메뉴 건너뛰기




Volumn 22, Issue 7, 2008, Pages 2151-2160

Distinguishing fibroblast promigratory and procontractile growth factor environments in 3-D collagen matrices

Author keywords

Cell contraction; Cell migration; Lysophosphatidic acid; Platelet derived growth factor; Sphingosine 1 phosphate; Wound repair

Indexed keywords

BASIC FIBROBLAST GROWTH FACTOR; COLLAGEN TYPE 1; ENDOTHELIN 1; EPIDERMAL GROWTH FACTOR; GROWTH FACTOR; LYSOPHOSPHATIDIC ACID; PLATELET DERIVED GROWTH FACTOR; SPHINGOSINE 1 PHOSPHATE; SPHINGOSINE 1 PHOSPHATE RECEPTOR; TRANSFORMING GROWTH FACTOR;

EID: 46749123441     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.07-097014     Document Type: Article
Times cited : (47)

References (73)
  • 1
    • 0001297636 scopus 로고
    • Production of a tissue-like structure by contraction of collagen lattices by human fibroblasts of different proliferative potential in vitro
    • Bell, E., Ivarsson, B., and Merrill, C. (1979) Production of a tissue-like structure by contraction of collagen lattices by human fibroblasts of different proliferative potential in vitro. Proc. Natl. Acad. Sci. U. S. A. 76, 1274-1278
    • (1979) Proc. Natl. Acad. Sci. U. S. A , vol.76 , pp. 1274-1278
    • Bell, E.1    Ivarsson, B.2    Merrill, C.3
  • 3
    • 0036774181 scopus 로고    scopus 로고
    • Cell interactions with three-dimensional matrices
    • Cukierman, E., Pankov, R., and Yamada, K. M. (2002) Cell interactions with three-dimensional matrices. Curr. Opin. Cell Biol. 14, 633-639
    • (2002) Curr. Opin. Cell Biol , vol.14 , pp. 633-639
    • Cukierman, E.1    Pankov, R.2    Yamada, K.M.3
  • 4
    • 0027955331 scopus 로고
    • Fibroblasts, myofibroblasts, and wound contraction
    • Grinnell, F. (1994) Fibroblasts, myofibroblasts, and wound contraction. J. Cell Biol. 124, 401-404
    • (1994) J. Cell Biol , vol.124 , pp. 401-404
    • Grinnell, F.1
  • 6
    • 0038738331 scopus 로고    scopus 로고
    • Fibroblast biology in three-dimensional collagen matrices
    • Grinnell, F. (2003) Fibroblast biology in three-dimensional collagen matrices. Trends Cell Biol. 13, 264-269
    • (2003) Trends Cell Biol , vol.13 , pp. 264-269
    • Grinnell, F.1
  • 8
    • 34247191989 scopus 로고    scopus 로고
    • Tissue engineering for cutaneous wounds
    • Clark, R. A., Ghosh, K., and Tonnesen, M. G. (2007) Tissue engineering for cutaneous wounds. J. Invest. Dermatol. 127, 1018-1029
    • (2007) J. Invest. Dermatol , vol.127 , pp. 1018-1029
    • Clark, R.A.1    Ghosh, K.2    Tonnesen, M.G.3
  • 9
    • 33846573898 scopus 로고    scopus 로고
    • Fibroblast differentiation in wound healing and fibrosis
    • Darby, I. A., and Hewitson, T. D. (2007) Fibroblast differentiation in wound healing and fibrosis. Int. Rev. Cytol. 257, 143-179
    • (2007) Int. Rev. Cytol , vol.257 , pp. 143-179
    • Darby, I.A.1    Hewitson, T.D.2
  • 10
    • 33847084614 scopus 로고    scopus 로고
    • Formation and function of the myofibroblast during tissue repair
    • Hinz, B. (2007) Formation and function of the myofibroblast during tissue repair. J. Invest. Dermatol. 127, 526-537
    • (2007) J. Invest. Dermatol , vol.127 , pp. 526-537
    • Hinz, B.1
  • 11
    • 33847392947 scopus 로고    scopus 로고
    • New developments in fibroblast and myofibroblast biology: Implications for fibrosis and scleroderma
