메뉴 건너뛰기




Volumn 1, Issue 6, 2009, Pages 1095-1111

Biochemical insights into the role of matrix metalloproteinases in regeneration: Challenges and recent developments

Author keywords

[No Author keywords available]

Indexed keywords

BENAZEPRIL; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE INHIBITOR; MYCOPHENOLIC ACID 2 MORPHOLINOETHYL ESTER; PD 166793; PGE 7113313; RECOMBINANT INTERLEUKIN 10; TISSUE INHIBITOR OF METALLOPROTEINASE; UNCLASSIFIED DRUG;

EID: 77953407314     PISSN: 17568919     EISSN: None     Source Type: Journal    
DOI: 10.4155/fmc.09.83     Document Type: Review
Times cited : (85)

References (146)
  • 2
    • 0038019916 scopus 로고    scopus 로고
    • Structural aspects of the metzincin clan of metalloendopeptidases
    • Gomis-Ruth FX. Structural aspects of the metzincin clan of metalloendopeptidases. Mol. Biotechnol. 24, 157-202 (2003).
    • (2003) Mol. Biotechnol. , vol.24 , pp. 157-202
    • Gomis-Ruth, F.X.1
  • 3
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodeling
    • Page-McCaw A, Ewald AJ, Werb Z. Matrix metalloproteinases and the regulation of tissue remodelling. Nat. Rev. Mol. Cell Biol. 8, 221-233 (2007).
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 221-233
    • Page-Mccaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 5
    • 0037900632 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Old dogs with new tricks
    • Somerville RP, Oblander SA, Apte SS. Matrix metalloproteinases: old dogs with new tricks. Genome Biol. 4, 216 (2003).
    • (2003) Genome Biol , vol.4 , pp. 216
    • Somerville, R.P.1    Oblander, S.A.2    Apte, S.S.3
  • 6
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases: Structure, function, and biochemistry
    • Visse R, Nagase H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ. Res. 92, 827-839 (2003).
    • (2003) Circ. Res. , vol.92 , pp. 827-839
    • Visse, R.1    Nagase, H.2
  • 7
    • 36549085160 scopus 로고    scopus 로고
    • Control of matrix metalloproteinase catalytic activity
    • Ra HJ, Parks WC. Control of matrix metalloproteinase catalytic activity. Matrix Biol. 26, 587-596 (2007).
    • (2007) Matrix Biol , vol.26 , pp. 587-596
    • Ra, H.J.1    Parks, W.C.2
  • 8
    • 0032701633 scopus 로고    scopus 로고
    • Increased myogenic potential and fusion of matrilysin-expressing myoblasts transplanted in mice
    • Caron NJ, Asselin I, Morel G, Tremblay JP. Increased myogenic potential and fusion of matrilysin-expressing myoblasts transplanted in mice. Cell Transplant 8, 465-476 (1999).
    • (1999) Cell Transplant , vol.8 , pp. 465-476
    • Caron, N.J.1    Asselin, I.2    Morel, G.3    Tremblay, J.P.4
  • 9
    • 40949153084 scopus 로고    scopus 로고
    • Induction of MMP-9 expression and endothelial injury by oxidative stress after spinal cord injury
    • Yu F, Kamada H, Niizuma K, Endo H, Chan PH. Induction of MMP-9 expression and endothelial injury by oxidative stress after spinal cord injury. J. Neurotrauma 25, 184-195 (2008).
    • (2008) J. Neurotrauma , vol.25 , pp. 184-195
    • Yu, F.1    Kamada, H.2    Niizuma, K.3    Endo, H.4    Chan, P.H.5
  • 11
    • 42149105217 scopus 로고    scopus 로고
    • Role of melatonin in regulating matrix metalloproteinase-9 via tissue inhibitors of metalloproteinase-1 during protection against endometriosis
    • Paul S, Sharma AV, Mahapatra PD et al. Role of melatonin in regulating matrix metalloproteinase-9 via tissue inhibitors of metalloproteinase-1 during protection against endometriosis. J. Pineal Res. 44, 439-449 (2008).
    • (2008) J. Pineal Res. , vol.44 , pp. 439-449
    • Paul, S.1    Sharma, A.V.2    Mahapatra, P.D.3
  • 12
    • 43849113107 scopus 로고    scopus 로고
    • Placental matrix metalloproteinase-1 expression is increased in labor
    • Vu TD, Yun F, Placido J, Reznik SE. Placental matrix metalloproteinase-1 expression is increased in labor. Reprod. Sci. 15, 420-424 (2008).
    • (2008) Reprod. Sci. , vol.15 , pp. 420-424
