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Volumn 101, Issue 5, 2007, Pages 1222-1237

Roles of MMP/TIMP in regulating matrix swelling and cell migration during chick corneal development

Author keywords

ADAM10; CD44v6; Cell migration; Corneal development; Ectodomain cleavage; Extracellular matrix; Matrix metalloproteinases; MT3 MMP

Indexed keywords

ADAM PROTEIN; CD44V6 ANTIGEN; COLLAGEN FIBER; COLLAGEN TYPE 9; COLLAGENASE 3; GELATINASE A; MATRIX METALLOPROTEINASE; TISSUE INHIBITOR OF METALLOPROTEINASE; TISSUE INHIBITOR OF METALLOPROTEINASE 1;

EID: 34547917186     PISSN: 07302312     EISSN: 10974644     Source Type: Journal    
DOI: 10.1002/jcb.21246     Document Type: Article
Times cited : (23)

References (76)
  • 1
  • 2
    • 0029896682 scopus 로고    scopus 로고
    • Expression and function of matrix metalloproteinases and their inhibitors at the maternal-embryonic boundary during mouse embryo implantation
    • Alexander CM, Hansell EJ, Behrendtsen O, Flannery ML, Kishnani NS, Hawkes SP, Werb Z. 1996. Expression and function of matrix metalloproteinases and their inhibitors at the maternal-embryonic boundary during mouse embryo implantation. Development 122:1723-1736.
    • (1996) Development , vol.122 , pp. 1723-1736
    • Alexander, C.M.1    Hansell, E.J.2    Behrendtsen, O.3    Flannery, M.L.4    Kishnani, N.S.5    Hawkes, S.P.6    Werb, Z.7
  • 4
    • 85011136111 scopus 로고
    • The behavior of fibroblasts from the developing avian cornea. Morphology and movement in situ and in vitro
    • Bard JB, Hay ED. 1975. The behavior of fibroblasts from the developing avian cornea. Morphology and movement in situ and in vitro. J Cell Biol 67:400-418.
    • (1975) J Cell Biol , vol.67 , pp. 400-418
    • Bard, J.B.1    Hay, E.D.2
  • 5
    • 0034731478 scopus 로고    scopus 로고
    • Localization of the death domain of tissue inhibitor of metalloproteinase-3 to the N terminus. Metalloproteinase inhibition is associated with proapoptotic activity
    • Bond M, Murphy G, Bennett MR, Amour A, Knauper V, Newby AC, Baker AH. 2000. Localization of the death domain of tissue inhibitor of metalloproteinase-3 to the N terminus. Metalloproteinase inhibition is associated with proapoptotic activity. J Biol Chem 275:41358-41363.
    • (2000) J Biol Chem , vol.275 , pp. 41358-41363
    • Bond, M.1    Murphy, G.2    Bennett, M.R.3    Amour, A.4    Knauper, V.5    Newby, A.C.6    Baker, A.H.7
  • 7
    • 0032127129 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1mut at the 'aggrecanase' and the MMP sites. Characterization of MT1-MMP catabolic activities on the interglobular domain of aggrecan
    • Buttner FH, Hughes CE, Margerie D, Lichte A, Tschesche H, Caterson B, Bartnik E. 1998. Membrane type 1 matrix metalloproteinase (MT1-MMP) cleaves the recombinant aggrecan substrate rAgg1mut at the 'aggrecanase' and the MMP sites. Characterization of MT1-MMP catabolic activities on the interglobular domain of aggrecan. Biochem J 333(Pt 1):159-165.
    • (1998) Biochem J , vol.333 , Issue.PART 1 , pp. 159-165
    • Buttner, F.H.1    Hughes, C.E.2    Margerie, D.3    Lichte, A.4    Tschesche, H.5    Caterson, B.6    Bartnik, E.7
  • 8
    • 0036022266 scopus 로고    scopus 로고
    • Synthetic matrix metalloproteinase inhibitor decreases early cardiac neural crest migration in chicken embryos
    • Cai DH, Brauer PR. 2002. Synthetic matrix metalloproteinase inhibitor decreases early cardiac neural crest migration in chicken embryos. Dev Dyn 224:441-449.