    • Abraham, D. J., Eckes, B., Rajkumar, V., and Krieg, T. (2007) New developments in fibroblast and myofibroblast biology: implications for fibrosis and scleroderma. Curr. Rheumatol. Rep. 9, 136-143
    • (2007) Curr. Rheumatol. Rep , vol.9 , pp. 136-143
    • Abraham, D.J.1    Eckes, B.2    Rajkumar, V.3    Krieg, T.4
  • 13
    • 30744442279 scopus 로고    scopus 로고
    • Cancer: The matrix is now in control
    • Comoglio, P. M., and Trusolino, L. (2005) Cancer: the matrix is now in control. Nat. Med. 11, 1156-1159
    • (2005) Nat. Med , vol.11 , pp. 1156-1159
    • Comoglio, P.M.1    Trusolino, L.2
  • 14
    • 23744432972 scopus 로고    scopus 로고
    • Stromagenesis: The changing face of fibroblastic microenvironments during tumor progression
    • Beacham, D. A., and Cukierman, E. (2005) Stromagenesis: the changing face of fibroblastic microenvironments during tumor progression. Semin. Cancer Biol. 15, 329-341
    • (2005) Semin. Cancer Biol , vol.15 , pp. 329-341
    • Beacham, D.A.1    Cukierman, E.2
  • 15
    • 0029294389 scopus 로고
    • The fibroblast-populated collagen microsphere assay of cell traction force-Part 2: Measurement of the cell traction parameter
    • Barocas, V. H., Moon, A. G., and Tranquillo, R. T. (1995) The fibroblast-populated collagen microsphere assay of cell traction force-Part 2: Measurement of the cell traction parameter. J. Biomech. Eng. 117, 161-170
    • (1995) J. Biomech. Eng , vol.117 , pp. 161-170
    • Barocas, V.H.1    Moon, A.G.2    Tranquillo, R.T.3
  • 16
    • 0033729465 scopus 로고    scopus 로고
    • Cell mechanics studied by a reconstituted model tissue
    • Wakatsuki, T., Kolodney, M. S., Zahalak, G. I., and Elson, E. L. (2000) Cell mechanics studied by a reconstituted model tissue. Biophys. J. 79, 2353-2368
    • (2000) Biophys. J , vol.79 , pp. 2353-2368
    • Wakatsuki, T.1    Kolodney, M.S.2    Zahalak, G.I.3    Elson, E.L.4
  • 17
    • 0036102097 scopus 로고    scopus 로고
    • Tensile mechanical properties of three-dimensional type I collagen extracellular matrices with varied microstructure
    • Roeder, B. A., Kokini, K., Sturgis, J. E., Robinson, J. P., and Voytik-Harbin, S. L. (2002) Tensile mechanical properties of three-dimensional type I collagen extracellular matrices with varied microstructure. J. Biomech. Eng. 124, 214-222
    • (2002) J. Biomech. Eng , vol.124 , pp. 214-222
    • Roeder, B.A.1    Kokini, K.2    Sturgis, J.E.3    Robinson, J.P.4    Voytik-Harbin, S.L.5
  • 18
    • 33846822104 scopus 로고    scopus 로고
    • Biomechanical and biochemical characteristics of a human fibroblast-produced and remodeled matrix
    • Ahlfors, J. E., and Billiar, K. L. (2007) Biomechanical and biochemical characteristics of a human fibroblast-produced and remodeled matrix. Biomaterials 28, 2183-2191
    • (2007) Biomaterials , vol.28 , pp. 2183-2191
    • Ahlfors, J.E.1    Billiar, K.L.2
  • 19
    • 36048993806 scopus 로고    scopus 로고
    • Mechanobiology of force transduction in dermal tissue
    • Silver, F. H., Siperko, L. M., and Seehra, G. P. (2002) Mechanobiology of force transduction in dermal tissue. Skin Res. Tech. 8, 1-21
    • (2002) Skin Res. Tech , vol.8 , pp. 1-21
    • Silver, F.H.1    Siperko, L.M.2    Seehra, G.P.3
  • 21
  • 22
    • 34547931078 scopus 로고    scopus 로고