    • Vu, T.D.1    Yun, F.2    Placido, J.3    Reznik, S.E.4
  • 14
    • 0035479845 scopus 로고    scopus 로고
    • Matrix metalloproteinases: They're not just for matrix anymore!
    • McCawley LJ, Matrisian LM. Matrix metalloproteinases: they're not just for matrix anymore! Curr. Opin. Cell Biol. 13, 534-540 (2001).
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 534-540
    • McCawley, L.J.1    Matrisian, L.M.2
  • 15
    • 3543134126 scopus 로고    scopus 로고
    • Matrix metalloproteinases as modulators of inflammation and innate immunity
    • Parks WC, Wilson CL, Lopez-Boado YS. Matrix metalloproteinases as modulators of inflammation and innate immunity. Nat. Rev. Immunol. 4, 617-629 (2004).
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 617-629
    • Parks, W.C.1    Wilson, C.L.2    Lopez-Boado, Y.S.3
  • 16
    • 61849140072 scopus 로고    scopus 로고
    • Enhanced activity of very low density lipoprotein receptor II promotes SGC7901 cell proliferation and migration
    • Yang P, Liu Z, Wang H et al. Enhanced activity of very low density lipoprotein receptor II promotes SGC7901 cell proliferation and migration. Life Sci. 84, 402-408 (2009).
    • (2009) Life Sci , vol.84 , pp. 402-408
    • Yang, P.1    Liu, Z.2    Wang, H.3
  • 17
    • 55349131011 scopus 로고    scopus 로고
    • Keratinocyte expression of MMP3 enhances differentiation and prevents tumor establishment
    • McCawley LJ, Wright J, LaFleur BJ, Crawford HC, Matrisian LM. Keratinocyte expression of MMP3 enhances differentiation and prevents tumor establishment. Am. J. Pathol. 173, 1528-1539 (2008).
    • (2008) Am. J. Pathol. , vol.173 , pp. 1528-1539
    • McCawley, L.J.1    Wright, J.2    Lafleur, B.J.3    Crawford, H.C.4    Matrisian, L.M.5
  • 18
    • 59649100885 scopus 로고    scopus 로고
    • Matrix metalloproteinase-1 promotes muscle cell migration and differentiation
    • Wang W, Pan H, Murray K, Jefferson BS, Li Y. Matrix metalloproteinase-1 promotes muscle cell migration and differentiation. Am. J. Pathol. 174, 541-549 (2009).
    • (2009) Am. J. Pathol. , vol.174 , pp. 541-549
    • Wang, W.1    Pan, H.2    Murray, K.3    Jefferson, B.S.4    Li, Y.5
  • 19
    • 25444432778 scopus 로고    scopus 로고
    • Invasion-associated MMP-2 and MMP-9 are up-regulated intracellularly in concert with apoptosis linked to melanoma cell detachment
    • Pereira AM, Strasberg-Rieber M, Rieber M. Invasion-associated MMP-2 and MMP-9 are up-regulated intracellularly in concert with apoptosis linked to melanoma cell detachment. Clin. Exp. Metastasis 22, 285-295 (2005).
    • (2005) Clin. Exp. Metastasis , vol.22 , pp. 285-295
    • Pereira, A.M.1    Strasberg-Rieber, M.2    Rieber, M.3
  • 20
    • 21144455107 scopus 로고    scopus 로고
    • Matrix metalloproteinases mediate b-adrenergic receptor-stimulated apoptosis in adult rat ventricular myocytes
    • Menon B, Singh M, Singh K. Matrix metalloproteinases mediate b-adrenergic receptor-stimulated apoptosis in adult rat ventricular myocytes. Am. J. Physiol. Cell Physiol. 289, C168-C176 (2005).
    • (2005) Am. J. Physiol. Cell Physiol. , vol.289
    • Menon, B.1    Singh, M.2    Singh, K.3
  • 21
    • 70449645644 scopus 로고    scopus 로고
    • A(5) (1) integrin ligand PHSRN induces invasion and a5 mRNA in endothelial cells to stimulate angiogenesis
    • Zeng ZZ, Yao H, Staszewski ED et al. a(5) (1) integrin ligand PHSRN induces invasion and a5 mRNA in endothelial cells to stimulate angiogenesis. Transl. Oncol. 2, 8-20 (2009).
    • (2009) Transl. Oncol. , vol.2 , pp. 8-20
    • Zeng, Z.Z.1    Yao, H.2    Staszewski, E.D.3
  • 22
    • 33847635753 scopus 로고    scopus 로고
    • Activation of proMMP-2 and Src by HHV8 vGPCR in human pulmonary arterial endothelial cells
    • Shan B, Morris CA, Zhuo Y, Shelby BD, Levy DR, Lasky JA. Activation of proMMP-2 and Src by HHV8 vGPCR in human pulmonary arterial endothelial cells. J. Mol. Cell Cardiol. 42, 517-525 (2007).