    • (2002) Dev Dyn , vol.224 , pp. 441-449
    • Cai, D.H.1    Brauer, P.R.2
  • 9
    • 0034935874 scopus 로고    scopus 로고
    • Nuclear translocation of ferritin in corneal epithelial cells
    • Cai CX, Linsenmayer TF. 2001. Nuclear translocation of ferritin in corneal epithelial cells. J Cell Sci 114:2327-2334.
    • (2001) J Cell Sci , vol.114 , pp. 2327-2334
    • Cai, C.X.1    Linsenmayer, T.F.2
  • 10
    • 0037780985 scopus 로고    scopus 로고
    • The liberation of CD44
    • Cichy J, Pure E. 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
  • 11
    • 0034255226 scopus 로고    scopus 로고
    • Expression of CD44 during early development of the chick embryo
    • Corbel C, Lehmann A, Davison F. 2000. Expression of CD44 during early development of the chick embryo. Mech Dev 96:111-114.
    • (2000) Mech Dev , vol.96 , pp. 111-114
    • Corbel, C.1    Lehmann, A.2    Davison, F.3
  • 12
    • 0003070439 scopus 로고
    • Corneal development. I. Corneal transparency
    • Coulombre AJ, Coulombre JL. 1958. Corneal development. I. Corneal transparency. J Cell Physiol 51:1-11.
    • (1958) J Cell Physiol , vol.51 , pp. 1-11
    • Coulombre, A.J.1    Coulombre, J.L.2
  • 13
    • 0142145947 scopus 로고
    • Corneal development. 3. The role of the thyroid in dehydration and the development of transparency
    • Coulombre AJ, Coulombre JL. 1964. Corneal development. 3. The role of the thyroid in dehydration and the development of transparency. Exp Eye Res 75:105-114.
    • (1964) Exp Eye Res , vol.75 , pp. 105-114
    • Coulombre, A.J.1    Coulombre, J.L.2
  • 14
    • 0032522576 scopus 로고    scopus 로고
    • Induction of matrix metalloproteinase activation cascades based on membrane-type 1 matrix metalloproteinase: Associated activation of gelatinase A, gelatinase B and collagenase 3
    • Cowell S, Knauper V, Stewart ML, D'Ortho MP, Stanton H, Hembry RM, Lopez-Otin C, Reynolds JJ, Murphy G. 1998. Induction of matrix metalloproteinase activation cascades based on membrane-type 1 matrix metalloproteinase: Associated activation of gelatinase A, gelatinase B and collagenase 3. Biochem J 331(Pt 2):453-458.
    • (1998) Biochem J , vol.331 , Issue.PART 2 , pp. 453-458
    • Cowell, S.1    Knauper, V.2    Stewart, M.L.3    D'Ortho, M.P.4    Stanton, H.5    Hembry, R.M.6    Lopez-Otin, C.7    Reynolds, J.J.8    Murphy, G.9
  • 17
    • 0035864376 scopus 로고    scopus 로고
    • MT1-MMP initiates activation of pro-MMP-2 and integrin alphav-beta3 promotes maturation of MMP-2 in breast carcinoma cells
    • Deryugina EI, Ratnikov B, Monosov E, Postnova TI, DiScipio R, Smith JW, Strongin AY. 2001. MT1-MMP initiates activation of pro-MMP-2 and integrin alphav-beta3 promotes maturation of MMP-2 in breast carcinoma cells. Exp Cell Res 263:209-223.
