosphoinositide biphosphate binding during epidermal growth factor receptor-mediated activation. Mol. Cell. Biol. 14 (2006) 5481-5496
    • (2006) Mol. Cell. Biol. , vol.14 , pp. 5481-5496
    • Shao, H.1    Chou, J.2    Baty, C.J.3    Burke, N.A.4    Watkins, S.C.5    Stolz, D.B.6    Wells, A.7
  • 9
    • 33746491305 scopus 로고    scopus 로고
    • Calpain-2 regulation of VEGF-mediated angiogenesis
    • Su Y., Cui Z., Li Z., and Block E.R. Calpain-2 regulation of VEGF-mediated angiogenesis. FASEB J. 9 (2006) 1443-1451
    • (2006) FASEB J. , vol.9 , pp. 1443-1451
    • Su, Y.1    Cui, Z.2    Li, Z.3    Block, E.R.4
  • 10
    • 0034903587 scopus 로고    scopus 로고
    • The calpain family and human disease
    • Huang Y., and Wang K.K.W. The calpain family and human disease. Trends Mol. Med. 7 (2001) 355-362
    • (2001) Trends Mol. Med. , vol.7 , pp. 355-362
    • Huang, Y.1    Wang, K.K.W.2
  • 11
    • 0842328803 scopus 로고    scopus 로고
    • Structure, activation, and biology of calpain
    • Review
    • Suzuki K., Hata S., Kawabata Y., and Sorimachi H. Structure, activation, and biology of calpain. Diabetes 53 Suppl 1 (2004) S12-S18 Review
    • (2004) Diabetes , vol.53 , Issue.SUPPL. 1
    • Suzuki, K.1    Hata, S.2    Kawabata, Y.3    Sorimachi, H.4
  • 12
    • 33644897573 scopus 로고    scopus 로고
    • Calpain inhibition: a therapeutic strategy targeting multiple disease states
    • Review
    • Carragher N.O. Calpain inhibition: a therapeutic strategy targeting multiple disease states. Curr. Pharm. Des. (2006) Review
    • (2006) Curr. Pharm. Des.
    • Carragher, N.O.1
  • 13
    • 3042597817 scopus 로고    scopus 로고
    • Insertion sequence 1 of muscle-specific calpain, p94, acts as an internal propeptide
    • Diaz B.G., Moldoveanu T., Kuiper M.J., Campbell R.L., and Davies P.L. Insertion sequence 1 of muscle-specific calpain, p94, acts as an internal propeptide. J. Biol. Chem. 279 26 (2004) 27656-27666
    • (2004) J. Biol. Chem. , vol.279 , Issue.26 , pp. 27656-27666
    • Diaz, B.G.1    Moldoveanu, T.2    Kuiper, M.J.3    Campbell, R.L.4    Davies, P.L.5
  • 14
    • 33748199182 scopus 로고    scopus 로고
    • Altered expression, intracellular distribution and activity of lymphocyte calpain II in Duchenne muscular dystrophy
    • [ahead of print]
    • Shanmuga Sundaram J., Mohana Rao V., Meena A.K., and Anandaraj M.P. Altered expression, intracellular distribution and activity of lymphocyte calpain II in Duchenne muscular dystrophy. Clin. Chim. Acta (2006) [ahead of print]
    • (2006) Clin. Chim. Acta
    • Shanmuga Sundaram, J.1    Mohana Rao, V.2    Meena, A.K.3    Anandaraj, M.P.4
  • 15
    • 33747117623 scopus 로고    scopus 로고
    • Relationship of calpain-mediated proteolysis to the expression of axonal and synaptic plasticity markers following traumatic brain injury in mice
    • [Epub ahead of print]
    • Thompson S.N., Gibson T.R., Thompson B.M., Deng Y., and Hall E.D. Relationship of calpain-mediated proteolysis to the expression of axonal and synaptic plasticity markers following traumatic brain injury in mice. Exp. Neurol. (2006) [Epub ahead of print]
    • (2006) Exp. Neurol.