    • (2007) J. Mol. Cell Cardiol. , vol.42 , pp. 517-525
    • Shan, B.1    Morris, C.A.2    Zhuo, Y.3    Shelby, B.D.4    Levy, D.R.5    Lasky, J.A.6
  • 24
    • 0036800192 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors: Biological actions and therapeutic opportunities
    • Baker AH, Edwards DR, Murphy G. Metalloproteinase inhibitors: biological actions and therapeutic opportunities. J. Cell Sci. 115, 3719-3727 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 3719-3727
    • Baker, A.H.1    Edwards, D.R.2    Murphy, G.3
  • 25
    • 38849148339 scopus 로고    scopus 로고
    • Catalytic properties of ADAM12 and its domain deletion mutants
    • Jacobsen J, Visse R, Sorensen HP et al. Catalytic properties of ADAM12 and its domain deletion mutants. Biochemistry 47, 537-547 (2008).
    • (2008) Biochemistry , vol.47 , pp. 537-547
    • Jacobsen, J.1    Visse, R.2    Sorensen, H.P.3
  • 26
    • 48849107531 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases in cell signaling: Metalloproteinase-independent biological activities
    • Stetler-Stevenson WG. Tissue inhibitors of metalloproteinases in cell signaling: metalloproteinase-independent biological activities. Sci. Signal 1, 6 (2008).
    • (2008) Sci. Signal , vol.1 , pp. 6
    • Stetler-Stevenson, W.G.1
  • 27
    • 58149379612 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 facilitates glial scar formation in the injured spinal cord
    • Hsu JY, Bourguignon LY, Adams CM et al. Matrix metalloproteinase-9 facilitates glial scar formation in the injured spinal cord. J. Neurosci. 28, 13467-13477 (2008).
    • (2008) J. Neurosci. , vol.28 , pp. 13467-13477
    • Hsu, J.Y.1    Bourguignon, L.Y.2    Adams, C.M.3
  • 28
    • 0035900495 scopus 로고    scopus 로고
    • Diminished corneal angiogenesis in gelatinase A-deficient mice
    • Kato T, Kure T, Chang JH et al. Diminished corneal angiogenesis in gelatinase A-deficient mice. FEBS Lett. 508, 187-190 (2001).
    • (2001) FEBS Lett. , vol.508 , pp. 187-190
    • Kato, T.1    Kure, T.2    Chang, J.H.3
  • 29
    • 3442883363 scopus 로고    scopus 로고
    • Structural alterations at the neuromuscular junctions of matrix metalloproteinase 3 null mutant mice
    • VanSaun M, Herrera AA, Werle MJ. Structural alterations at the neuromuscular junctions of matrix metalloproteinase 3 null mutant mice. J. Neurocytol. 32, 1129-1142 (2003).
    • (2003) J. Neurocytol. , vol.32 , pp. 1129-1142
    • Van Saun, M.1    Herrera, A.A.2    Werle, M.J.3
  • 30
    • 0242442568 scopus 로고    scopus 로고
    • An adverse role for matrix metalloproteinase after spinal cord injury in mice
    • Wells JE, Rice TK, Nuttall RK et al. An adverse role for matrix metalloproteinase after spinal cord injury in mice. J. Neurosci. 23, 10107-10115 (2003)
    • (2003) J. Neurosci. , vol.23 , pp. 10107-10115
    • Wells, J.E.1    Rice, T.K.2    Nuttall, R.K.3
  • 31
    • 0034635966 scopus 로고    scopus 로고
    • Impaired endochondral ossification and angiogenesis in mice deficient in membranetype matrix metalloproteinase i
    • Zhou, Z, Apte SS, Soininen R et al. Impaired endochondral ossification and angiogenesis in mice deficient in membranetype matrix metalloproteinase I. Proc. Natl Acad. Sci. USA 97, 4052-4057 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 4052-4057
    • Zhou, Z.1    Apte, S.S.2    Soininen, R.3
  • 33
    • 6444240024 scopus 로고    scopus 로고
    • TIMP-3 deficiency leads to dilated cardiomyopathy
    • Fedak PW, Smookler DS, Kassiri Z et al. TIMP-3 deficiency leads to dilated cardiomyopathy. Circulation 110, 2401-2409 (2004).
    • (2004) Circulation , vol.110 , pp. 2401-2409
    • Fedak, P.W.1    Smookler, D.S.2    Kassiri, Z.3
  • 34
    • 0030939391 scopus 로고    scopus 로고
    • Amphibian limb regeneration: Rebuilding a complex structure
    • Brockes JP. Amphibian limb regeneration: rebuilding a complex structure. Science 276, 81-87 (1997).