    • (2001) Exp Cell Res , vol.263 , pp. 209-223
    • Deryugina, E.I.1    Ratnikov, B.2    Monosov, E.3    Postnova, T.I.4    DiScipio, R.5    Smith, J.W.6    Strongin, A.Y.7
  • 18
    • 0029968263 scopus 로고    scopus 로고
    • Spatial and temporal variations in extracellular matrix of periocular and corneal regions during corneal stromal development
    • Doane KJ, Ting WH, McLaughlin JS, Birk DE. 1996. Spatial and temporal variations in extracellular matrix of periocular and corneal regions during corneal stromal development. Exp Eye Res 62:271-283.
    • (1996) Exp Eye Res , vol.62 , pp. 271-283
    • Doane, K.J.1    Ting, W.H.2    McLaughlin, J.S.3    Birk, D.E.4
  • 19
    • 0036024620 scopus 로고    scopus 로고
    • Pertubation of beta1 integrin function using anti-sense or function-blocking antibodies on corneal cells grown on fibronectin and tenascin
    • Doane KJ, Bhattacharya R, Marchant J. 2002. Pertubation of beta1 integrin function using anti-sense or function-blocking antibodies on corneal cells grown on fibronectin and tenascin. Cell Biol Int 26:131-144.
    • (2002) Cell Biol Int , vol.26 , pp. 131-144
    • Doane, K.J.1    Bhattacharya, R.2    Marchant, J.3
  • 20
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad M, Werb Z. 2002. New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2:161-174.
    • (2002) Nat Rev Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 21
    • 0031784501 scopus 로고    scopus 로고
    • Proteolytic mechanisms in corneal ulceration and repair
    • Fini ME, Cook JR, Mohan R. 1998a. Proteolytic mechanisms in corneal ulceration and repair. Arch Dermatol Res 290(Suppl 14):S12-S23.
    • (1998) Arch Dermatol Res , vol.290 , Issue.SUPPL. 14
    • Fini, M.E.1    Cook, J.R.2    Mohan, R.3
  • 22
    • 0003089209 scopus 로고    scopus 로고
    • Regulation of metrix metalloproteinase gene expression
    • Parks WC, Mecharm RP, editors, New York: Academic Press, pp
    • Fini ME, Cook JR, Mohan R, Brinckerhoff CE. 1998b. Regulation of metrix metalloproteinase gene expression. In: Parks WC, Mecharm RP, editors. Matrix metalloproteinases. New York: Academic Press, pp 299-356.
    • (1998) Matrix metalloproteinases , pp. 299-356
    • Fini, M.E.1    Cook, J.R.2    Mohan, R.3    Brinckerhoff, C.E.4
  • 23
    • 0031959089 scopus 로고    scopus 로고
    • Collagen type IX and developmentally regulated swelling of the avian primary corneal stroma
    • Fitch JM, Fini ME, Beebe DC, Linsenmayer TF. 1998. Collagen type IX and developmentally regulated swelling of the avian primary corneal stroma. Dev Dyn 212:27-37.
    • (1998) Dev Dyn , vol.212 , pp. 27-37
    • Fitch, J.M.1    Fini, M.E.2    Beebe, D.C.3    Linsenmayer, T.F.4
  • 24
    • 11244302902 scopus 로고    scopus 로고
    • Cellular invasion of the chicken corneal stroma during development: Regulation by multiple matrix metalloproteases and the lens
    • Fitch JM, Kidder JM, Linsenmayer TF. 2005. Cellular invasion of the chicken corneal stroma during development: Regulation by multiple matrix metalloproteases and the lens. Dev Dyn 232:106-118.
    • (2005) Dev Dyn , vol.232 , pp. 106-118
    • Fitch, J.M.1    Kidder, J.M.2    Linsenmayer, T.F.3
  • 25
    • 0032479462 scopus 로고    scopus 로고
    • Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggrecan interglobular domain
    • Fosang AJ, Last K, Fujii Y, Seiki M, Okada Y. 1998. Membrane-type 1 MMP (MMP-14) cleaves at three sites in the aggrecan interglobular domain. FEBS Lett 430:186-190.