    • Thompson, S.N.1    Gibson, T.R.2    Thompson, B.M.3    Deng, Y.4    Hall, E.D.5
  • 16
    • 33751428743 scopus 로고    scopus 로고
    • Molecular and cellular basis of calpainopathy (limb girdle muscular dystrophy type 2 A)
    • [Epub ahead of print]
    • Kramerova I., Beckmann J.S., and Spencer M.J. Molecular and cellular basis of calpainopathy (limb girdle muscular dystrophy type 2 A). Biochim. Biophys. Acta (2006) [Epub ahead of print]
    • (2006) Biochim. Biophys. Acta
    • Kramerova, I.1    Beckmann, J.S.2    Spencer, M.J.3
  • 17
    • 23044437768 scopus 로고    scopus 로고
    • Lymphocyte effector mechanisms in innate and adaptive immunity
    • Review
    • Moretta L. Lymphocyte effector mechanisms in innate and adaptive immunity. Curr. Opin. Immunol. 17 3 (2005) 303-305 Review
    • (2005) Curr. Opin. Immunol. , vol.17 , Issue.3 , pp. 303-305
    • Moretta, L.1
  • 18
    • 27144503808 scopus 로고    scopus 로고
    • NK cell activating receptors and tumor recognition in humans
    • Review
    • Bottino C., Moretta L., and Moretta A. NK cell activating receptors and tumor recognition in humans. Curr. Top. Microbiol. Immunol. 298 (2006) 175-182 Review
    • (2006) Curr. Top. Microbiol. Immunol. , vol.298 , pp. 175-182
    • Bottino, C.1    Moretta, L.2    Moretta, A.3
  • 21
    • 26244435035 scopus 로고    scopus 로고
    • NK-DC interaction: on the usefulness of auto-aggression
    • Review
    • Marcenaro E., Ferranti B., and Moretta A. NK-DC interaction: on the usefulness of auto-aggression. Autoimmun. Rev. 4 8 (2005) 520-525 Review
    • (2005) Autoimmun. Rev. , vol.4 , Issue.8 , pp. 520-525
    • Marcenaro, E.1    Ferranti, B.2    Moretta, A.3
  • 24
    • 0037968230 scopus 로고    scopus 로고
    • Digestion of mu- and m-calpain by trypsin and chymotrypsin
    • Thompson V.F., Lawson K.R., Barlow J., and Goll D.E. Digestion of mu- and m-calpain by trypsin and chymotrypsin. Biochim. Biophys. Acta 1648 1-2 (2003) 140-153
    • (2003) Biochim. Biophys. Acta , vol.1648 , Issue.1-2 , pp. 140-153
    • Thompson, V.F.1    Lawson, K.R.2    Barlow, J.3    Goll, D.E.4
  • 26
    • 0030593657 scopus 로고    scopus 로고
    • Autolysis of human erythrocyte calpain produces two active enzyme forms with different cell localization
    • Michetti M., Salamino F., Tedesco I., Averna M., Minafra R., Melloni E., and Pontremoli S. Autolysis of human erythrocyte calpain produces two active enzyme forms with different cell localization. FEBS Lett. 392 (1996) 11-15
    • (1996) FEBS Lett. , vol.392 , pp. 11-15
    • Michetti, M.1    Salamino, F.2    Tedesco, I.3    Averna, M.4    Minafra, R.5    Melloni, E.6    Pontremoli, S.7
  • 28
    • 0031892439 scopus 로고    scopus 로고
    • Cloning and expression of mRNA for calpain Lp82 from rat lens: splice variant of p94
    • Ma H., Fukiage C., Azuma M., and Shearer T.R. Cloning and expression of mRNA for calpain Lp82 from rat lens: splice variant of p94. Invest. Ophthalmol. Vis. Sci. 39 2 (1998) 454-461
    • (1998) Invest. Ophthalmol. Vis. Sci. , vol.39 , Issue.2 , pp. 454-461
    • Ma, H.1    Fukiage, C.2    Azuma, M.3    Shearer, T.R.4
  • 29
    • 0032144279 scopus 로고    scopus 로고
    • Protein for Lp82 calpain is expressed and enzymatically active in young rat lens
