메뉴 건너뛰기




Volumn 165, Issue 6, 2004, Pages 893-902

Cell-matrix interaction via CD44 is independently regulated by different metalloproteinases activated in response to extracellular Ca2+ influx and PKC activation

Author keywords

ADAM10; ADAM17; Calmodulin; CD44; Rac

Indexed keywords

ADAM 10 PROTEIN; ADAM PROTEIN; CALCIUM ION; CALMODULIN; CELL ADHESION MOLECULE; FIBRONECTIN; GUANOSINE TRIPHOSPHATASE; HERMES ANTIGEN; HYALURONIC ACID; METALLOPROTEINASE; PHORBOL ESTER; PROTEIN; PROTEIN KINASE C; RAC PROTEIN; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME; UNCLASSIFIED DRUG;

EID: 3042554386     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200310024     Document Type: Article
Times cited : (251)

References (44)
  • 3
    • 0035430436 scopus 로고    scopus 로고
    • Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases
    • Anders, A., S. Gilbert, W. Garten, R. Postina, and F. Fahrenholz. 2001. Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases. FASEB J. 15:1837-1839.
    • (2001) FASEB J. , vol.15 , pp. 1837-1839
    • Anders, A.1    Gilbert, S.2    Garten, W.3    Postina, R.4    Fahrenholz, F.5
  • 4
    • 0025282411 scopus 로고
    • CD44 is the principal cell surface receptor for hyaluronate
    • Aruffo, A., I. Stamenkovic, M. Melnick, C.B. Underhill, and B. Seed. 1990. CD44 is the principal cell surface receptor for hyaluronate. Cell. 61:1303-1313.
    • (1990) Cell , vol.61 , pp. 1303-1313
    • Aruffo, A.1    Stamenkovic, I.2    Melnick, M.3    Underhill, C.B.4    Seed, B.5
  • 5
    • 0036304655 scopus 로고    scopus 로고
    • Polarized calcium and calmodulin signaling in secretory epithelia
    • Ashby, M.C., and A.V. Tepikin. 2002. Polarized calcium and calmodulin signaling in secretory epithelia. Physiol. Rev. 82:701-734.
    • (2002) Physiol. Rev. , vol.82 , pp. 701-734
    • Ashby, M.C.1    Tepikin, A.V.2
  • 6
    • 0034695446 scopus 로고    scopus 로고
    • CD44 interaction with tiam1 promotes Rac1 signaling and hyaluronic acid-mediated breast tumor cell migration
    • Bourguignon, L.Y., H. Zhu, L. Shao, and Y.W. Chen. 2000. CD44 interaction with tiam1 promotes Rac1 signaling and hyaluronic acid-mediated breast tumor cell migration. J. Biol. Chem. 275:1829-1838.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1829-1838
    • Bourguignon, L.Y.1    Zhu, H.2    Shao, L.3    Chen, Y.W.4
  • 7
    • 0842281652 scopus 로고    scopus 로고
    • Rho and Rac take center stage
    • Burridge, K., and K. Wennerberg. 2004. Rho and Rac take center stage. Cell. 116: 167-179.
    • (2004) Cell , vol.116 , pp. 167-179
    • Burridge, K.1    Wennerberg, K.2
  • 8
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor
    • Buxbaum, J.D., K.N. Liu, Y. Luo, J.L. Slack, K.L. Stocking, J.J. Peschon, R.S. Johnson, B.J. Castner, D.P. Cerretti, and R.A. Black. 1998. Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor, J. Biol. Chem. 273:27765-27767.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27765-27767
    • Buxbaum, J.D.1    Liu, K.N.2    Luo, Y.3    Slack, J.L.4    Stocking, K.L.5    Peschon, J.J.6    Johnson, R.S.7    Castner, B.J.8    Cerretti, D.P.9    Black, R.A.10
  • 9
    • 0037780985 scopus 로고    scopus 로고
    • The liberation of CD44
    • Cichy, J., and E. Pure. 2003. The liberation of CD44. J. Cell Biol. 161:839-843.
    • (2003) J. Cell Biol. , vol.161 , pp. 839-843
    • Cichy, J.1    Pure, E.2
  • 10
    • 0033551228 scopus 로고    scopus 로고