    • (1998) FEBS Lett , vol.430 , pp. 186-190
    • Fosang, A.J.1    Last, K.2    Fujii, Y.3    Seiki, M.4    Okada, Y.5
  • 26
    • 0030717692 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: Structure, regulation and biological functions
    • Gomez DE, Alonso DF, Yoshiji H, Thorgeirsson UP. 1997. Tissue inhibitors of metalloproteinases: Structure, regulation and biological functions. Eur J Cell Biol 74:111-122.
    • (1997) Eur J Cell Biol , vol.74 , pp. 111-122
    • Gomez, D.E.1    Alonso, D.F.2    Yoshiji, H.3    Thorgeirsson, U.P.4
  • 27
    • 0037377036 scopus 로고    scopus 로고
    • ADAM 10: An active metalloprotease expressed during avian epithelial morphogenesis
    • Hall RJ, Erickson CA. 2003. ADAM 10: An active metalloprotease expressed during avian epithelial morphogenesis. Dev Biol 256:146-159.
    • (2003) Dev Biol , vol.256 , pp. 146-159
    • Hall, R.J.1    Erickson, C.A.2
  • 29
    • 0019306591 scopus 로고
    • Development of the vertebrate cornea
    • Hay ED. 1979. Development of the vertebrate cornea. Int Rev Cytol 63:263-322.
    • (1979) Int Rev Cytol , vol.63 , pp. 263-322
    • Hay, E.D.1
  • 30
    • 0014611096 scopus 로고
    • Fine structure of the developing avian cornea
    • Hay ED, Revel JP. 1969. Fine structure of the developing avian cornea. Monogr Dev Biol 1:1-144.
    • (1969) Monogr Dev Biol , vol.1 , pp. 1-144
    • Hay, E.D.1    Revel, J.P.2
  • 31
    • 0019943174 scopus 로고
    • Immunohistochemical localization of collagen types I and II in the developing chick cornea and tibia by electron microscopy
    • Hendrix MJ, Hay ED, von der Mark K, Linsenmayer TF. 1982. Immunohistochemical localization of collagen types I and II in the developing chick cornea and tibia by electron microscopy. Invest Ophthalmol Vis Sci 22:359-375.
    • (1982) Invest Ophthalmol Vis Sci , vol.22 , pp. 359-375
    • Hendrix, M.J.1    Hay, E.D.2    von der Mark, K.3    Linsenmayer, T.F.4
  • 32
    • 0035793638 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-2 (TIMP-2) suppresses TKR-growth factor signaling independent of metalloproteinase inhibition
    • Hoegy SE, Oh HR, Corcoran ML, Stetler-Stevenson WG. 2001. Tissue inhibitor of metalloproteinases-2 (TIMP-2) suppresses TKR-growth factor signaling independent of metalloproteinase inhibition. J Biol Chem 276:3203-3214.
    • (2001) J Biol Chem , vol.276 , pp. 3203-3214
    • Hoegy, S.E.1    Oh, H.R.2    Corcoran, M.L.3    Stetler-Stevenson, W.G.4
  • 35
    • 0036193222 scopus 로고    scopus 로고
    • Matrix metalloproteinases mediate the dismantling of mesenchymal structures in the tadpole tail during thyroid hormone-induced tail resorption
    • Jung JC, Leco KJ, Edwards DR, Fini ME. 2002. Matrix metalloproteinases mediate the dismantling of mesenchymal structures in the tadpole tail during thyroid hormone-induced tail resorption. Dev Dyn 223:402-413.
    • (2002) Dev Dyn , vol.223 , pp. 402-413
    • Jung, J.C.1    Leco, K.J.2    Edwards, D.R.3    Fini, M.E.4
  • 36
    • 0035947766 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration
    • Kajita M, Itoh Y, Chiba T, Mori H, Okada A, Kinoh H, Seiki M. 2001. Membrane-type 1 matrix metalloproteinase 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    Mori, H.4    Okada, A.5    Kinoh, H.6    Seiki, M.7
  • 37
    • 0037114003 scopus 로고    scopus 로고
    • Matrix metalloproteinase-dependent activation of latent transforming growth factor-beta controls the conversion of osteoblasts into osteocytes by blocking osteoblast apoptosis
    • Karsdal MA, Larsen L, Engsig MT, Lou H, Ferreras M, Lochter A, Delaisse JM, Foged NT. 2002. Matrix metalloproteinase-dependent activation of latent transforming growth factor-beta controls the conversion of osteoblasts into osteocytes by blocking osteoblast apoptosis. J Biol Chem 277:44061-44067.
