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Volumn 95, Issue 9, 2003, Pages 615-623

Myoblast migration is prevented by a calpain-dependent accumulation of MARCKS

Author keywords

MARCKS; Migration; Myoblast; Ubiquitous calpains

Indexed keywords

CALPAIN; COMPLEMENTARY DNA; DNA FRAGMENT; MARCKS PROTEIN; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN SUBUNIT;

EID: 0742271381     PISSN: 02484900     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biolcel.2003.09.005     Document Type: Article
Times cited : (33)

References (80)
  • 1
    • 0033650175 scopus 로고    scopus 로고
    • Calpain zymography with casein or fluorescein isothiocyanate casein
    • Arthur J.S. Mykles D.L. Calpain zymography with casein or fluorescein isothiocyanate casein Methods Mol. Biol. 144 2000 109-116
    • (2000) Methods Mol. Biol. , vol.144 , pp. 109-116
    • Arthur, J.S.1    Mykles, D.L.2
  • 3
    • 0026639826 scopus 로고
    • Signal transduction, and the actin cytoskeleton: The roles of MARCKS, and profilin
    • Aderem A. Signal transduction, and the actin cytoskeleton: the roles of MARCKS, and profilin Trends Biochem. Sci. 17 1992 438-443
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 438-443
    • Aderem, A.1
  • 6
    • 0029949921 scopus 로고    scopus 로고
    • The role of calpastatin (the specific calpain inhibitor) in myoblast differentiation and fusion
    • Barnoy S. Glasner T. Kosower N.S. The role of calpastatin (the specific calpain inhibitor) in myoblast differentiation and fusion Biochem. Biophys. Res. Commun. 220 1996 933-938
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 933-938
    • Barnoy, S.1    Glasner, T.2    Kosower, N.S.3
  • 7
    • 0034667733 scopus 로고    scopus 로고
    • Regulation of calpain and calpastatin in differentiating myoblasts: mRNA levels, protein synthesis and stability
    • Barnoy S. Supino-Rosin L. Kosower N.S. Regulation of calpain and calpastatin in differentiating myoblasts: mRNA levels, protein synthesis and stability Biochem. J. 351 2000 413-420
    • (2000) Biochem. J. , vol.351 , pp. 413-420
    • Barnoy, S.1    Supino-Rosin, L.2    Kosower, N.S.3
  • 8
    • 0036711804 scopus 로고    scopus 로고
    • Regulation of focal complex composition and disassembly by the calcium-dependent protease calpain
    • Bhatt A. Kaverina I. Otey C. Huttenlocher A. Regulation of focal complex composition and disassembly by the calcium-dependent protease calpain J. Cell Sci. 115 2002 3415-3425
    • (2002) J. Cell Sci. , vol.115 , pp. 3415-3425
    • Bhatt, A.1    Kaverina, I.2    Otey, C.3    Huttenlocher, A.4
  • 9
    • 0023661249 scopus 로고
    • Colocalization of calciumdependent protease II and one of its substrates at sites of cell adhesion
    • Beckerle M.C. Burridge K. DeMartino G.N. Croall D.E. Colocalization of calciumdependent protease II and one of its substrates at sites of cell adhesion Cell 51 1987 569-577
    • (1987) Cell , vol.51 , pp. 569-577
    • Beckerle, M.C.1    Burridge, K.2    DeMartino, G.N.3    Croall, D.E.4
  • 10
    • 0035504758 scopus 로고    scopus 로고
    • Differential activation of ERKs to focal adhesions by PKC epsilon is required for PMA-induced adhesion and migration of human glioma cells
    • Besson A. Davy A. Robbins S.M. Yong V.W. Differential activation of ERKs to focal adhesions by PKC epsilon is required for PMA-induced adhesion and migration of human glioma cells Oncogene 20 2001 7398-7407
    • (2001) Oncogene , vol.20 , pp. 7398-7407
    • Besson, A.1    Davy, A.2    Robbins, S.M.3    Yong, V.W.4
  • 11
    • 0027392102 scopus 로고