    • Hormone-induced secretory and nuclear translocation of calmodulin: Oscillations of calmodulin concentration with the nucleus as an integrator
    • Craske, M., T. Takeo, O. Gerasimenko, C. Vaillant, K. Torok, O.H. Petersen, and A.V. Tepikin. 1999. Hormone-induced secretory and nuclear translocation of calmodulin: oscillations of calmodulin concentration with the nucleus as an integrator. Proc. Natl. Acad. Sci. USA. 96:4426-4431.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4426-4431
    • Craske, M.1    Takeo, T.2    Gerasimenko, O.3    Vaillant, C.4    Torok, K.5    Petersen, O.H.6    Tepikin, A.V.7
  • 11
    • 0032079871 scopus 로고    scopus 로고
    • Extracellular calcium influx stimulates metalloproteinase cleavage and secretion of heparin-binding EGF-like growth factor independently of protein kinase C
    • Dethlefsen, S.M., G. Raab, M.A. Moses, R.M. Adam, M. Magsbrun, and M.R. Freeman. 1998. Extracellular calcium influx stimulates metalloproteinase cleavage and secretion of heparin-binding EGF-like growth factor independently of protein kinase C. J. Cell. Biochem. 69:143-153.
    • (1998) J. Cell. Biochem. , vol.69 , pp. 143-153
    • Dethlefsen, S.M.1    Raab, G.2    Moses, M.A.3    Adam, R.M.4    Magsbrun, M.5    Freeman, M.R.6
  • 13
    • 0035985185 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: A potential role in regulated shedding
    • Diaz-Rodriguez, E., J.C. Montero, A. Esparis-Ogando, L. Yuste, and A. Pandiella. 2002. Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding. Mol. Biol. Cell. 13:2031-2044.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2031-2044
    • Diaz-Rodriguez, E.1    Montero, J.C.2    Esparis-Ogando, A.3    Yuste, L.4    Pandiella, A.5
  • 14
    • 0043095391 scopus 로고    scopus 로고
    • TACE/ADAM-17 enzymatic activity is increased in response to cellular stimulation
    • Doedens, J.R., R.M. Mahimkar, and R.A. Black. 2003. TACE/ADAM-17 enzymatic activity is increased in response to cellular stimulation. Biochem. Biophys. Res. Commun. 308:331-338.
    • (2003) Biochem. Biophys. Res. Commun. , vol.308 , pp. 331-338
    • Doedens, J.R.1    Mahimkar, R.M.2    Black, R.A.3
  • 18
    • 0042237924 scopus 로고    scopus 로고
    • The disintegrin-like metalloproteinase ADAM 10 is involved in constitutive cleavage of CX3CL1 (fractalkine) and regulates CX3CL1-mediated cell-cell adhesion
    • Hundhausen, C., D. Misztela, T.A. Berkhout, N. Broadway, P. Saftig, K. Reiss, D. Hartmann, F. Fahrenholz, R. Postina, V. Matthews, et al. 2003. The disintegrin-like metalloproteinase ADAM 10 is involved in constitutive cleavage of CX3CL1 (fractalkine) and regulates CX3CL1-mediated cell-cell adhesion. Blood. 102:1186-1195.
    • (2003) Blood , vol.102 , pp. 1186-1195
    • Hundhausen, C.1    Misztela, D.2    Berkhout, T.A.3    Broadway, N.4    Saftig, P.5    Reiss, K.6    Hartmann, D.7    Fahrenholz, F.8    Postina, R.9    Matthews, V.10
  • 19
    • 0033604454 scopus 로고    scopus 로고
    • Calcium influx triggers the sequential proteolysis of extracellular and cytoplasmic domains of E-cadherin, leading to loss of beta-catenin from cell-cell contacts
    • Ito, K., I. Okamoto, N. Araki, Y. Kawano, M. Nakao, S. Fujiyama, K. Tomita, T. Mimori, and H. Saya. 1999. Calcium influx triggers the sequential proteolysis of extracellular and cytoplasmic domains of E-cadherin, leading to loss of beta-catenin from cell-cell contacts. Oncogene. 18:7080-7090.
    • (1999) Oncogene , vol.18 , pp. 7080-7090