    • Modeling tissue morphogenesis and cancer in 3-D
    • Yamada, K. M., and Cukierman, E. (2007) Modeling tissue morphogenesis and cancer in 3-D. Cell 130, 601-610
    • (2007) Cell , vol.130 , pp. 601-610
    • Yamada, K.M.1    Cukierman, E.2
  • 23
    • 0025078397 scopus 로고
    • Cell locomotion forces versus cell contraction forces for collagen lattice contraction: An in vitro model of wound contraction
    • Ehrlich, H. P., and Rajaratnam, J. B. (1990) Cell locomotion forces versus cell contraction forces for collagen lattice contraction: an in vitro model of wound contraction. Tissue Cell 22, 407-417
    • (1990) Tissue Cell , vol.22 , pp. 407-417
    • Ehrlich, H.P.1    Rajaratnam, J.B.2
  • 24
    • 0033570184 scopus 로고    scopus 로고
    • Increased myosin light chain phosphorylation is not required for growth factor stimulation of collagen matrix contraction
    • Skuta, G., Ho, C. H., and Grinnell, F. (1999) Increased myosin light chain phosphorylation is not required for growth factor stimulation of collagen matrix contraction. J. Biol. Chem. 274, 30163-30168
    • (1999) J. Biol. Chem , vol.274 , pp. 30163-30168
    • Skuta, G.1    Ho, C.H.2    Grinnell, F.3
  • 25
    • 31944433804 scopus 로고    scopus 로고
    • P21-activated kinase 1: Convergence point in PDGF- and LPA-stimulated collagen matrix contraction by human fibroblasts
    • Rhee, S., and Grinnell, F. (2006) P21-activated kinase 1: convergence point in PDGF- and LPA-stimulated collagen matrix contraction by human fibroblasts. J. Cell Biol. 172, 423-432
    • (2006) J. Cell Biol , vol.172 , pp. 423-432
    • Rhee, S.1    Grinnell, F.2
  • 26
    • 0025980387 scopus 로고
    • Stress relaxation of contracted collagen gels: Disruption of actin filament bundles, release of cell surface fibronectin, and downregulation of DNA and protein synthesis
    • Mochitate, K., Pawelek, P., and Grinnell, F. (1991) Stress relaxation of contracted collagen gels: disruption of actin filament bundles, release of cell surface fibronectin, and downregulation of DNA and protein synthesis. Exp. Cell Res. 193, 198-207
    • (1991) Exp. Cell Res , vol.193 , pp. 198-207
    • Mochitate, K.1    Pawelek, P.2    Grinnell, F.3
  • 28
    • 0034141607 scopus 로고    scopus 로고
    • Regulation of LPA-promoted myofibroblast contraction: Role of Rho, myosin light chain kinase, and myosin light chain phosphatase
    • Parizi, M., Howard, E. W., and Tomasek, J. J. (2000) Regulation of LPA-promoted myofibroblast contraction: Role of Rho, myosin light chain kinase, and myosin light chain phosphatase. Exp. Cell Res. 254, 210-220
    • (2000) Exp. Cell Res , vol.254 , pp. 210-220
    • Parizi, M.1    Howard, E.W.2    Tomasek, J.J.3
  • 29
    • 0346850860 scopus 로고    scopus 로고
    • Different molecular motors mediate platelet-derived growth factor and lysophosphatidic acid-stimulated floating collagen matrix contraction
    • Abe, M., Ho, C. H., Kamm, K. E., and Grinnell, F. (2003) Different molecular motors mediate platelet-derived growth factor and lysophosphatidic acid-stimulated floating collagen matrix contraction. J. Biol. Chem. 278, 47707-47712
    • (2003) J. Biol. Chem , vol.278 , pp. 47707-47712
    • Abe, M.1    Ho, C.H.2    Kamm, K.E.3    Grinnell, F.4
  • 30
    • 0033534684 scopus 로고    scopus 로고