    • The MARCKS family of cellular protein kinase C substrates
    • Blackshear P.J. The MARCKS family of cellular protein kinase C substrates J. Biol. Chem. 268 1993 1501-1504
    • (1993) J. Biol. Chem. , vol.268 , pp. 1501-1504
    • Blackshear, P.J.1
  • 14
    • 0033579475 scopus 로고    scopus 로고
    • Phosphorylation-dependent conformational changes induce a switch in the actin-binding function of MARCKS
    • Bubb M.R. Lenox R.H. Edison A. S. Phosphorylation-dependent conformational changes induce a switch in the actin-binding function of MARCKS J. Biol. Chem. 274 1999 36472-36478
    • (1999) J. Biol. Chem. , vol.274 , pp. 36472-36478
    • Bubb, M.R.1    Lenox, R.H.2    Edison A., S.3
  • 15
    • 0033229742 scopus 로고    scopus 로고
    • Degraded collagen fragments promote rapid disassembly of smooth muscle focal adhesions that correlates with cleavage of pp125(FAK), paxillin, and talin
    • Carragher N.O. Levkau B. Ross R. Raines E.W. Degraded collagen fragments promote rapid disassembly of smooth muscle focal adhesions that correlates with cleavage of pp125(FAK), paxillin, and talin J. Cell Biol. 147 1999 619-630
    • (1999) J. Cell Biol. , vol.147 , pp. 619-630
    • Carragher, N.O.1    Levkau, B.2    Ross, R.3    Raines, E.W.4
  • 19
    • 0027940509 scopus 로고
    • Domain structure of calpain: Mapping the binding site for calpastatin
    • Croall D.E. McGrody K.S. Domain structure of calpain: mapping the binding site for calpastatin Biochemistry 33 1994 13223-13230
    • (1994) Biochemistry , vol.33 , pp. 13223-13230
    • Croall, D.E.1    McGrody, K.S.2
  • 22
    • 0027468977 scopus 로고
    • Sequence analysis of lens beta-crystallins suggests involvement of calpain in cataract formation
    • David L.L. Shearer T.R. Shih M. Sequence analysis of lens beta-crystallins suggests involvement of calpain in cataract formation J. Biol. Chem. 268 1993 1937-1940
    • (1993) J. Biol. Chem. , vol.268 , pp. 1937-1940
    • David, L.L.1    Shearer, T.R.2    Shih, M.3
  • 24
    • 0036217064 scopus 로고    scopus 로고
    • Involvement of myogenic regulator factors during fusion in the cell line C2C12
    • Dedieu S. Mazeres G. Cottin P. Brustis J.J. Involvement of myogenic regulator factors during fusion in the cell line C2C12 Int. J. Dev. Biol. 46 2002b 235-241
    • (2002) Int. J. Dev. Biol. , vol.46 , pp. 235-241
    • Dedieu, S.1    Mazeres, G.2    Cottin, P.3    Brustis, J.J.4
  • 25
    • 0037436341 scopus 로고    scopus 로고
    • Transactivation of capn2 by myogenic regulatory factors during myogenesis
    • Dedieu S. Mazeres G. Dourdin N. Cottin P. Brustis J. J. Transactivation of capn2 by myogenic regulatory factors during myogenesis J. Mol. Biol. 326 2003a 453-465
    • (2003) J. Mol. Biol. , vol.326 , pp. 453-465
    • Dedieu, S.1    Mazeres, G.2    Dourdin, N.3    Cottin, P.4    Brustis J., J.5
  • 27
    • 0037092517 scopus 로고    scopus 로고
    • Sequential activation of individual PKC isozymes in integrin-mediated muscle cell spreading: A role for MARCKS in an integrin signaling pathway
    • Disatnik M.H. Boutet S.C. Lee C.H. Mochly-Rosen D. Rando T.A. Sequential activation of individual PKC isozymes in integrin-mediated muscle cell spreading: a role for MARCKS in an integrin signaling pathway J. Cell Sci. 115 2002 2151-2163
    • (2002) J. Cell Sci. , vol.115 , pp. 2151-2163
    • Disatnik, M.H.1    Boutet, S.C.2    Lee, C.H.3    Mochly-Rosen, D.4    Rando, T.A.5
  • 28
    • 0031585178 scopus 로고    scopus 로고
    • Inhibitors of actin polymerization and calmodulin binding enhance protein kinase C-induced translocation of MARCKS in C6 glioma cells
