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Volumn 72, Issue 15, 2012, Pages 1595-1610

Effects of lysophosphatidic acid on calpain-mediated proteolysis of focal adhesion kinase in human prostate cancer cells

Author keywords

cell adhesion; LPA receptor antagonist; paxillin; tyrosine kinases

Indexed keywords

CALCIUM; CALPAIN; FOCAL ADHESION KINASE; GROWTH FACTOR; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; LYSOPHOSPHATIDIC ACID; PAXILLIN; PROTEIN KINASE C ALPHA; RAS PROTEIN;

EID: 84867040209     PISSN: 02704137     EISSN: 10970045     Source Type: Journal    
DOI: 10.1002/pros.22513     Document Type: Article
Times cited : (6)

References (74)
  • 1
    • 0037509990 scopus 로고    scopus 로고
    • Focal adhesion kinase: The first ten years
    • Parsons JT,. Focal adhesion kinase: The first ten years. J Cell Sci 2003; 116: 1409-1416.
    • (2003) J Cell Sci , vol.116 , pp. 1409-1416
    • Parsons, J.T.1
  • 2
    • 21244494930 scopus 로고    scopus 로고
    • G protein-coupled receptor activation rapidly stimulates focal adhesion kinase phosphorylation at Ser-843
    • Fan RS, Jacamo RO, Jiang Z, Sinnett-Smith J, Rozengurt E,. G protein-coupled receptor activation rapidly stimulates focal adhesion kinase phosphorylation at Ser-843. J Biol Chem 2005; 280: 24212-24220.
    • (2005) J Biol Chem , vol.280 , pp. 24212-24220
    • Fan, R.S.1    Jacamo, R.O.2    Jiang, Z.3    Sinnett-Smith, J.4    Rozengurt, E.5
  • 3
    • 3142521875 scopus 로고    scopus 로고
    • Control of motile and invasive cell phenotypes by focal adhesion kinase
    • Schlaepfer DD, Mitra SK, Ilic D,. Control of motile and invasive cell phenotypes by focal adhesion kinase. Biochim Biophys Acta 2004; 1692: 77-102.
    • (2004) Biochim Biophys Acta , vol.1692 , pp. 77-102
    • Schlaepfer, D.D.1    Mitra, S.K.2    Ilic, D.3
  • 4
    • 0142141199 scopus 로고    scopus 로고
    • Focal adhesion kinase signaling activities and their implications in the control of cell survival and motility
    • Hanks SK, Ryzhova L, Shin NY, Brabek J,. Focal adhesion kinase signaling activities and their implications in the control of cell survival and motility. Front Biosci 2003; 8: d982-d996.
    • (2003) Front Biosci , vol.8
    • Hanks, S.K.1    Ryzhova, L.2    Shin, N.Y.3    Brabek, J.4
  • 5
    • 33745186178 scopus 로고    scopus 로고
    • The signaling and biological implications of FAK overexpression in cancer
    • Seisser PMF, Hanks SK,. The signaling and biological implications of FAK overexpression in cancer. Clin Cancer Res 2006; 12: 3233-3237.
    • (2006) Clin Cancer Res , vol.12 , pp. 3233-3237
    • Seisser, P.M.F.1    Hanks, S.K.2
  • 6
    • 0030118419 scopus 로고    scopus 로고
    • Correlations between the expression, phosphotyrosine content and enzymatic activity of focal adhesion kinase pp125FAK in tumor and nontransformed cells
    • Withers BE, Hanks SK, Fry DW,. Correlations between the expression, phosphotyrosine content and enzymatic activity of focal adhesion kinase pp125FAK in tumor and nontransformed cells. Cancer Biochem Biophys 1996; 15: 127-139.
    • (1996) Cancer Biochem Biophys , vol.15 , pp. 127-139
    • Withers, B.E.1    Hanks, S.K.2    Fry, D.W.3
  • 8
    • 0032486198 scopus 로고    scopus 로고
    • Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN
    • Tamura M, Gu J, Matsumoto K, Aota S, Parsons R, Yamada KM,. Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN. Science 1998; 280: 1614-1617.