    • Differences in the regulation of fibroblast contraction of floating versus stressed collagen matrices
    • Grinnell, F., Ho, C. H., Lin, Y. C., and Skuta, G. (1999) Differences in the regulation of fibroblast contraction of floating versus stressed collagen matrices. J. Biol. Chem. 274, 918-923
    • (1999) J. Biol. Chem , vol.274 , pp. 918-923
    • Grinnell, F.1    Ho, C.H.2    Lin, Y.C.3    Skuta, G.4
  • 31
    • 27944465002 scopus 로고    scopus 로고
    • Nested collagen matrices: A new model to study migration of human fibroblast populations in three dimensions
    • Grinnell, F., Rocha, L. B., Iucu, C., Rhee, S., and Jiang, H. (2006) Nested collagen matrices: a new model to study migration of human fibroblast populations in three dimensions. Exp. Cell Res. 312, 86-94
    • (2006) Exp. Cell Res , vol.312 , pp. 86-94
    • Grinnell, F.1    Rocha, L.B.2    Iucu, C.3    Rhee, S.4    Jiang, H.5
  • 32
    • 33846980084 scopus 로고    scopus 로고
    • Growth factors: The promise and the problems
    • Davidson, J. M. (2007) Growth factors: the promise and the problems. Int. J. Low. Extrem. Wounds 6, 8-10
    • (2007) Int. J. Low. Extrem. Wounds , vol.6 , pp. 8-10
    • Davidson, J.M.1
  • 33
    • 16844362298 scopus 로고    scopus 로고
    • Engineered growth factors and cutaneous wound healing: Success and possible questions in the past 10 years
    • Fu, X., Li, X., Cheng, B., Chen, W., and Sheng, Z. (2005) Engineered growth factors and cutaneous wound healing: success and possible questions in the past 10 years. Wound Repair Regen. 13, 122-130
    • (2005) Wound Repair Regen , vol.13 , pp. 122-130
    • Fu, X.1    Li, X.2    Cheng, B.3    Chen, W.4    Sheng, Z.5
  • 34
    • 0038676258 scopus 로고    scopus 로고
    • Regulation of wound healing by growth factors and cytokines
    • Werner, S., and Grose, R. (2003) Regulation of wound healing by growth factors and cytokines. Physiol. Rev. 83, 835-870
    • (2003) Physiol. Rev , vol.83 , pp. 835-870
    • Werner, S.1    Grose, R.2
  • 35
    • 0037837212 scopus 로고    scopus 로고
    • Growth factors in wound healing
    • Cross, K. J., and Mustoe, T. A. (2003) Growth factors in wound healing. Surg. Clin. North Am. 83, 531-545
    • (2003) Surg. Clin. North Am , vol.83 , pp. 531-545
    • Cross, K.J.1    Mustoe, T.A.2
  • 36
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A. J., Paterson, H. F., Johnston, C. L., Diekmann, D., and Hall, A. (1992) The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70, 401-410
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 37
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A. J., and Hall, A. (1992) The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70, 389-399
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 38
    • 0026664282 scopus 로고
    • Regulation of fibroblast-mediated collagen gel contraction by platelet-derived growth factor, interleukin-1 alpha and transforming growth factor-beta 1
    • Tingstrom, A., Heldin, C. H., and Rubin, K. (1992) Regulation of fibroblast-mediated collagen gel contraction by platelet-derived growth factor, interleukin-1 alpha and transforming growth factor-beta 1. J. Cell Sci. 102, 315-322
    • (1992) J. Cell Sci , vol.102 , pp. 315-322
    • Tingstrom, A.1    Heldin, C.H.2    Rubin, K.3
  • 39
    • 0033864576 scopus 로고    scopus 로고