    • Ma H., Shih M., Hata I., Fukiage C., Azuma M., and Shearer T.R. Protein for Lp82 calpain is expressed and enzymatically active in young rat lens. Exp. Eye Res. 67 2 (1998) 221-229
    • (1998) Exp. Eye Res. , vol.67 , Issue.2 , pp. 221-229
    • Ma, H.1    Shih, M.2    Hata, I.3    Fukiage, C.4    Azuma, M.5    Shearer, T.R.6
  • 30
    • 0034536146 scopus 로고    scopus 로고
    • Identification and characterization of a retina-specific calpain (Rt88) from rat
    • Azuma M., Fukiage C., Higashine M., Nakajima T., Ma H., and Shearer T.R. Identification and characterization of a retina-specific calpain (Rt88) from rat. Curr. Eye Res. 21 3 (2000) 710-720
    • (2000) Curr. Eye Res. , vol.21 , Issue.3 , pp. 710-720
    • Azuma, M.1    Fukiage, C.2    Higashine, M.3    Nakajima, T.4    Ma, H.5    Shearer, T.R.6
  • 31
    • 33745138487 scopus 로고    scopus 로고
    • Low activity by the calpain system in primate lenses causes resistance to calcium-induced proteolysis
    • Nakajima E., Walkup R.D., Ma H., Shearer T.R., and Azuma M. Low activity by the calpain system in primate lenses causes resistance to calcium-induced proteolysis. Exp. Eye Res. 83 3 (2006) 593-601
    • (2006) Exp. Eye Res. , vol.83 , Issue.3 , pp. 593-601
    • Nakajima, E.1    Walkup, R.D.2    Ma, H.3    Shearer, T.R.4    Azuma, M.5
  • 33
    • 0034625483 scopus 로고    scopus 로고
    • Differential degradation of calpastatin by mu- and m-calpain in Ca(2+)-enriched human neuroblastoma LAN-5 cells
    • De Tullio R., Averna M., Salamino F., Pontremoli S., and Melloni E. Differential degradation of calpastatin by mu- and m-calpain in Ca(2+)-enriched human neuroblastoma LAN-5 cells. FEBS Lett. 475 1 (2000) 17-21
    • (2000) FEBS Lett. , vol.475 , Issue.1 , pp. 17-21
    • De Tullio, R.1    Averna, M.2    Salamino, F.3    Pontremoli, S.4    Melloni, E.5
  • 34
  • 35
    • 33646877707 scopus 로고    scopus 로고
    • Interaction between catalytically inactive calpain and calpastatin. Evidence for its occurrence in stimulated cells
    • Averna M., Stifanese R., De Tullio R., Defranchi E., Salamino F., Melloni E., and Pontremoli S. Interaction between catalytically inactive calpain and calpastatin. Evidence for its occurrence in stimulated cells. FEBS J. 273 8 (2006) 1660-1668
    • (2006) FEBS J. , vol.273 , Issue.8 , pp. 1660-1668
    • Averna, M.1    Stifanese, R.2    De Tullio, R.3    Defranchi, E.4    Salamino, F.5    Melloni, E.6    Pontremoli, S.7
  • 36
    • 0023915899 scopus 로고
    • Effects of a monoclonal anti-calpain antibody on responses of stimulated human neutrophils. Evidence for a role for proteolytically modified protein kinase C
    • Pontremoli S., Melloni E., Damiani G., Salamino F., Sparatore B., Michetti M., and Horecker B.L. Effects of a monoclonal anti-calpain antibody on responses of stimulated human neutrophils. Evidence for a role for proteolytically modified protein kinase C. J. Biol. Chem. 263 (1988) 1915-1919
    • (1988) J. Biol. Chem. , vol.263 , pp. 1915-1919
    • Pontremoli, S.1    Melloni, E.2    Damiani, G.3    Salamino, F.4    Sparatore, B.5    Michetti, M.6    Horecker, B.L.7
  • 38
    • 33644595569 scopus 로고    scopus 로고
    • Detection of polyclonal antibody against any area of the protein-antigen using immobilized protein-antigens: the critical role of the immobilization protocol