    • (1998) Science , vol.280 , pp. 1614-1617
    • Tamura, M.1    Gu, J.2    Matsumoto, K.3    Aota, S.4    Parsons, R.5    Yamada, K.M.6
  • 10
    • 0030892186 scopus 로고    scopus 로고
    • Calpain: A cytosolic proteinase active at the membranes
    • Molinari M, Carafoli E,. Calpain: A cytosolic proteinase active at the membranes. J Membr Biol 1997; 156: 1-8.
    • (1997) J Membr Biol , vol.156 , pp. 1-8
    • Molinari, M.1    Carafoli, E.2
  • 11
    • 0035930548 scopus 로고    scopus 로고
    • Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts
    • Dourdin N, Bhatt AK, Dutt P, Greer PA, Arthur SC, Elce JS, Huttenlocher A,. Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts. J Biol Chem 2001; 276: 38382-38388.
    • (2001) J Biol Chem , vol.276 , pp. 38382-38388
    • Dourdin, N.1    Bhatt, A.K.2    Dutt, P.3    Greer, P.A.4    Arthur, S.C.5    Elce, J.S.6    Huttenlocher, A.7
  • 12
    • 26244434596 scopus 로고    scopus 로고
    • Regulating cell migration: Calpains make the cut
    • Franco SJ, Huttenlocher A,. Regulating cell migration: Calpains make the cut. J Cell Sci 2005; 118: 3829-3838.
    • (2005) J Cell Sci , vol.118 , pp. 3829-3838
    • Franco, S.J.1    Huttenlocher, A.2
  • 13
    • 0346095195 scopus 로고    scopus 로고
    • Myoblast migration is regulated by calpain through its involvement in cell attachment and cytoskeletal organization
    • Dedieu S, Poussard S, Mazeres G, Grise F, Dargelos E, Cottin P, Brustis JJ,. Myoblast migration is regulated by calpain through its involvement in cell attachment and cytoskeletal organization. Exp Cell Res 2004; 292: 187-200.
    • (2004) Exp Cell Res , vol.292 , pp. 187-200
    • Dedieu, S.1    Poussard, S.2    Mazeres, G.3    Grise, F.4    Dargelos, E.5    Cottin, P.6    Brustis, J.J.7
  • 15
    • 33646822656 scopus 로고    scopus 로고
    • Integrin a2-mediated ERK and calpain activation play a critical role in cell adhesion and motility via focal adhesion kinase signaling. Identification of a novel signaling pathway
    • Sawhney RS, Cookson MM, Omar Y, Hauser J, Brattain MG,. Integrin a2-mediated ERK and calpain activation play a critical role in cell adhesion and motility via focal adhesion kinase signaling. Identification of a novel signaling pathway. J Biol Chem 2006; 281: 8497-8510.
    • (2006) J Biol Chem , vol.281 , pp. 8497-8510
    • Sawhney, R.S.1    Cookson, M.M.2    Omar, Y.3    Hauser, J.4    Brattain, M.G.5
  • 16
    • 0041924982 scopus 로고    scopus 로고
    • A novel role for FAK as a protease-targeting adaptor protein: Regulation by p42 ERK and Src
    • Carragher NO, Westhoff MA, Fincham VJ, Schaller MD, Frame MC,. A novel role for FAK as a protease-targeting adaptor protein: Regulation by p42 ERK and Src. Curr Biol 2003; 13: 1442-1450.
    • (2003) Curr Biol , vol.13 , pp. 1442-1450
    • Carragher, N.O.1    Westhoff, M.A.2    Fincham, V.J.3    Schaller, M.D.4    Frame, M.C.5
  • 17
    • 0029890020 scopus 로고    scopus 로고
    • Targeted proteolysis of the focal adhesion kinase pp125FAK during c-MYC-induced apoptosis is suppressed by integrin signalling
    • Crouch DH, Fincham VJ, Frame MC,. Targeted proteolysis of the focal adhesion kinase pp125FAK during c-MYC-induced apoptosis is suppressed by integrin signalling. Oncogene 1996; 12: 2689-2696.