    • Contraction of collagen matrices mediated by alpha2beta1A and alpha(v)beta3 integrins
    • Cooke, M. E., Sakai, T., and Mosher, D. F. (2000) Contraction of collagen matrices mediated by alpha2beta1A and alpha(v)beta3 integrins. J. Cell Sci. 113, 2375-2383
    • (2000) J. Cell Sci , vol.113 , pp. 2375-2383
    • Cooke, M.E.1    Sakai, T.2    Mosher, D.F.3
  • 40
    • 33744945040 scopus 로고    scopus 로고
    • Multiple signaling pathways mediate compaction of collagen matrices by EGF-stimulated fibroblasts
    • Smith, K. D., Wells, A., and Lauffenburger, D. A. (2006) Multiple signaling pathways mediate compaction of collagen matrices by EGF-stimulated fibroblasts. Exp. Cell Res. 312, 1970-1982
    • (2006) Exp. Cell Res , vol.312 , pp. 1970-1982
    • Smith, K.D.1    Wells, A.2    Lauffenburger, D.A.3
  • 41
    • 0025989629 scopus 로고
    • Endothelins produced by endothelial cells promote collagen gel contraction by fibroblasts
    • Guidry, C., and Hook, M. (1991) Endothelins produced by endothelial cells promote collagen gel contraction by fibroblasts. J. Cell Biol. 115, 873-880
    • (1991) J. Cell Biol , vol.115 , pp. 873-880
    • Guidry, C.1    Hook, M.2
  • 42
    • 36849096127 scopus 로고    scopus 로고
    • Evidence that PI3K, Rac, Rho, and Rho kinase are involved in basic fibroblast growth factor-stimulated fibroblast-collagen matrix contraction
    • Abe, M., Sogabe, Y., Syuto, T., Yokoyama, Y., and Ishikawa, O. (2007) Evidence that PI3K, Rac, Rho, and Rho kinase are involved in basic fibroblast growth factor-stimulated fibroblast-collagen matrix contraction. J. Cell Biochem.
    • (2007) J. Cell Biochem
    • Abe, M.1    Sogabe, Y.2    Syuto, T.3    Yokoyama, Y.4    Ishikawa, O.5
  • 44
    • 34248395119 scopus 로고    scopus 로고
    • Microtubule function in fibroblast spreading is modulated according to the tension state of cell-matrix interactions
    • Rhee, S., Jiang, H., Ho, C. H., and Grinnell, F. (2007) Microtubule function in fibroblast spreading is modulated according to the tension state of cell-matrix interactions. Proc. Natl. Acad. Sci. U. S. A. 104, 5425-5430
    • (2007) Proc. Natl. Acad. Sci. U. S. A , vol.104 , pp. 5425-5430
    • Rhee, S.1    Jiang, H.2    Ho, C.H.3    Grinnell, F.4
  • 45
    • 0020517748 scopus 로고
    • Human platelet-derived growth factor: Radioimmunoassay and discovery of a specific plasma-binding protein
    • Huang, J. S., Huang, S. S., and Deuel, T. F. (1983) Human platelet-derived growth factor: radioimmunoassay and discovery of a specific plasma-binding protein. J. Cell Biol. 97, 383-388
    • (1983) J. Cell Biol , vol.97 , pp. 383-388
    • Huang, J.S.1    Huang, S.S.2    Deuel, T.F.3
  • 46
    • 0030021251 scopus 로고    scopus 로고
    • Lower cytokine release by fetal porcine platelets: A possible explanation for reduced inflammation after fetal wounding
    • Olutoye, O. O., Yager, D. R., Cohen, I. K., and Diegelmann, R. F. (1996) Lower cytokine release by fetal porcine platelets: a possible explanation for reduced inflammation after fetal wounding. J. Pediatr. Surg. 31, 91-95
    • (1996) J. Pediatr. Surg , vol.31 , pp. 91-95
    • Olutoye, O.O.1    Yager, D.R.2    Cohen, I.K.3    Diegelmann, R.F.4
  • 47
    • 0037370012 scopus 로고    scopus 로고