    • 1356
    • Douglas D.N. Fink H.S. Rose S.D. Ridgway N.D. Cook H.W. Byers D.M. Inhibitors of actin polymerization and calmodulin binding enhance protein kinase C-induced translocation of MARCKS in C6 glioma cells Biochim. Biophys. Acta 1356 1997 121-130
    • (1997) Biochim. Biophys. Acta , pp. 121-130
    • Douglas, D.N.1    Fink, H.S.2    Rose, S.D.3    Ridgway, N.D.4    Cook, H.W.5    Byers, D.M.6
  • 32
    • 0035968342 scopus 로고    scopus 로고
    • Membrane proximal ERK signaling is required for M-calpain activation downstream of epidermal growth factor receptor signaling
    • Glading A. Uberall F. Keyse S.M. Lauffenburger D.A. Wells A. Membrane proximal ERK signaling is required for M-calpain activation downstream of epidermal growth factor receptor signaling J. Biol. Chem. 276 2001 23341-23348
    • (2001) J. Biol. Chem. , vol.276 , pp. 23341-23348
    • Glading, A.1    Uberall, F.2    Keyse, S.M.3    Lauffenburger, D.A.4    Wells, A.5
  • 33
    • 0025868336 scopus 로고
    • Studies of the alpha-actinin/actin interaction in the Z-disk by using calpain
    • Goll D.E. Dayton W.R. Singh I. Robson R.M. Studies of the alpha-actinin/actin interaction in the Z-disk by using calpain J. Biol. Chem. 266 1991 8501-8510
    • (1991) J. Biol. Chem. , vol.266 , pp. 8501-8510
    • Goll, D.E.1    Dayton, W.R.2    Singh, I.3    Robson, R.M.4
  • 37
    • 0024205349 scopus 로고
    • Activation mechanism of calciumactivated neutral protease. Evidence for the existence of intramolecular and intermolecular autolyses
    • Inomata M. Kasai Y. Nakamura M. Kawashima S. Activation mechanism of calciumactivated neutral protease. Evidence for the existence of intramolecular and intermolecular autolyses J. Biol. Chem. 263 1988 19783-19787
    • (1988) J. Biol. Chem. , vol.263 , pp. 19783-19787
    • Inomata, M.1    Kasai, Y.2    Nakamura, M.3    Kawashima, S.4
  • 38
    • 0033590104 scopus 로고    scopus 로고
    • Inflammatory cytokines induced down-regulation of m-calpain mRNA expression in fibroblastic synoviocytes from patients with osteoarthritis and rheumatoid arthritis
    • Ishikawa H. Nakagawa Y. Shimizu K. Nishihara H. Matsusue Y. Nakamura T. Inflammatory cytokines induced down-regulation of m-calpain mRNA expression in fibroblastic synoviocytes from patients with osteoarthritis and rheumatoid arthritis Biochem. Biophys. Res. Commun. 266 1999 341-346
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 341-346
    • Ishikawa, H.1    Nakagawa, Y.2    Shimizu, K.3    Nishihara, H.4    Matsusue, Y.5    Nakamura, T.6
  • 39
    • 0034176206 scopus 로고    scopus 로고
    • Involvement of the theta-type protein kinase C in translocation of myristoylated alanine-rich C kinase substrate (MARCKS) during myogenesis of chick embryonic myoblasts
    • Kim S.S. Kim J.H. Kim H.S. Park D.E. Chung C.H. Involvement of the theta-type protein kinase C in translocation of myristoylated alanine-rich C kinase substrate (MARCKS) during myogenesis of chick embryonic myoblasts Biochem. J. 347 2000 139-146
    • (2000) Biochem. J. , vol.347 , pp. 139-146
    • Kim, S.S.1    Kim, J.H.2    Kim, H.S.3    Park, D.E.4    Chung, C.H.5
  • 40
    • 0037096159 scopus 로고    scopus 로고
    • Involvement of protein phosphatase-1-mediated MARCKS translocation in myogenic differentiation of embryonic muscle cells
    • Kim S.S. Kim J.H. Lee S.H. Chung S.S. Bang O.S. Park D. Chung C.H. Involvement of protein phosphatase-1-mediated MARCKS translocation in myogenic differentiation of embryonic muscle cells J. Cell Sci. 115 2002 2465-2473
    • (2002) J. Cell Sci. , vol.115 , pp. 2465-2473