    • (1996) Oncogene , vol.12 , pp. 2689-2696
    • Crouch, D.H.1    Fincham, V.J.2    Frame, M.C.3
  • 18
    • 4444338326 scopus 로고    scopus 로고
    • Src-mediated phosphorylation of focal adhesion kinase couples actin and adhesion dynamics to survival signaling
    • Westhoff MA, Serrels B, Fincham VJ, Frame MC, Carragher NO,. Src-mediated phosphorylation of focal adhesion kinase couples actin and adhesion dynamics to survival signaling. Mol Cell Biol 2004; 24: 8113-8133.
    • (2004) Mol Cell Biol , vol.24 , pp. 8113-8133
    • Westhoff, M.A.1    Serrels, B.2    Fincham, V.J.3    Frame, M.C.4    Carragher, N.O.5
  • 19
    • 0029971297 scopus 로고    scopus 로고
    • A mechanism for regulation of the adhesion-associated protein tyrosine kinase pp125FAK
    • Richardson A, Parsons T,. A mechanism for regulation of the adhesion-associated protein tyrosine kinase pp125FAK. Nature 1996; 380: 538-540.
    • (1996) Nature , vol.380 , pp. 538-540
    • Richardson, A.1    Parsons, T.2
  • 21
    • 0032479435 scopus 로고    scopus 로고
    • Caspases cleave focal adhesion kinase during apoptosis to generate a FRNK-like polypeptide
    • Gervais FG, Thornberry NA, Ruffolo SC, Nicholson DW, Roy S,. Caspases cleave focal adhesion kinase during apoptosis to generate a FRNK-like polypeptide. J Biol Chem 1998; 273: 17102-17108.
    • (1998) J Biol Chem , vol.273 , pp. 17102-17108
    • Gervais, F.G.1    Thornberry, N.A.2    Ruffolo, S.C.3    Nicholson, D.W.4    Roy, S.5
  • 23
    • 0038487319 scopus 로고    scopus 로고
    • Lysophosphatidic acid signaling: How a small lipid does big things
    • Luquain C, Sciorra VA, Morris AJ,. Lysophosphatidic acid signaling: How a small lipid does big things. Trends Biochem Sci 2003; 28: 377-383.
    • (2003) Trends Biochem Sci , vol.28 , pp. 377-383
    • Luquain, C.1    Sciorra, V.A.2    Morris, A.J.3
  • 24
    • 2442658976 scopus 로고    scopus 로고
    • Lysophospholipid G protein-coupled receptors
    • Anliker B, Chun J,. Lysophospholipid G protein-coupled receptors. J Biol Chem 2004; 279: 20555-20558.
    • (2004) J Biol Chem , vol.279 , pp. 20555-20558
    • Anliker, B.1    Chun, J.2
  • 26
    • 0031938954 scopus 로고    scopus 로고
    • Lysophosphatidic acid stimulates phospholipase D activity and cell proliferation in PC-3 human prostate cancer cells
    • Qi C, Park JH, Gibbs TC, Shirley DW, Bradshaw CD, Ella KM, Meier KE,. Lysophosphatidic acid stimulates phospholipase D activity and cell proliferation in PC-3 human prostate cancer cells. J Cell Physiol 1998; 174: 261-272.
    • (1998) J Cell Physiol , vol.174 , pp. 261-272
    • Qi, C.1    Park, J.H.2    Gibbs, T.C.3    Shirley, D.W.4    Bradshaw, C.D.5    Ella, K.M.6    Meier, K.E.7
  • 27
    • 0034014895 scopus 로고    scopus 로고
    • Regulation of expression of Edg family receptors in human prostate cancer cell lines
    • Gibbs TC, Xie Y, Meier KE,. Regulation of expression of Edg family receptors in human prostate cancer cell lines. Ann NY Acad Sci 2000; 905: 290-293.
    • (2000) Ann NY Acad Sci , vol.905 , pp. 290-293
    • Gibbs, T.C.1    Xie, Y.2    Meier, K.E.3
  • 28
    • 0036789666 scopus 로고    scopus 로고
    • Expression of focal adhesion kinase in normal and pathologic human prostate tissues
    • Rovin JD, Frierson HF Jr, Ledinh W, Parsons JT, Adams RB,. Expression of focal adhesion kinase in normal and pathologic human prostate tissues. Prostate 2002; 53: 124-132.