    • Ito, K.1    Okamoto, I.2    Araki, N.3    Kawano, Y.4    Nakao, M.5    Fujiyama, S.6    Tomita, K.7    Mimori, T.8    Saya, H.9
  • 20
    • 0032549712 scopus 로고    scopus 로고
    • Calmodulin regulates L-selectin adhesion molecule expression and function through a protease-dependent mechanism
    • Kahn, J., B. Walcheck, G.I. Migaki, M.A. Jutila, and T.K. Kishimoto. 1998. Calmodulin regulates L-selectin adhesion molecule expression and function through a protease-dependent mechanism. Cell. 92:809-818.
    • (1998) Cell , vol.92 , pp. 809-818
    • Kahn, J.1    Walcheck, B.2    Migaki, G.I.3    Jutila, M.A.4    Kishimoto, T.K.5
  • 21
    • 0035947766 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloptoteinase cleaves CD44 and promotes cell migration
    • Kajita, M., Y. Itoh, T. Chiba, H. Moti, A. Okada, H. Kinoh, and M. Seiki. 2001. Membrane-type 1 matrix metalloptoteinase cleaves CD44 and promotes cell migration. J. Cell Biol. 153:893-904.
    • (2001) J. Cell Biol. , vol.153 , pp. 893-904
    • Kajita, M.1    Itoh, Y.2    Chiba, T.3    Moti, H.4    Okada, A.5    Kinoh, H.6    Seiki, M.7
  • 22
    • 0034703063 scopus 로고    scopus 로고
    • Ras oncoptotein induces CD44 cleavage through phosphoinositide 3-OH kinase and the rho family of small G proteins
    • Kawano, Y., I. Okamoto, D. Murakami, H. Itoh, M. Yoshida, S. Ueda, and H. Saya. 2000. Ras oncoptotein induces CD44 cleavage through phosphoinositide 3-OH kinase and the rho family of small G proteins. J. Biol. Chem. 275:29628-29635.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29628-29635
    • Kawano, Y.1    Okamoto, I.2    Murakami, D.3    Itoh, H.4    Yoshida, M.5    Ueda, S.6    Saya, H.7
  • 24
    • 0033595232 scopus 로고    scopus 로고
    • Regulation of cell movement is mediated by stretch-activated calcium channels
    • Lee, J., A. Ishihara, G. Oxford, B. Johnson, and K. Jacobson. 1999. Regulation of cell movement is mediated by stretch-activated calcium channels. Nature. 400:382-386.
    • (1999) Nature , vol.400 , pp. 382-386
    • Lee, J.1    Ishihara, A.2    Oxford, G.3    Johnson, B.4    Jacobson, K.5
  • 25
    • 0001286055 scopus 로고    scopus 로고
    • CD44 structure and function
    • Lesley, J., and R. Hyman. 1998. CD44 structure and function. Front. Biosci. 3:D616-D630.
    • (1998) Front. Biosci. , vol.3
    • Lesley, J.1    Hyman, R.2
  • 27
    • 0031973304 scopus 로고    scopus 로고
    • Cytosolic calmodulin is increased in SK-N-SH human neuroblastoma cells due to release of calcium from intracellular stores
    • McGinnis, K.M., Z. Shariat-Madar, and M.E. Gnegy. 1998. Cytosolic calmodulin is increased in SK-N-SH human neuroblastoma cells due to release of calcium from intracellular stores. J. Neurochem. 70:139-146.
    • (1998) J. Neurochem. , vol.70 , pp. 139-146
    • McGinnis, K.M.1    Shariat-Madar, Z.2    Gnegy, M.E.3
  • 29
    • 0035074356 scopus 로고    scopus 로고
    • Shedding of c-Met is regulated by crosstalk between a G-protein coupled receptor and the EGF receptor and is mediated by a TIMP-3 sensitive metalloproteinase
    • Nath, D., N.J. Williamson, R. Jarvis, and G. Murphy. 2001. Shedding of c-Met is regulated by crosstalk between a G-protein coupled receptor and the EGF receptor and is mediated by a TIMP-3 sensitive metalloproteinase. J. Cell Sci. 114:1213-1220.
    • (2001) J. Cell Sci. , vol.114 , pp. 1213-1220
    • Nath, D.1    Williamson, N.J.2    Jarvis, R.3    Murphy, G.4
  • 30
    • 0033520361 scopus 로고    scopus 로고