    • Kim, S.S.1    Kim, J.H.2    Lee, S.H.3    Chung, S.S.4    Bang, O.S.5    Park, D.6    Chung, C.H.7
  • 41
    • 0033597821 scopus 로고    scopus 로고
    • Calpain mediates integrin-induced signaling at a point upstream of Rho family members
    • Kulkarni S. Saido T.C. Suzuki K. Fox J.E. Calpain mediates integrin-induced signaling at a point upstream of Rho family members J. Biol. Chem. 274 1999 21265-21275
    • (1999) J. Biol. Chem. , vol.274 , pp. 21265-21275
    • Kulkarni, S.1    Saido, T.C.2    Suzuki, K.3    Fox, J.E.4
  • 42
    • 0037214421 scopus 로고    scopus 로고
    • Calpain mediates progressive plasma membrane permeability and proteolysis of cytoskeleton-associated paxillin, talin, and vinculin during renal cell death
    • Liu X. Schnellmann R.G. Calpain mediates progressive plasma membrane permeability and proteolysis of cytoskeleton-associated paxillin, talin, and vinculin during renal cell death J. Pharmacol. Exp. Ther. 304 2003 63-70
    • (2003) J. Pharmacol. Exp. Ther. , vol.304 , pp. 63-70
    • Liu, X.1    Schnellmann, R.G.2
  • 43
    • 0033218025 scopus 로고    scopus 로고
    • Tissue release of cardiac markers: From physiology to clinical applications
    • Mair J. Tissue release of cardiac markers: from physiology to clinical applications Clin. Chem. Lab. Med. 37 1999 1077-1084
    • (1999) Clin. Chem. Lab. Med. , vol.37 , pp. 1077-1084
    • Mair, J.1
  • 44
    • 0026564312 scopus 로고
    • Affinity purification and characterization of Myristoylated Alanine-rich Protein Kinase C Substrate (MARCKS) from bovine brain
    • Manenti S. Sorokine O. Van Dorsselaer A. Taniguchi H. Affinity purification and characterization of Myristoylated Alanine-rich Protein Kinase C Substrate (MARCKS) from bovine brain J. Biol. Chem. 267 1992 22310-22315
    • (1992) J. Biol. Chem. , vol.267 , pp. 22310-22315
    • Manenti, S.1    Sorokine, O.2    Van Dorsselaer, A.3    Taniguchi, H.4
  • 45
    • 0027965091 scopus 로고
    • Measurement of cell migration stimulated by interleukin 8: Use of ATP chemiluminescence
    • McCafferty A.C. Cree I.A. Measurement of cell migration stimulated by interleukin 8: use of ATP chemiluminescence Cytokine 6 1994 450-453
    • (1994) Cytokine , vol.6 , pp. 450-453
    • McCafferty, A.C.1    Cree, I.A.2
  • 46
    • 0021164750 scopus 로고
    • Characterization of the single peptide generated from the amino-terminus end of alpha- and beta-hemoglobin chains by the Ca2+-dependent neutral proteinase
    • Melloni E. Salamino F. Sparatore B. Michetti M. Pontremoli S. Characterization of the single peptide generated from the amino-terminus end of alpha- and beta-hemoglobin chains by the Ca2+-dependent neutral proteinase Biochim. Biophys. Acta 788 1984 11-16
    • (1984) Biochim. Biophys. Acta , vol.788 , pp. 11-16
    • Melloni, E.1    Salamino, F.2    Sparatore, B.3    Michetti, M.4    Pontremoli, S.5
  • 47
    • 0032584719 scopus 로고    scopus 로고
    • Cleavage of the cytoplasmic domain of the integrin beta3 subunit during endothelial cell apoptosis
    • Meredith Jr J. Mu Z. Saido T. Du X. Cleavage of the cytoplasmic domain of the integrin beta3 subunit during endothelial cell apoptosis J. Biol. Chem. 273 1998 19525-19531
    • (1998) J. Biol. Chem. , vol.273 , pp. 19525-19531
    • Meredith Jr., J.1    Mu, Z.2    Saido, T.3    Du, X.4
  • 49
    • 0029882525 scopus 로고    scopus 로고
    • Increased M-calpain expression in the mesencephalon of patients with Parkinson's disease but not in other neurodegenerative disorders involving the mesencephalon: A role in nerve cell death?