    • Fuentes M., Mateo C., Fernández-Lafuente R., and Guisán J.M. Detection of polyclonal antibody against any area of the protein-antigen using immobilized protein-antigens: the critical role of the immobilization protocol. Biomacromolecules 7 (2006) 540-544
    • (2006) Biomacromolecules , vol.7 , pp. 540-544
    • Fuentes, M.1    Mateo, C.2    Fernández-Lafuente, R.3    Guisán, J.M.4
  • 39
    • 0028281045 scopus 로고
    • Characterization of a human cell line (NK-92) with phenotypical and functional characteristics of activated natural killer cells
    • Gong J.H., Maki G., and Klingemann H.G. Characterization of a human cell line (NK-92) with phenotypical and functional characteristics of activated natural killer cells. Leukaemia 8 (1994) 652-658
    • (1994) Leukaemia , vol.8 , pp. 652-658
    • Gong, J.H.1    Maki, G.2    Klingemann, H.G.3
  • 40
    • 0025820956 scopus 로고
    • Identification of two calpastatin forms in rat skeletal muscle and their susceptibility to digestion by homologous calpains
    • Pontremoli S., Melloni E., Viotti P.L., Michetti M., Salamino F., and Horecker B.L. Identification of two calpastatin forms in rat skeletal muscle and their susceptibility to digestion by homologous calpains. Arch. Biochem. Biophys. 288 (1991) 646-652
    • (1991) Arch. Biochem. Biophys. , vol.288 , pp. 646-652
    • Pontremoli, S.1    Melloni, E.2    Viotti, P.L.3    Michetti, M.4    Salamino, F.5    Horecker, B.L.6
  • 41
    • 0030796860 scopus 로고    scopus 로고
    • Modulation of rat brain calpastatin efficiency by post-translational modifications
    • Salamino F., Averna M., Tedesco I., De Tullio R., Melloni E., and Pontremoli S. Modulation of rat brain calpastatin efficiency by post-translational modifications. FEBS Lett. 412 (1997) 433-438
    • (1997) FEBS Lett. , vol.412 , pp. 433-438
    • Salamino, F.1    Averna, M.2    Tedesco, I.3    De Tullio, R.4    Melloni, E.5    Pontremoli, S.6
  • 42
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principal of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principal of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 43
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 44
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin J., Staehelin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76 (1979) 4350-4354
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, J.1    Staehelin, T.2    Gordon, J.3
  • 45
    • 0026518154 scopus 로고
    • Ovarian expression of cellular Ki-ras p21 varies with physiological status
    • Palejwala S., and Goldsmith L.T. Ovarian expression of cellular Ki-ras p21 varies with physiological status. Proc. Natl. Acad. Sci. USA 89 (1992) 4202-4206
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4202-4206
    • Palejwala, S.1    Goldsmith, L.T.2
  • 48
    • 33747717424 scopus 로고    scopus 로고
    • Association of calpastatin with inactive calpain: a novel mechanism to control the activation of the protease?
    • [Epub ahead of print]
    • Melloni E., Averna M., Stifanese R., DeTullio R., Defranchi E., Salamino F., and Pontremoli S. Association of calpastatin with inactive calpain: a novel mechanism to control the activation of the protease?. J. Biol. Chem. (2006) [Epub ahead of print]
    • (2006) J. Biol. Chem.