    • (2002) Prostate , vol.53 , pp. 124-132
    • Rovin, J.D.1    Frierson, Jr.H.F.2    Ledinh, W.3    Parsons, J.T.4    Adams, R.B.5
  • 29
    • 0029737857 scopus 로고    scopus 로고
    • Regulation and activation of focal adhesion kinase and paxillin during the adhesion, proliferation, and differentiation of prostatic epithelial cells in vitro and in vivo
    • Tremblay L, Hauck W, Nguyen LT, Allard P, Landry F, Chapdelaine A, Chevalier S,. Regulation and activation of focal adhesion kinase and paxillin during the adhesion, proliferation, and differentiation of prostatic epithelial cells in vitro and in vivo. Mol Endocrinol 1996; 10: 1010-1020.
    • (1996) Mol Endocrinol , vol.10 , pp. 1010-1020
    • Tremblay, L.1    Hauck, W.2    Nguyen, L.T.3    Allard, P.4    Landry, F.5    Chapdelaine, A.6    Chevalier, S.7
  • 30
    • 0029795243 scopus 로고    scopus 로고
    • Focal adhesion kinase (pp125FAK) expression, activation and association with paxillin and p50CSK in human metastatic prostate cancer
    • Tremblay L, Hauck W, Aprikian AG, Begin LR, Chapdelaine A, Chevalier S,. Focal adhesion kinase (pp125FAK) expression, activation and association with paxillin and p50CSK in human metastatic prostate cancer. Int J Cancer 1996; 68: 164-171.
    • (1996) Int J Cancer , vol.68 , pp. 164-171
    • Tremblay, L.1    Hauck, W.2    Aprikian, A.G.3    Begin, L.R.4    Chapdelaine, A.5    Chevalier, S.6
  • 31
    • 0030787791 scopus 로고    scopus 로고
    • Bombesin stimulates the motility of human prostate-carcinoma cells through tyrosine phosphorylation of focal adhesion kinase and of integrin-associated proteins
    • Aprikian AG, Tremblay L, Han K, Chevalier S,. Bombesin stimulates the motility of human prostate-carcinoma cells through tyrosine phosphorylation of focal adhesion kinase and of integrin-associated proteins. Int J Cancer 1997; 72: 498-504.
    • (1997) Int J Cancer , vol.72 , pp. 498-504
    • Aprikian, A.G.1    Tremblay, L.2    Han, K.3    Chevalier, S.4
  • 32
    • 0030005414 scopus 로고    scopus 로고
    • Actin disruption inhibits bombesin stimulation of focal adhesion kinase (pp125FAK) in prostate carcinoma
    • Duncan MD, Harmon JW, Duncan LK,. Actin disruption inhibits bombesin stimulation of focal adhesion kinase (pp125FAK) in prostate carcinoma. J Surg Res 1996; 63: 359-363.
    • (1996) J Surg Res , vol.63 , pp. 359-363
    • Duncan, M.D.1    Harmon, J.W.2    Duncan, L.K.3
  • 33
    • 0037031878 scopus 로고    scopus 로고
    • Role for 18:1 lysophosphatidic acid as an autocrine mediator in prostate cancer cells
    • Xie Y, Gibbs TC, Mukhin Y, Meier KE,. Role for 18:1 lysophosphatidic acid as an autocrine mediator in prostate cancer cells. J Biol Chem 2002; 277: 32516-32526.
    • (2002) J Biol Chem , vol.277 , pp. 32516-32526
    • Xie, Y.1    Gibbs, T.C.2    Mukhin, Y.3    Meier, K.E.4
  • 34
    • 18144389798 scopus 로고    scopus 로고
    • Focal adhesion kinase is required for bombesin-induced prostate cancer cell motility
    • Lacoste J, Aprikian AG, Chevalier S,. Focal adhesion kinase is required for bombesin-induced prostate cancer cell motility. Mol Cell Endocrinol 2005; 235: 51-61.