    • (2002) J Biol Chem , vol.277 , pp. 44061-44067
    • Karsdal, M.A.1    Larsen, L.2    Engsig, M.T.3    Lou, H.4    Ferreras, M.5    Lochter, A.6    Delaisse, J.M.7    Foged, N.T.8
  • 38
    • 0035918309 scopus 로고    scopus 로고
    • TIMP-3 is a potent inhibitor of aggrecanase 1 (ADAM-TS4) and aggrecanase 2 (ADAM-TS5)
    • Kashiwagi M, Tortorella M, Nagase H, Brew K. 2001. TIMP-3 is a potent inhibitor of aggrecanase 1 (ADAM-TS4) and aggrecanase 2 (ADAM-TS5). J Biol Chem 276:12501-12504.
    • (2001) J Biol Chem , vol.276 , pp. 12501-12504
    • Kashiwagi, M.1    Tortorella, M.2    Nagase, H.3    Brew, K.4
  • 40
    • 0030037395 scopus 로고    scopus 로고
    • Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme
    • Knauper V, Will H, Lopez-Otin C, Smith B, Atkinson SJ, Stanton H, Hembry RM, Murphy G. 1996. Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme. J Biol Chem 271:17124-17131.
    • (1996) J Biol Chem , vol.271 , pp. 17124-17131
    • Knauper, V.1    Will, H.2    Lopez-Otin, C.3    Smith, B.4    Atkinson, S.J.5    Stanton, H.6    Hembry, R.M.7    Murphy, G.8
  • 41
    • 0030898796 scopus 로고    scopus 로고
    • The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction
    • Knauper V, Cowell S, Smith B, Lopez-Otin C, O'Shea M, Morris H, Zardi L, Murphy G. 1997. The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction. J Biol Chem 272:7608-7616.
    • (1997) J Biol Chem , vol.272 , pp. 7608-7616
    • Knauper, V.1    Cowell, S.2    Smith, B.3    Lopez-Otin, C.4    O'Shea, M.5    Morris, H.6    Zardi, L.7    Murphy, G.8
  • 42
    • 0034614939 scopus 로고    scopus 로고
    • Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5
    • Koshikawa N, Giannelli G, Cirulli V, Miyazaki K, Quaranta V. 2000. Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5. J Cell Biol 148:615-624.
    • (2000) J Cell Biol , vol.148 , pp. 615-624
    • Koshikawa, N.1    Giannelli, G.2    Cirulli, V.3    Miyazaki, K.4    Quaranta, V.5
  • 43
    • 0036928241 scopus 로고    scopus 로고
    • Association of type XII collagen with regions of increased stability and keratocyte density in the cornea
    • Marchant JK, Zhang G, Birk DE. 2002. Association of type XII collagen with regions of increased stability and keratocyte density in the cornea. Exp Eye Res 75:683-694.
    • (2002) Exp Eye Res , vol.75 , pp. 683-694
    • Marchant, J.K.1    Zhang, G.2    Birk, D.E.3
  • 44
    • 0029863018 scopus 로고    scopus 로고
    • CD44 exon variant 6 epitope and hyaluronate synthase are expressed on HT29 human colorectal carcinoma cells in a SCID mouse model of metastasis formation
    • Mitchell BS, Whitehouse A, Prehm P, Delpech B, Schumacher U. 1996. CD44 exon variant 6 epitope and hyaluronate synthase are expressed on HT29 human colorectal carcinoma cells in a SCID mouse model of metastasis formation. Clin Exp Metastasis 14:107-114.