    • Melloni, E.1    Averna, M.2    Stifanese, R.3    DeTullio, R.4    Defranchi, E.5    Salamino, F.6    Pontremoli, S.7
  • 50
    • 0021284744 scopus 로고
    • Two cytosolic, calcium-dependent, neutral proteinases from rabbit liver: purification and properties of the proenzymes
    • Meloni E., Pontremoli S., Salamino F., Sparatore B., Horecker M., and Michetti B.L. Two cytosolic, calcium-dependent, neutral proteinases from rabbit liver: purification and properties of the proenzymes. Arch. Biochem. Biophys. 232 (1983) 505-512
    • (1983) Arch. Biochem. Biophys. , vol.232 , pp. 505-512
    • Meloni, E.1    Pontremoli, S.2    Salamino, F.3    Sparatore, B.4    Horecker, M.5    Michetti, B.L.6
  • 51
    • 1242326458 scopus 로고    scopus 로고
    • Possible regulation of the conventional calpain system by skeletal muscle-specific calpain, p94/calpain 3
    • Epub
    • Ono Y., Kakinuma K., Torii F., Irie A., Nakagawa K., Labeit S., Abe K., Suzuki K., and Sorimachi H. Possible regulation of the conventional calpain system by skeletal muscle-specific calpain, p94/calpain 3. J. Biol. Chem. 279 4 (2004) 2761-2771 Epub
    • (2004) J. Biol. Chem. , vol.279 , Issue.4 , pp. 2761-2771
    • Ono, Y.1    Kakinuma, K.2    Torii, F.3    Irie, A.4    Nakagawa, K.5    Labeit, S.6    Abe, K.7    Suzuki, K.8    Sorimachi, H.9
  • 53
    • 33751409952 scopus 로고
    • Biological application of ionophores
    • Pressman BC. Biological application of ionophores. Ann. Rev. Biochem. 45 (1986) 530-550
    • (1986) Ann. Rev. Biochem. , vol.45 , pp. 530-550
    • Pressman, BC.1
  • 54
    • 33646081532 scopus 로고    scopus 로고
    • 2+ on rapid and transient contents of superoxide generation in differentiated THP-1 cells
    • 2+ on rapid and transient contents of superoxide generation in differentiated THP-1 cells. Biochem. Biophys. Res. Commun. 344 (2006) 571-580
    • (2006) Biochem. Biophys. Res. Commun. , vol.344 , pp. 571-580
    • Ishibashi, K.1    Okazaki, S.2    Hiramatsu, M.3
  • 55
    • 33751431101 scopus 로고    scopus 로고
    • Phyto-and endogenous estrogens differently activate intracellular calcium ion mobilization in bovine endometrial cells
    • [Epub ahead of print]
    • Woclawek-Potocka I., Borkowski K., Korzekwa A., Okuda K., and Sharzynski D.J. Phyto-and endogenous estrogens differently activate intracellular calcium ion mobilization in bovine endometrial cells. J. Reprod. Dev. (2006) [Epub ahead of print]
    • (2006) J. Reprod. Dev.
    • Woclawek-Potocka, I.1    Borkowski, K.2    Korzekwa, A.3    Okuda, K.4    Sharzynski, D.J.5
  • 56
    • 33750213600 scopus 로고    scopus 로고
    • Early activation and redistribution of calpain activity in skeletal muscle during hindlimb unweighting and reweighting
    • Enns D.L., and Belcastro A.N. Early activation and redistribution of calpain activity in skeletal muscle during hindlimb unweighting and reweighting. Can. J. Physiol. Pharmacol. 84 (2006) 601-609
    • (2006) Can. J. Physiol. Pharmacol. , vol.84 , pp. 601-609
    • Enns, D.L.1    Belcastro, A.N.2


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