    • Mouatt-Prigent A. Karlsson J.O. Agid Y. Hirsch E.C. Increased M-calpain expression in the mesencephalon of patients with Parkinson's disease but not in other neurodegenerative disorders involving the mesencephalon: a role in nerve cell death? Neuroscience 73 1996 979-987
    • (1996) Neuroscience , vol.73 , pp. 979-987
    • Mouatt-Prigent, A.1    Karlsson, J.O.2    Agid, Y.3    Hirsch, E.C.4
  • 51
    • 0031976733 scopus 로고    scopus 로고
    • Physical and biochemical regulation of integrin release during rear detachment of migrating cells
    • Palecek S.P. Huttenlocher A. Horwitz A.F. Lauffenburger D.A. Physical and biochemical regulation of integrin release during rear detachment of migrating cells J. Cell Sci. 111 1998 929-940
    • (1998) J. Cell Sci. , vol.111 , pp. 929-940
    • Palecek, S.P.1    Huttenlocher, A.2    Horwitz, A.F.3    Lauffenburger, D.A.4
  • 52
    • 0026182528 scopus 로고
    • An indirect bioluminescence method for the quantitative measurement of polymorphonuclear cell chemotaxis
    • Partsch G. Schwarzer C. An indirect bioluminescence method for the quantitative measurement of polymorphonuclear cell chemotaxis J. Biolumin. Chemilumin. 6 1991 159-167
    • (1991) J. Biolumin. Chemilumin. , vol.6 , pp. 159-167
    • Partsch, G.1    Schwarzer, C.2
  • 53
    • 0034625418 scopus 로고    scopus 로고
    • Mitotic clonal expansion during preadipocyte differentiation: Calpain-mediated turnover of p27
    • Patel Y.M. Lane M.D. Mitotic clonal expansion during preadipocyte differentiation: calpain-mediated turnover of p27 J. Biol. Chem. 275 2000 17653-17660
    • (2000) J. Biol. Chem. , vol.275 , pp. 17653-17660
    • Patel, Y.M.1    Lane, M.D.2
  • 55
    • 0034494961 scopus 로고    scopus 로고
    • Focal adhesions: Structure and dynamics
    • Petit V. Thiery J.P. Focal adhesions: structure and dynamics Biol. Cell 92 2000 477-494
    • (2000) Biol. Cell , vol.92 , pp. 477-494
    • Petit, V.1    Thiery, J.P.2
  • 58
    • 0028283214 scopus 로고    scopus 로고
    • Proteolytic cleavage of the integrin beta 4 subunit
    • Potts A.J. Croall D.E. Hemler M.E. Proteolytic cleavage of the integrin beta 4 subunit Exp. Cell Res. 212 1999 2-9
    • (1999) Exp. Cell Res. , vol.212 , pp. 2-9
    • Potts, A.J.1    Croall, D.E.2    Hemler, M.E.3
  • 59
    • 0027728978 scopus 로고
    • Quantitative measurement of calpain I and II mRNAs in differentiating rat muscle cells using a competitive polymerase chain reaction method
    • Poussard S. Cottin P. Brustis J.J. Talmat S. Elamrani N. Ducastaing A. Quantitative measurement of calpain I and II mRNAs in differentiating rat muscle cells using a competitive polymerase chain reaction method Biochimie 75 1993 885-890
    • (1993) Biochimie , vol.75 , pp. 885-890
    • Poussard, S.1    Cottin, P.2    Brustis, J.J.3    Talmat, S.4    Elamrani, N.5    Ducastaing, A.6
  • 64
    • 0027474051 scopus 로고
    • Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: A potential molecular basis for neuronal degeneration
    • Saito K. Elce J.S. Hamos J.E. Nixon R.A. 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. U. S. A. 90 1993 2628-2632
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 2628-2632
    • Saito, K.1    Elce, J.S.2    Hamos, J.E.3    Nixon, R.A.4