    • Inhibitory and stimulatory regulation of Rac and cell motility by the G12/13-Rho and Gi pathways integrated downstream of a single G protein-coupled sphingosine-1-phosphate receptor isoform
    • Sugimoto, N., Takuwa, N., Okamoto, H., Sakurada, S., and Takuwa, Y. (2003) Inhibitory and stimulatory regulation of Rac and cell motility by the G12/13-Rho and Gi pathways integrated downstream of a single G protein-coupled sphingosine-1-phosphate receptor isoform. Mol. Cell. Biol. 23, 1534-1545
    • (2003) Mol. Cell. Biol , vol.23 , pp. 1534-1545
    • Sugimoto, N.1    Takuwa, N.2    Okamoto, H.3    Sakurada, S.4    Takuwa, Y.5
  • 49
    • 0037328762 scopus 로고    scopus 로고
    • Dendritic fibroblasts in three-dimensional collagen matrices
    • Grinnell, F., Ho, C. H., Tamariz, E., Lee, D. J., and Skuta, G. (2003) Dendritic fibroblasts in three-dimensional collagen matrices. Mol. Biol. Cell 14, 384-395
    • (2003) Mol. Biol. Cell , vol.14 , pp. 384-395
    • Grinnell, F.1    Ho, C.H.2    Tamariz, E.3    Lee, D.J.4    Skuta, G.5
  • 50
    • 0347990559 scopus 로고    scopus 로고
    • Mechanism of human dermal fibroblast migration driven by type I collagen and platelet-derived growth factor-BB
    • Li, W., Fan, J., Chen, M., Guan, S., Sawcer, D., Bokoch, G. M., and Woodley, D. T. (2004) Mechanism of human dermal fibroblast migration driven by type I collagen and platelet-derived growth factor-BB. Mol. Biol. Cell 15, 294-309
    • (2004) Mol. Biol. Cell , vol.15 , pp. 294-309
    • Li, W.1    Fan, J.2    Chen, M.3    Guan, S.4    Sawcer, D.5    Bokoch, G.M.6    Woodley, D.T.7
  • 52
    • 0030961305 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate, a bioactive sphingolipid abundantly stored in platelets, is a normal constituent of human plasma and serum
    • Yatomi, Y., Igarashi, Y., Yang, L., Hisano, N., Qi, R., Asazuma, N., Satoh, K., Ozaki, Y., and Kume, S. (1997) Sphingosine 1-phosphate, a bioactive sphingolipid abundantly stored in platelets, is a normal constituent of human plasma and serum. J. Biochem. 121, 969-973
    • (1997) J. Biochem , vol.121 , pp. 969-973
    • Yatomi, Y.1    Igarashi, Y.2    Yang, L.3    Hisano, N.4    Qi, R.5    Asazuma, N.6    Satoh, K.7    Ozaki, Y.8    Kume, S.9
  • 53
    • 0031729124 scopus 로고    scopus 로고
    • Diversity of cellular receptors and functions for the lysophospholipid growth factors lysophosphatidic acid and sphingosine 1-phosphate
    • Goetzl, E. J., and An, S. (1998) Diversity of cellular receptors and functions for the lysophospholipid growth factors lysophosphatidic acid and sphingosine 1-phosphate. FASEB J. 12, 1589-1598
    • (1998) FASEB J , vol.12 , pp. 1589-1598
    • Goetzl, E.J.1    An, S.2
  • 54
    • 0027232391 scopus 로고
    • The bioactive phospholipid lysophosphatidic acid is released from activated platelets
    • Eichholtz, T., Jalink, K., Fahrenfort, I., and Moolenaar, W. H. (1993) The bioactive phospholipid lysophosphatidic acid is released from activated platelets. Biochem. J. 291, 677-680
    • (1993) Biochem. J , vol.291 , pp. 677-680
    • Eichholtz, T.1    Jalink, K.2    Fahrenfort, I.3    Moolenaar, W.H.4
  • 55
    • 0036434445 scopus 로고    scopus 로고
    • Enhancement of sphingosine 1-phosphate-induced migration of vascular endothelial cells and smooth muscle cells by an EDG-5 antagonist