    • Regulated CD44 cleavage under the control of protein kinase C, calcium influx, and the Rho family of small G proteins
    • Okamoto, I., Y. Kawano, M. Matsumoto, M. Suga, K. Kaibuchi, M. Ando, and H. Saya. 1999a. Regulated CD44 cleavage under the control of protein kinase C, calcium influx, and the Rho family of small G proteins. J. Biol. Chem. 274:25525-25534.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25525-25534
    • Okamoto, I.1    Kawano, Y.2    Matsumoto, M.3    Suga, M.4    Kaibuchi, K.5    Ando, M.6    Saya, H.7
  • 35
    • 0030198503 scopus 로고    scopus 로고
    • CD44 phosphorylation regulates melanoma cell and fibroblast migration on, but not attachment to, a hyaluronan substratum
    • Peck, D., and Isacke. 1996. CD44 phosphorylation regulates melanoma cell and fibroblast migration on, but not attachment to, a hyaluronan substratum. Curr. Biol. 6:884-890.
    • (1996) Curr. Biol. , vol.6 , pp. 884-890
    • Peck, D.1    Isacke2
  • 38
    • 0032741143 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: Modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding
    • Schlondorff, J., and C.P. Blobel. 1999. Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding. J. Cell Sci. 112:3603-3617.
    • (1999) J. Cell Sci. , vol.112 , pp. 3603-3617
    • Schlondorff, J.1    Blobel, C.P.2
  • 39
    • 0021175468 scopus 로고
    • Control of cell shape and locomotion by external calcium
    • Strohmeier, R., and J. Bereiter-Hahn. 1984. Control of cell shape and locomotion by external calcium. Exp. Cell Res. 154:412-420.
    • (1984) Exp. Cell Res. , vol.154 , pp. 412-420
    • Strohmeier, R.1    Bereiter-Hahn, J.2
  • 41
    • 0041589199 scopus 로고    scopus 로고
    • Intracellular coupling via limiting calmodulin
    • Tran, Q.K., D.J. Black, and A. Persechini. 2003. Intracellular coupling via limiting calmodulin. J. Biol. Chem. 278:24247-24250.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24247-24250
    • Tran, Q.K.1    Black, D.J.2    Persechini, A.3
  • 42
    • 0035851151 scopus 로고    scopus 로고
    • The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein
    • Vincent, B., E. Paitel, P. Saftig, Y. Frobert, D. Hartmann, B. De Strooper, J. Grassi, E. Lopez-Perez, and F. Checler. 2001. The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein. J. Biol. Chem. 276:37743-37746.
    • (2001) J. Biol. Chem. , vol.276 , pp. 37743-37746
    • Vincent, B.1    Paitel, E.2    Saftig, P.3    Frobert, Y.4    Hartmann, D.5    De Strooper, B.6    Grassi, J.7    Lopez-Perez, E.8    Checler, F.9
  • 43
    • 0037157854 scopus 로고    scopus 로고
    • The metalloprotease Kuzbanian (ADAM10) mediates the transactivation of EGF receptor by G protein-coupled receptors
    • Yan, Y., K. Shirakabe, and Z. Werb. 2002. The metalloprotease Kuzbanian (ADAM10) mediates the transactivation of EGF receptor by G protein-coupled receptors. J. Cell Biol. 158:221-226.
    • (2002) J. Cell Biol. , vol.158 , pp. 221-226
    • Yan, Y.1    Shirakabe, K.2    Werb, Z.3
  • 44
    • 0030789748 scopus 로고    scopus 로고
    • Calcium influx inhibits MT1-MMP processing and blocks MMP-2 activation
    • Yu, M., H. Sato, M. Seiki, S. Spiegel, and E.W. Thompson. 1997. Calcium influx inhibits MT1-MMP processing and blocks MMP-2 activation. FEBS Lett. 412:568-572.
    • (1997) FEBS Lett. , vol.412 , pp. 568-572
    • Yu, M.1    Sato, H.2    Seiki, M.3    Spiegel, S.4    Thompson, E.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.