  • 65
    • 0034936674 scopus 로고    scopus 로고
    • Calpain function in the modulation of signal transduction molecules
    • Sato K. Kawashima S. Calpain function in the modulation of signal transduction molecules Biol. Chem. 382 2001 743-751
    • (2001) Biol. Chem. , vol.382 , pp. 743-751
    • Sato, K.1    Kawashima, S.2
  • 66
    • 0031028205 scopus 로고    scopus 로고
    • Calpain cleavage of focal adhesion proteins regulates the cytoskeletal attachment of integrin alphaIIbbeta3 (platelet glycoprotein IIb/IIIa) and the cellular retraction of fibrin clots
    • Schoenwaelder S.M. Yuan Y. Cooray P. Salem H.H. Jackson S.P. Calpain cleavage of focal adhesion proteins regulates the cytoskeletal attachment of integrin alphaIIbbeta3 (platelet glycoprotein IIb/IIIa) and the cellular retraction of fibrin clots J. Biol. Chem. 272 1997 1694-1702
    • (1997) J. Biol. Chem. , vol.272 , pp. 1694-1702
    • Schoenwaelder, S.M.1    Yuan, Y.2    Cooray, P.3    Salem, H.H.4    Jackson, S.P.5
  • 67
    • 0030002451 scopus 로고    scopus 로고
    • Proteolytic cleavage of alpha-actinin by calpain in T cells stimulated with anti-CD3 monoclonal antibody
    • Selliah N. Brooks W.H. Roszman T.L. Proteolytic cleavage of alpha-actinin by calpain in T cells stimulated with anti-CD3 monoclonal antibody J. Immunol. 156 1996 3215-3221
    • (1996) J. Immunol. , vol.156 , pp. 3215-3221
    • Selliah, N.1    Brooks, W.H.2    Roszman, T.L.3
  • 68
    • 0036207773 scopus 로고    scopus 로고
    • Activation of m-calpain (calpain II) by epidermal growth factor is limited by protein kinase A phosphorylation of m-calpain
    • Shiraha H. Glading A. Chou J. Jia Z. Wells A. Activation of m-calpain (calpain II) by epidermal growth factor is limited by protein kinase A phosphorylation of m-calpain Mol. Cell Biol. 22 2002 2716-2727
    • (2002) Mol. Cell Biol. , vol.22 , pp. 2716-2727
    • Shiraha, H.1    Glading, A.2    Chou, J.3    Jia, Z.4    Wells, A.5
  • 69
    • 0024369426 scopus 로고
    • Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle
    • Sorimachi H. Imajoh-Ohmi S. Emori Y. Kawasaki H. Ohno S. Minami Y. Suzuki K. Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle J. Biol. Chem. 264 1989 20106-20111
    • (1989) J. Biol. Chem. , vol.264 , pp. 20106-20111
    • Sorimachi, H.1    Imajoh-Ohmi, S.2    Emori, Y.3    Kawasaki, H.4    Ohno, S.5    Minami, Y.6    Suzuki, K.7
  • 70
    • 0035943628 scopus 로고    scopus 로고
    • Overexpression of the myristoylated alanine-rich C-kinase substrate inhibits cell adhesion to extracellular matrix components
    • Spizz G. Blackshear P.J. Overexpression of the myristoylated alanine-rich C-kinase substrate inhibits cell adhesion to extracellular matrix components J. Biol. Chem. 276 2001 32264-32273
    • (2001) J. Biol. Chem. , vol.276 , pp. 32264-32273
    • Spizz, G.1    Blackshear, P.J.2
  • 71
    • 0032498543 scopus 로고    scopus 로고
    • LFA-1-mediated adhesion is regulated by cytoskeletal restraint, and by a Ca2+-dependent protease, calpain
    • Stewart M.P. McDowall A. Hogg N. LFA-1-mediated adhesion is regulated by cytoskeletal restraint, and by a Ca2+-dependent protease, calpain J. Cell Biol. 140 1998 699-707
    • (1998) J. Cell Biol. , vol.140 , pp. 699-707