    • Osada, M., Yatomi, Y., Ohmori, T., Ikeda, H., and Ozaki, Y. (2002) Enhancement of sphingosine 1-phosphate-induced migration of vascular endothelial cells and smooth muscle cells by an EDG-5 antagonist. Biochem. Biophys. Res. Commun. 299, 483-487
    • (2002) Biochem. Biophys. Res. Commun , vol.299 , pp. 483-487
    • Osada, M.1    Yatomi, Y.2    Ohmori, T.3    Ikeda, H.4    Ozaki, Y.5
  • 56
    • 0042858413 scopus 로고    scopus 로고
    • Ligand-dependent inhibition of B16 melanoma cell migration and invasion via endogenous S1P2 G protein-coupled receptor. Requirement of inhibition of cellular RAC activity
    • Arikawa, K., Takuwa, N., Yamaguchi, H., Sugimoto, N., Kitayama, J., Nagawa, H., Takehara, K., and Takuwa, Y. (2003) Ligand-dependent inhibition of B16 melanoma cell migration and invasion via endogenous S1P2 G protein-coupled receptor. Requirement of inhibition of cellular RAC activity. J. Biol. Chem. 278, 32841-32851
    • (2003) J. Biol. Chem , vol.278 , pp. 32841-32851
    • Arikawa, K.1    Takuwa, N.2    Yamaguchi, H.3    Sugimoto, N.4    Kitayama, J.5    Nagawa, H.6    Takehara, K.7    Takuwa, Y.8
  • 57
    • 0030723163 scopus 로고    scopus 로고
    • Platelet-derived growth factor and fibronectin-stimulated migration are differentially regulated by the Rac and extracellular signal-regulated kinase pathways
    • Anand-Apte, B., Zetter, B. R., Viswanathan, A., Qiu, R. G., Chen, J., Ruggieri, R., and Symons, M. (1997) Platelet-derived growth factor and fibronectin-stimulated migration are differentially regulated by the Rac and extracellular signal-regulated kinase pathways. J. Biol. Chem. 272, 30688-30692
    • (1997) J. Biol. Chem , vol.272 , pp. 30688-30692
    • Anand-Apte, B.1    Zetter, B.R.2    Viswanathan, A.3    Qiu, R.G.4    Chen, J.5    Ruggieri, R.6    Symons, M.7
  • 59
    • 0034810439 scopus 로고    scopus 로고
    • RhoA/rho-associated kinase mediates fibroblast contractile force generation
    • Yee, H. F., Jr., Melton, A. C., and Tran, B. N. (2001) RhoA/rho-associated kinase mediates fibroblast contractile force generation. Biochem. Biophys. Res. Commun. 280, 1340-1345
    • (2001) Biochem. Biophys. Res. Commun , vol.280 , pp. 1340-1345
    • Yee Jr., H.F.1    Melton, A.C.2    Tran, B.N.3
  • 60
    • 33947147730 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate signaling in the cardiovascular system
    • Peters, S. L., and Alewijnse, A. E. (2007) Sphingosine-1-phosphate signaling in the cardiovascular system. Curr. Opin. Pharmacol. 7, 186-192
    • (2007) Curr. Opin. Pharmacol , vol.7 , pp. 186-192
    • Peters, S.L.1    Alewijnse, A.E.2
  • 61
    • 0037162064 scopus 로고    scopus 로고
    • Subtype-specific differential regulation of Rho family G proteins and cell migration by the Edg family sphingosine-1-phosphate receptors
    • Takuwa, Y. (2002) Subtype-specific differential regulation of Rho family G proteins and cell migration by the Edg family sphingosine-1-phosphate receptors. Biochim. Biophys. Acta 1582, 112-120
    • (2002) Biochim. Biophys. Acta , vol.1582 , pp. 112-120
    • Takuwa, Y.1
  • 63
    • 0036569034 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate signaling: Providing cells with a sense of direction
    • Spiegel, S., English, D., and Milstien, S. (2002) Sphingosine 1-phosphate signaling: providing cells with a sense of direction. Trends Cell Biol. 12, 236-242