    • (2005) Mol Cell Endocrinol , vol.235 , pp. 51-61
    • Lacoste, J.1    Aprikian, A.G.2    Chevalier, S.3
  • 35
    • 0041633860 scopus 로고    scopus 로고
    • Calpain-2 as a target for limiting prostate cancer invasion
    • Mamoune A, Luo JH, Lauffenburger DA, Wells A,. Calpain-2 as a target for limiting prostate cancer invasion. Canc Res 2003; 63: 4532-4640.
    • (2003) Canc Res , vol.63 , pp. 4532-4640
    • Mamoune, A.1    Luo, J.H.2    Lauffenburger, D.A.3    Wells, A.4
  • 36
    • 0030048709 scopus 로고    scopus 로고
    • Meier KE Synergistic effects of insulin and phorbol ester on mitogen-activated protein kinase in Rat-1 HIR cells
    • Knoepp SM, Wisehart-Johnson AE, Buse MG, Bradshaw CD, Ella KM,. Meier KE Synergistic effects of insulin and phorbol ester on mitogen-activated protein kinase in Rat-1 HIR cells. J Biol Chem 1996; 271: 1678-1686.
    • (1996) J Biol Chem , vol.271 , pp. 1678-1686
    • Knoepp, S.M.1    Wisehart-Johnson, A.E.2    Buse, M.G.3    Bradshaw, C.D.4    Ella, K.M.5
  • 37
    • 0036357414 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of paxillin, FAK, and p130CAS: Effects on cell spreading and migration
    • Panetti TS,. Tyrosine phosphorylation of paxillin, FAK, and p130CAS: Effects on cell spreading and migration. Front Biosci 2002; 7: d143-d150.
    • (2002) Front Biosci , vol.7
    • Panetti, T.S.1
  • 38
    • 0031047981 scopus 로고    scopus 로고
    • Complexes of focal adhesion kinase (FAK) and Crk-associated substrate (p130Cas) are elevated in cytoskeleton-associated fractions following adhesion and Src transformation
    • Polte TR, Hanks SK,. Complexes of focal adhesion kinase (FAK) and Crk-associated substrate (p130Cas) are elevated in cytoskeleton-associated fractions following adhesion and Src transformation. J Biol Chem 1997; 272: 5501-5509.
    • (1997) J Biol Chem , vol.272 , pp. 5501-5509
    • Polte, T.R.1    Hanks, S.K.2
  • 39
    • 5144223110 scopus 로고    scopus 로고
    • Cleavage of p130Cas in anoikis
    • Wei L, Yang Y, Zhang X, Yu Q,. Cleavage of p130Cas in anoikis. Cell Biochem 2003; 91: 325-336.
    • (2003) Cell Biochem , vol.91 , pp. 325-336
    • Wei, L.1    Yang, Y.2    Zhang, X.3    Yu, Q.4
  • 40
    • 0029925581 scopus 로고    scopus 로고
    • Thrombin stimulates association of src homology domain containing adaptor protein Nck with pp125FAK
    • Choudhury GG, Marra F, Abboud HE,. Thrombin stimulates association of src homology domain containing adaptor protein Nck with pp125FAK. Am J Physiol 1996; 270: 295-300.
    • (1996) Am J Physiol , vol.270 , pp. 295-300
    • Choudhury, G.G.1    Marra, F.2    Abboud, H.E.3
  • 41
    • 0031921101 scopus 로고    scopus 로고
    • Multiple Grb2-mediated integrin stimulated signaling pathways to ERK2/mitogen-activated protein kinase: Summation of both c-Src- and focal adhesion kinase-initiated tyrosine phosphorylation events
    • Schlaepfer DD, Jones KC, Hunter T,. Multiple Grb2-mediated integrin stimulated signaling pathways to ERK2/mitogen-activated protein kinase: Summation of both c-Src- and focal adhesion kinase-initiated tyrosine phosphorylation events. Mol Cell Biol 1998; 18: 2571-2585.