    • Stewart, M.P.1    McDowall, A.2    Hogg, N.3
  • 72
    • 0029053995 scopus 로고
    • Membrane association of the myristoylated alaninerich C kinase substrate (MARCKS) protein. Mutational analysis provides evidence for complex interactions
    • Swierczynski S.L. Blackshear P.J. Membrane association of the myristoylated alaninerich C kinase substrate (MARCKS) protein. Mutational analysis provides evidence for complex interactions J. Biol. Chem. 270 1995 13436-13445
    • (1995) J. Biol. Chem. , vol.270 , pp. 13436-13445
    • Swierczynski, S.L.1    Blackshear, P.J.2
  • 73
    • 0032589785 scopus 로고    scopus 로고
    • Externalization of calpain (calcium-dependent neutral cysteine proteinase) in human arthritic cartilage
    • Szomor Z. Shimizu K. Yamamoto S. Yasuda T. Ishikawa H. Nakamura T. Externalization of calpain (calcium-dependent neutral cysteine proteinase) in human arthritic cartilage Clin. Exp. Rheumatol. 17 1999 569-574
    • (1999) Clin. Exp. Rheumatol. , vol.17 , pp. 569-574
    • Szomor, Z.1    Shimizu, K.2    Yamamoto, S.3    Yasuda, T.4    Ishikawa, H.5    Nakamura, T.6
  • 77
    • 0037333187 scopus 로고    scopus 로고
    • Calpain inhibitor (BSF 409425) diminishes ischemia/reperfusion-induced damage of rabbit heart mitochondria
    • Trumbeckaite S. Neuhof C. Zierz S. Gellerich F.N. Calpain inhibitor (BSF 409425) diminishes ischemia/reperfusion-induced damage of rabbit heart mitochondria Biochem. Pharmacol. 65 2003 911-916
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 911-916
    • Trumbeckaite, S.1    Neuhof, C.2    Zierz, S.3    Gellerich, F.N.4
  • 78
    • 0345540626 scopus 로고    scopus 로고
    • Translocation of MARCKS and reorganization of the cytoskeleton by PMA correlates with the ion selectivity, the confluence, and transformation state of kidney epithelial cell lines
    • Vaaraniemi J. Palovuori R. Lehto V.P. Eskelinen S. Translocation of MARCKS and reorganization of the cytoskeleton by PMA correlates with the ion selectivity, the confluence, and transformation state of kidney epithelial cell lines J. Cell Physiol. 181 1999 83-95
    • (1999) J. Cell Physiol. , vol.181 , pp. 83-95
    • Vaaraniemi, J.1    Palovuori, R.2    Lehto, V.P.3    Eskelinen, S.4
  • 79
    • 0031969695 scopus 로고    scopus 로고
    • Calpain inhibitors, but not caspase inhibitors, prevent actin proteolysis and DNA fragmentation during apoptosis
    • Villa P.G. Henzel W.J. Sensenbrenner M. Henderson C.E. Pettmann B. Calpain inhibitors, but not caspase inhibitors, prevent actin proteolysis and DNA fragmentation during apoptosis J. Cell Sci. 111 1998 713-722
    • (1998) J. Cell Sci. , vol.111 , pp. 713-722
    • Villa, P.G.1    Henzel, W.J.2    Sensenbrenner, M.3    Henderson, C.E.4    Pettmann, B.5
  • 80
    • 0035958967 scopus 로고    scopus 로고
    • Calpain cleavage promotes talin binding to the beta 3 integrin cytoplasmic domain
    • Yan, B. Calderwood D.A. Yaspan B. Ginsberg M.H. Calpain cleavage promotes talin binding to the beta 3 integrin cytoplasmic domain J. Biol. Chem. 276 2001 28164-28170
    • (2001) J. Biol. Chem. , vol.276 , pp. 28164-28170
    • Yan, B.1    Calderwood, D.A.2    Yaspan, B.3    Ginsberg, M.H.4


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