    • (2002) Trends Cell Biol , vol.12 , pp. 236-242
    • Spiegel, S.1    English, D.2    Milstien, S.3
  • 64
    • 2542478053 scopus 로고    scopus 로고
    • Wound healing: An overview of acute, fibrotic and delayed healing
    • Diegelmann, R. F., and Evans, M. C. (2004) Wound healing: an overview of acute, fibrotic and delayed healing. Front. Biosci. 9, 283-289
    • (2004) Front. Biosci , vol.9 , pp. 283-289
    • Diegelmann, R.F.1    Evans, M.C.2
  • 65
    • 0030934532 scopus 로고    scopus 로고
    • Wound healing-aiming for perfect skin regeneration
    • Martin, P. (1997) Wound healing-aiming for perfect skin regeneration. Science 276, 75-81
    • (1997) Science , vol.276 , pp. 75-81
    • Martin, P.1
  • 67
    • 33846627240 scopus 로고    scopus 로고
    • Pathophysiology of acute wound healing
    • Li, J., Chen, J., and Kirsner, R. (2007) Pathophysiology of acute wound healing. Clin. Dermatol. 25, 9-18
    • (2007) Clin. Dermatol , vol.25 , pp. 9-18
    • Li, J.1    Chen, J.2    Kirsner, R.3
  • 68
    • 34848814480 scopus 로고    scopus 로고
    • Regulation of fibroblast functions by lysophospholipid mediators: Potential roles in wound healing
    • Watterson, K. R., Lanning, D. A., Diegelmann, R. F., and Spiegel, S. (2007) Regulation of fibroblast functions by lysophospholipid mediators: potential roles in wound healing. Wound Repair. Regen. 15, 607-616
    • (2007) Wound Repair. Regen , vol.15 , pp. 607-616
    • Watterson, K.R.1    Lanning, D.A.2    Diegelmann, R.F.3    Spiegel, S.4
  • 69
    • 0027202705 scopus 로고
    • Wound fluid from chronic leg ulcers contains elevated levels of metalloproteinases MMP-2 and MMP-9
    • Wysocki, A. B., Staiano-Coico, L., and Grinnell, F. (1993) Wound fluid from chronic leg ulcers contains elevated levels of metalloproteinases MMP-2 and MMP-9. J. Invest. Dermatol. 101, 64-68
    • (1993) J. Invest. Dermatol , vol.101 , pp. 64-68
    • Wysocki, A.B.1    Staiano-Coico, L.2    Grinnell, F.3
  • 70
    • 0029938994 scopus 로고    scopus 로고
    • Fibronectin degradation in chronic wounds depends on the relative levels of elastase, alpha1-proteinase inhibitor, and alpha2-macroglobulin
    • Grinnell, F., and Zhu, M. (1996) Fibronectin degradation in chronic wounds depends on the relative levels of elastase, alpha1-proteinase inhibitor, and alpha2-macroglobulin. J. Invest. Dermatol. 106, 335-341
    • (1996) J. Invest. Dermatol , vol.106 , pp. 335-341
    • Grinnell, F.1    Zhu, M.2
  • 72
    • 34447636273 scopus 로고    scopus 로고
    • Recent insights into the causes of chronic leg ulceration in venous diseases and implications on other types of chronic wounds
    • Chen, W. Y., and Rogers, A. A. (2007) Recent insights into the causes of chronic leg ulceration in venous diseases and implications on other types of chronic wounds. Wound Repair. Regen. 15, 434-449
    • (2007) Wound Repair. Regen , vol.15 , pp. 434-449
    • Chen, W.Y.1    Rogers, A.A.2
  • 73
    • 4344706187 scopus 로고    scopus 로고
    • The ins and outs of lysophosphatidic acid signaling
    • Moolenaar, W. H., van Meeteren, L. A., and Giepmans, B. N. (2004) The ins and outs of lysophosphatidic acid signaling. Bioessays 26, 870-881
    • (2004) Bioessays , vol.26 , pp. 870-881
    • Moolenaar, W.H.1    van Meeteren, L.A.2    Giepmans, B.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.