    • (1998) Mol Cell Biol , vol.18 , pp. 2571-2585
    • Schlaepfer, D.D.1    Jones, K.C.2    Hunter, T.3
  • 44
    • 0028143317 scopus 로고
    • The role of calcium, pH, and cell proliferation in the programmed (apoptotic) death of androgen-independent prostatic cancer cells induced by thapsigargin
    • Furuya Y, Lundmo P, Short AD, Gill DL, Isaacs JT,. The role of calcium, pH, and cell proliferation in the programmed (apoptotic) death of androgen-independent prostatic cancer cells induced by thapsigargin. Canc Res 1994; 54: 6167-6175.
    • (1994) Canc Res , vol.54 , pp. 6167-6175
    • Furuya, Y.1    Lundmo, P.2    Short, A.D.3    Gill, D.L.4    Isaacs, J.T.5
  • 46
    • 69449095279 scopus 로고    scopus 로고
    • Signal transduction responses to lysophosphatidic acid and sphingosine 1-phosphate in human prostate cancer cells
    • Gibbs TC, Rubio MV, Zhang Z, Xie X, Kipp KR, Meier KE,. Signal transduction responses to lysophosphatidic acid and sphingosine 1-phosphate in human prostate cancer cells. Prostate 2009; 69: 1493-1506.
    • (2009) Prostate , vol.69 , pp. 1493-1506
    • Gibbs, T.C.1    Rubio, M.V.2    Zhang, Z.3    Xie, X.4    Kipp, K.R.5    Meier, K.E.6
  • 48
    • 0030889054 scopus 로고    scopus 로고
    • Syndecan-4 proteoglycan regulates the distribution and activity of protein kinase C
    • Oh ES, Woods A, Couchman JR,. Syndecan-4 proteoglycan regulates the distribution and activity of protein kinase C. J Biol Chem 1997; 272: 8133-8136.
    • (1997) J Biol Chem , vol.272 , pp. 8133-8136
    • Oh, E.S.1    Woods, A.2    Couchman, J.R.3
  • 49
  • 50
    • 0030793696 scopus 로고    scopus 로고
    • Adhesion of fibroblasts to fibronectin stimulates both serine and tyrosine phosphorylation of paxillin
    • Bellis SL, Perotta JA, Curtis MS, Turner CE,. Adhesion of fibroblasts to fibronectin stimulates both serine and tyrosine phosphorylation of paxillin. Biochem J 1997; 325: 375-381.
    • (1997) Biochem J , vol.325 , pp. 375-381
    • Bellis, S.L.1    Perotta, J.A.2    Curtis, M.S.3    Turner, C.E.4
  • 51
    • 0030944686 scopus 로고    scopus 로고
    • Paxillin is tyrosine-phosphorylated by and preferentially associates with the calcium-dependent tyrosine kinase in rat liver epithelial cells
    • Li X, Earp HS,. Paxillin is tyrosine-phosphorylated by and preferentially associates with the calcium-dependent tyrosine kinase in rat liver epithelial cells. J Biol Chem 1997; 272: 14341-14348.
    • (1997) J Biol Chem , vol.272 , pp. 14341-14348
    • Li, X.1    Earp, H.S.2
  • 52
    • 0034646637 scopus 로고    scopus 로고
    • Phosphorylation of paxillin via the ERK mitogen-activated protein kinase cascade in EL4 thymoma cells
    • Ku H, Meier KE,. Phosphorylation of paxillin via the ERK mitogen-activated protein kinase cascade in EL4 thymoma cells. J Biol Chem 2000; 275: 11333-11340.
    • (2000) J Biol Chem , vol.275 , pp. 11333-11340
    • Ku, H.1    Meier, K.E.2
  • 53
    • 0027089685 scopus 로고
    • Modulation of cellular signals by calpain
    • Suzuki K, Saiodo TC, Hirai S,. Modulation of cellular signals by calpain. Ann NY Acad Sci 1992; 674: 218-227.