    • (1996) Clin Exp Metastasis , vol.14 , pp. 107-114
    • Mitchell, B.S.1    Whitehouse, A.2    Prehm, P.3    Delpech, B.4    Schumacher, U.5
  • 45
    • 0036683241 scopus 로고    scopus 로고
    • CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain
    • Mori H, Tomari T, Koshikawa N, Kajita M, Itoh Y, Sato H, Tojo H, Yana I, Seiki M. 2002. CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain. EMBO J 21:3949-3959.
    • (2002) EMBO J , vol.21 , pp. 3949-3959
    • Mori, H.1    Tomari, T.2    Koshikawa, N.3    Kajita, M.4    Itoh, Y.5    Sato, H.6    Tojo, H.7    Yana, I.8    Seiki, M.9
  • 47
    • 3042554386 scopus 로고    scopus 로고
    • Cell-matrix interaction via CD44 is independently regulated by different metalloproteinases activated in response to extracellular Ca(2+) influx and PKC activation
    • Nagano O, Murakami D, Hartmann D, De Strooper B, Saftig P, Iwatsubo T, Nakajima M, Shinohara M, Saya H. 2004. Cell-matrix interaction via CD44 is independently regulated by different metalloproteinases activated in response to extracellular Ca(2+) influx and PKC activation. J Cell Biol 165:893-902.
    • (2004) J Cell Biol , vol.165 , pp. 893-902
    • Nagano, O.1    Murakami, D.2    Hartmann, D.3    De Strooper, B.4    Saftig, P.5    Iwatsubo, T.6    Nakajima, M.7    Shinohara, M.8    Saya, H.9
  • 48
    • 0002883217 scopus 로고    scopus 로고
    • editors. Matrix metalloproteinases. New York: Academic Press, pp
    • Nagase H. 1998. Stromelysins 1 and 2. In: Parks WC, Mecharm RP, editors. Matrix metalloproteinases. New York: Academic Press, pp 43-84.
    • (1998) Stromelysins 1 and 2 , pp. 43-84
    • Nagase, H.1
  • 49
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase H, Woessner JF, Jr. 1999. Matrix metalloproteinases. J Biol Chem 274:21491-21494.
    • (1999) J Biol Chem , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner Jr., J.F.2
  • 50
    • 0030966842 scopus 로고    scopus 로고
    • CD44: Structure, function, and association with the malignant process
    • Naor D, Sionov RV, Ish-Shalom D. 1997. CD44: Structure, function, and association with the malignant process. Adv Cancer Res 71:241-319.
    • (1997) Adv Cancer Res , vol.71 , pp. 241-319
    • Naor, D.1    Sionov, R.V.2    Ish-Shalom, D.3
  • 51
    • 0031025218 scopus 로고    scopus 로고
    • Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules
    • Ohuchi E, Imai K, Fujii Y, Sato H, Seiki M, Okada Y. 1997. Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules. J Biol Chem 272:2446-2451.
    • (1997) J Biol Chem , vol.272 , pp. 2446-2451
    • Ohuchi, E.1    Imai, K.2    Fujii, Y.3    Sato, H.4    Seiki, M.5    Okada, Y.6
  • 54
    • 0031048966 scopus 로고    scopus 로고
    • Proteolytic activation of the precursor of membrane type 1 matrix metalloproteinase by human plasmin. A possible cell surface activator
    • Okumura Y, Sato H, Seiki M, Kido H. 1997. Proteolytic activation of the precursor of membrane type 1 matrix metalloproteinase by human plasmin. A possible cell surface activator. FEBS Lett 402:181-184.
    • (1997) FEBS Lett , vol.402 , pp. 181-184
    • Okumura, Y.1    Sato, H.2    Seiki, M.3    Kido, H.4
  • 55
    • 0031059914 scopus 로고    scopus 로고
    • The extracellular matrix in neural crest-cell migration
    • Perris R. 1997. The extracellular matrix in neural crest-cell migration. Trends Neurosci 20:23-31.