    • (1992) Ann NY Acad Sci , vol.674 , pp. 218-227
    • Suzuki, K.1    Saiodo, T.C.2    Hirai, S.3
  • 54
    • 0028216630 scopus 로고
    • Protein kinase C V3 domain mutants with differential sensitivities to m-calpain are not resistant to phorbol-ester-induced down-regulation
    • Junco M, Webster C, Crawford C, Bosca L, Parker PJ,. Protein kinase C V3 domain mutants with differential sensitivities to m-calpain are not resistant to phorbol-ester-induced down-regulation. Eur J Biochem 1994; 223: 259-263.
    • (1994) Eur J Biochem , vol.223 , pp. 259-263
    • Junco, M.1    Webster, C.2    Crawford, C.3    Bosca, L.4    Parker, P.J.5
  • 55
    • 21844442832 scopus 로고    scopus 로고
    • Biologically active milli-calpain associated with caveolae is involved in a spatially compartmentalised signalling involving protein kinase C alpha and myristoylated alanine-rich C-kinase substrate (MARCKS)
    • Goudenege S, Poussard S, Dulong S, Cottin P,. Biologically active milli-calpain associated with caveolae is involved in a spatially compartmentalised signalling involving protein kinase C alpha and myristoylated alanine-rich C-kinase substrate (MARCKS). Int J Biochem Cell Biol 2005; 37: 1900-1910.
    • (2005) Int J Biochem Cell Biol , vol.37 , pp. 1900-1910
    • Goudenege, S.1    Poussard, S.2    Dulong, S.3    Cottin, P.4
  • 56
    • 0027258640 scopus 로고
    • Pp60src is an endogenous substrate for calpain in human blood platelets
    • Oda A, Druker BJ, Ariyoshi H, Smith M, Salzman EW,. pp60src is an endogenous substrate for calpain in human blood platelets. J Biol Chem 1993; 68: 12603-12608.
    • (1993) J Biol Chem , vol.68 , pp. 12603-12608
    • Oda, A.1    Druker, B.J.2    Ariyoshi, H.3    Smith, M.4    Salzman, E.W.5
  • 57
    • 0029666503 scopus 로고    scopus 로고
    • P120c-cbl is present in human blood platelets and is differentially involved in signaling by thrombopoietin and thrombin
    • Oda A, Ozaki K, Druker BJ, Miyakawa Y, Miyazaki H, Handa M, Morita H, Ohashi H, Ikeda Y,. p120c-cbl is present in human blood platelets and is differentially involved in signaling by thrombopoietin and thrombin. Blood 1996; 88: 1330-1338.
    • (1996) Blood , vol.88 , pp. 1330-1338
    • Oda, A.1    Ozaki, K.2    Druker, B.J.3    Miyakawa, Y.4    Miyazaki, H.5    Handa, M.6    Morita, H.7    Ohashi, H.8    Ikeda, Y.9
  • 58
    • 0028034082 scopus 로고
    • Unphosphorylated and tyrosine-phosphorylated forms of a focal adhesion protein, paxillin, are substrates for calpain II in vitro: Implications for the possible involvement of calpain II in mitosis-specific degradation of paxillin
    • Yamaguchi R, Maki M, Hatanaka M, Sabe H,. Unphosphorylated and tyrosine-phosphorylated forms of a focal adhesion protein, paxillin, are substrates for calpain II in vitro: implications for the possible involvement of calpain II in mitosis-specific degradation of paxillin. FEBS Lett 1994; 356: 114-116.
    • (1994) FEBS Lett , vol.356 , pp. 114-116
    • Yamaguchi, R.1    Maki, M.2    Hatanaka, M.3    Sabe, H.4
  • 59
    • 4043077024 scopus 로고    scopus 로고
    • Isoform specific function of calpain 2 in regulating membrane protrusion
    • Franco S, Perrin B, Huttenlocher A,. Isoform specific function of calpain 2 in regulating membrane protrusion. Exp Cell Res 2004; 299: 179-187.
    • (2004) Exp Cell Res , vol.299 , pp. 179-187
    • Franco, S.1    Perrin, B.2    Huttenlocher, A.3
  • 61
    • 0028088153 scopus 로고
    • Calpain: New perspectives in molecular diversity and physiological- pathological involvement
    • Saido TC, Sorimachi H, Suzuki K,. Calpain: New perspectives in molecular diversity and physiological-pathological involvement. FASEB J 1994; 8: 814-822.
    • (1994) FASEB J , vol.8 , pp. 814-822
    • Saido, T.C.1    Sorimachi, H.2    Suzuki, K.3
  • 65
    • 0029093670 scopus 로고
    • The chemotactic response to PDGF-BB: Evidence of a role for Ras
    • Kundra V, Anand-Apte B, Feig LA, Zetter BR,. The chemotactic response to PDGF-BB: Evidence of a role for Ras. J Cell Biol 1995; 130: 725-731.
    • (1995) J Cell Biol , vol.130 , pp. 725-731
    • Kundra, V.1    Anand-Apte, B.2    Feig, L.A.3    Zetter, B.R.4
  • 66
    • 0031455169 scopus 로고    scopus 로고
    • Calcium-dependent signaling pathways in T cells. Potential role of calpain, protein tyrosine phosphatase 1b, and p130Cas in integrin-mediated signaling events
    • Rock MT, Brooks WH, Roszman TL,. Calcium-dependent signaling pathways in T cells. Potential role of calpain, protein tyrosine phosphatase 1b, and p130Cas in integrin-mediated signaling events. J Biol Chem 1997; 272: 33377-33383.
    • (1997) J Biol Chem , vol.272 , pp. 33377-33383
    • Rock, M.T.1    Brooks, W.H.2    Roszman, T.L.3
  • 67
    • 0030845292 scopus 로고    scopus 로고
    • Calpain regulation of cytoskeletal signaling complexes in von Willebrand factor-stimulated platelets
    • Yuan Y, Dopheide SM, Ivanidis C, Salem HH, Jackson SP,. Calpain regulation of cytoskeletal signaling complexes in Von Willebrand factor-stimulated platelets. J Biol Chem 1997; 272: 21847-21854.
    • (1997) J Biol Chem , vol.272 , pp. 21847-21854
    • Yuan, Y.1    Dopheide, S.M.2    Ivanidis, C.3    Salem, H.H.4    Jackson, S.P.5
  • 69
    • 0032536543 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of focal adhesion kinase pp125FAK and disassembly of focal adhesions in human endothelial cell apoptosis
    • Levkau B, Herren B, Koyama H, Ross R, Raines EW,. Caspase-mediated cleavage of focal adhesion kinase pp125FAK and disassembly of focal adhesions in human endothelial cell apoptosis. J Exp Med 1998; 187: 579-586.
    • (1998) J Exp Med , vol.187 , pp. 579-586
    • Levkau, B.1    Herren, B.2    Koyama, H.3    Ross, R.4    Raines, E.W.5
  • 70
    • 0032549670 scopus 로고    scopus 로고
    • Caspase-dependent cleavage of signaling proteins during apoptosis. A turn-off mechanism for anti-apoptotic signals
    • Widmann C, Gibson S, Johnson GL,. Caspase-dependent cleavage of signaling proteins during apoptosis. A turn-off mechanism for anti-apoptotic signals. J Biol Chem 1998; 273: 7141-7147.
    • (1998) J Biol Chem , vol.273 , pp. 7141-7147
    • Widmann, C.1    Gibson, S.2    Johnson, G.L.3
  • 72
    • 0031032041 scopus 로고    scopus 로고
    • The Nck SH2/SH3 adaptor protein is present in the nucleus and associates with the nuclear protein SAM68
    • Lawe DC, Hahn C, Wong AJ,. The Nck SH2/SH3 adaptor protein is present in the nucleus and associates with the nuclear protein SAM68. Oncogene 1997; 14: 223-231.
    • (1997) Oncogene , vol.14 , pp. 223-231
    • Lawe, D.C.1    Hahn, C.2    Wong, A.J.3
  • 73
    • 77951184829 scopus 로고    scopus 로고
    • Cellular functions of FAK kinases: Insight into molecular mechanisms and novel functions
    • Schaller MD,. Cellular functions of FAK kinases: Insight into molecular mechanisms and novel functions. J Cell Sci 2010; 123: 1007-1013.
    • (2010) J Cell Sci , vol.123 , pp. 1007-1013
    • Schaller, M.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.