    • (1997) Trends Neurosci , vol.20 , pp. 23-31
    • Perris, R.1
  • 57
  • 58
    • 0029996724 scopus 로고    scopus 로고
    • Cell surface binding and activation of gelatinase A induced by expression of membrane-type-1-matrix metalloproteinase (MT1-MMP)
    • Sato H, Takino T, Kinoshita T, Imai K, Okada Y, Stetler Stevenson WG, Seiki M. 1996. Cell surface binding and activation of gelatinase A induced by expression of membrane-type-1-matrix metalloproteinase (MT1-MMP). FEBS Lett 385:238-240.
    • (1996) FEBS Lett , vol.385 , pp. 238-240
    • Sato, H.1    Takino, T.2    Kinoshita, T.3    Imai, K.4    Okada, Y.5    Stetler Stevenson, W.G.6    Seiki, M.7
  • 59
    • 0033003771 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinases
    • Seiki M. 1999. Membrane-type matrix metalloproteinases. Apmis 107:137-143.
    • (1999) Apmis , vol.107 , pp. 137-143
    • Seiki, M.1
  • 60
    • 0030942574 scopus 로고    scopus 로고
    • Expression of three membrane-type matrix metalloproteinases (MT-MMPs) in rat vascular smooth muscle cells and characterization of MT3-MMPs with and without transmembrane domain
    • Shofuda K, Yasumitsu H, Nishihashi A, Miki K, Miyazaki K. 1997. Expression of three membrane-type matrix metalloproteinases (MT-MMPs) in rat vascular smooth muscle cells and characterization of MT3-MMPs with and without transmembrane domain. J Biol Chem 272:9749-9754.
    • (1997) J Biol Chem , vol.272 , pp. 9749-9754
    • Shofuda, K.1    Yasumitsu, H.2    Nishihashi, A.3    Miki, K.4    Miyazaki, K.5
  • 61
    • 0036353544 scopus 로고    scopus 로고
    • Two-stage compaction of the secondary avian cornea during development
    • Siegler V, Quantock AJ. 2002. Two-stage compaction of the secondary avian cornea during development. Exp Eye Res 74:427-431.
    • (2002) Exp Eye Res , vol.74 , pp. 427-431
    • Siegler, V.1    Quantock, A.J.2
  • 62
    • 0034914003 scopus 로고    scopus 로고
    • Cell surface-expressed Thomsen-Friedenreich antigen in colon cancer is predominantly carried on high molecular weight splice variants of CD44
    • Singh R, Campbell BJ, Yu LG, Fernig DG, Milton JD, Goodlad RA, FitzGerald AJ, Rhodes JM. 2001. Cell surface-expressed Thomsen-Friedenreich antigen in colon cancer is predominantly carried on high molecular weight splice variants of CD44. Glycobiology 11:587-592.
    • (2001) Glycobiology , vol.11 , pp. 587-592
    • Singh, R.1    Campbell, B.J.2    Yu, L.G.3    Fernig, D.G.4    Milton, J.D.5    Goodlad, R.A.6    FitzGerald, A.J.7    Rhodes, J.M.8
  • 65
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht MD, Werb Z. 2001. How matrix metalloproteinases regulate cell behavior. Annu Rev Cell Dev Biol 17:463-516.
    • (2001) Annu Rev Cell Dev Biol , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 66
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease
    • Strongin AY, Collier I, Bannikov G, Marmer BL, Grant GA, Goldberg GI. 1995. Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J Biol Chem 270:5331-5338.
    • (1995) J Biol Chem , vol.270 , pp. 5331-5338
    • Strongin, A.Y.1    Collier, I.2    Bannikov, G.3    Marmer, B.L.4    Grant, G.A.5    Goldberg, G.I.6
  • 67
    • 0023763090 scopus 로고
    • Embryonic chicken cornea and cartilage synthesize type IX collagen molecules with different amino-terminal domains
    • Svoboda KK, Nishimura I, Sugrue SP, Ninomiya Y, Olsen BR. 1988. Embryonic chicken cornea and cartilage synthesize type IX collagen molecules with different amino-terminal domains. Proc Natl Acad Sci USA 85:7496-7500.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 7496-7500
    • Svoboda, K.K.1    Nishimura, I.2    Sugrue, S.P.3    Ninomiya, Y.4    Olsen, B.R.5
  • 68
    • 0842280615 scopus 로고    scopus 로고
    • The role of the CD44 transmembrane and cytoplasmic domains in coordinating adhesive and signalling events
    • Thorne RF, Legg JW, Isacke CM. 2004. The role of the CD44 transmembrane and cytoplasmic domains in coordinating adhesive and signalling events. J Cell Sci 117:373-380.
    • (2004) J Cell Sci , vol.117 , pp. 373-380
    • Thorne, R.F.1    Legg, J.W.2    Isacke, C.M.3
  • 69
    • 0015124266 scopus 로고
    • Hyaluronate production and removal during corneal development in the chick
    • Toole BP, Trelstad RL. 1971. Hyaluronate production and removal during corneal development in the chick. Dev Biol 26:28-35.
    • (1971) Dev Biol , vol.26 , pp. 28-35
    • Toole, B.P.1    Trelstad, R.L.2
  • 71
    • 0015123838 scopus 로고
    • Morphogenesis of the collagenous stroma in the chick cornea
    • Trelstad RL, Coulombre AJ. 1971. Morphogenesis of the collagenous stroma in the chick cornea. J Cell Biol 50:840-858.
    • (1971) J Cell Biol , vol.50 , pp. 840-858
    • Trelstad, R.L.1    Coulombre, A.J.2
  • 73
    • 0025949206 scopus 로고    scopus 로고
    • Wu JJ, Lark MW, Chun LE, Eyre DR. 1991. Sites of stromelysin cleavage in collagen types II, IX, X, and XI of cartilage. J Biol Chem 266:5625-5628.
    • Wu JJ, Lark MW, Chun LE, Eyre DR. 1991. Sites of stromelysin cleavage in collagen types II, IX, X, and XI of cartilage. J Biol Chem 266:5625-5628.
  • 74
    • 0036383115 scopus 로고    scopus 로고
    • The roles of types XII and XIV collagen in fibrillogenesis and matrix assembly in the developing cornea
    • Young BB, Zhang G, Koch M, Birk DE. 2002. The roles of types XII and XIV collagen in fibrillogenesis and matrix assembly in the developing cornea. J Cell Biochem 87:208-220.
    • (2002) J Cell Biochem , vol.87 , pp. 208-220
    • Young, B.B.1    Zhang, G.2    Koch, M.3    Birk, D.E.4
  • 75
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis
    • Yu Q, Stamenkovic I. 2000. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev 14:163-176.
    • (2000) Genes Dev , vol.14 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2
  • 76
    • 10744221757 scopus 로고    scopus 로고
    • Differential inhibition of membrane type 3 (MT3)-matrix metalloproteinase (MMP) and MT1-MMP by tissue inhibitor of metalloproteinase (TIMP)-2 and TIMP-3 regulates pro-MMP-2 activation
    • Zhao H, Bernardo MM, Osenkowski P, Sohail A, Pei D, Nagase H, Kashiwagi M, Soloway PD, DeClerck YA, Fridman R. 2004. Differential inhibition of membrane type 3 (MT3)-matrix metalloproteinase (MMP) and MT1-MMP by tissue inhibitor of metalloproteinase (TIMP)-2 and TIMP-3 regulates pro-MMP-2 activation. J Biol Chem 279:8592-8601.
    • (2004) J Biol Chem , vol.279 , pp. 8592-8601
    • Zhao, H.1    Bernardo, M.M.2    Osenkowski, P.3    Sohail, A.4    Pei, D.5    Nagase, H.6    Kashiwagi, M.7    Soloway, P.D.8    DeClerck, Y.A.9    Fridman, R.10


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