    • (1997) Science , vol.276 , pp. 81-87
    • Brockes, J.P.1
  • 35
    • 36549041410 scopus 로고    scopus 로고
    • Initiation of limb regeneration: The critical steps for regenerative capacity
    • Yokoyama H. Initiation of limb regeneration: the critical steps for regenerative capacity. Dev. Growth Differ. 50, 13-22 (2008).
    • (2008) Dev. Growth Differ. , vol.50 , pp. 13-22
    • Yokoyama, H.1
  • 36
    • 39249084246 scopus 로고    scopus 로고
    • Development and regeneration of the neonatal digit tip in mice
    • Han M, Yang X, Lee J, Allan CH, Muneoka K. Development and regeneration of the neonatal digit tip in mice. Dev. Biol. 315, 125-135 (2008).
    • (2008) Dev. Biol. , vol.315 , pp. 125-135
    • Han, M.1    Yang, X.2    Lee, J.3    Allan, C.H.4    Muneoka, K.5
  • 37
    • 0027469631 scopus 로고
    • Regeneration of the distal phalanx. A case report
    • Vidal P, Dickson MG. Regeneration of the distal phalanx. A case report. J. Hand Surg. [Br.] 18, 230-233 (1993).
    • (1993) J. Hand Surg. [Br.] , vol.18 , pp. 230-233
    • Vidal, P.1    Dickson, M.G.2
  • 38
    • 33646087460 scopus 로고    scopus 로고
    • Reverse homodigital artery flap coverage for bone and nailbed grafts in fingertip amputations
    • Alagoz MS, Uysal CA, Kerem M, Sensoz O. Reverse homodigital artery flap coverage for bone and nailbed grafts in fingertip amputations. Ann. Plast. Surg. 56, 279-283 (2006).
    • (2006) Ann. Plast. Surg. , vol.56 , pp. 279-283
    • Alagoz, M.S.1    Uysal, C.A.2    Kerem, M.3    Sensoz, O.4
  • 39
    • 37349061391 scopus 로고    scopus 로고
    • Interaction between macrophages TGF-b1 and the COX-2 pathway during the inflammatory phase of skeletal muscle healing after injury
    • Shen W, Li Y, Zhu J, Schwendener R, Huard J. Interaction between macrophages, TGF-b1, and the COX-2 pathway during the inflammatory phase of skeletal muscle healing after injury. J. Cell Physiol. 214, 405-412 (2008).
    • (2008) J. Cell Physiol. , vol.214 , pp. 405-412
    • Shen, W.1    Li, Y.2    Zhu, J.3    Schwendener, R.4    Huard, J.5
  • 40
    • 43049092274 scopus 로고    scopus 로고
    • Metalloproteinases and their inhibitors: Regulators of wound healing
    • Gill SE, Parks WC. Metalloproteinases and their inhibitors: regulators of wound healing. Int. J. Biochem. Cell Biol. 40, 1334-1347 (2008).
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 1334-1347
    • Gill, S.E.1    Parks, W.C.2
  • 41
    • 38549093209 scopus 로고    scopus 로고
    • Wound epidermis formation and function in urodele amphibian limb regeneration
    • Campbell LJ, Crews CM. Wound epidermis formation and function in urodele amphibian limb regeneration. Cell Mol. Life Sci. 65, 73-79 (2008).
    • (2008) Cell Mol. Life Sci. , vol.65 , pp. 73-79
    • Campbell, L.J.1    Crews, C.M.2
  • 42
    • 1242293760 scopus 로고    scopus 로고
    • Transforming growth factor-b1 induces the differentiation of myogenic cells into fibrotic cells in injured skeletal muscle: A key event in muscle fibrogenesis
    • Li Y, Foster W, Deasy BM et al. Transforming growth factor-b1 induces the differentiation of myogenic cells into fibrotic cells in injured skeletal muscle: a key event in muscle fibrogenesis. Am. J. Pathol. 164, 1007-1019 (2004).
    • (2004) Am. J. Pathol. , vol.164 , pp. 1007-1019
    • Li, Y.1    Foster, W.2    Deasy, B.M.3
  • 43
    • 0029901914 scopus 로고    scopus 로고
    • Cloning and characterization of cDNAs for matrix metalloproteinases of regenerating newt limbs
    • Miyazaki K, Uchiyama K, Imokawa Y, Yoshizato K. Cloning and characterization of cDNAs for matrix metalloproteinases of regenerating newt limbs. Proc. Natl Acad. Sci. USA 93, 6819-6824 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 6819-6824
    • Miyazaki, K.1    Uchiyama, K.2    Imokawa, Y.3    Yoshizato, K.4
  • 44
    • 56849108439 scopus 로고    scopus 로고
    • Regulation of dermal fibroblast dedifferentiation and redifferentiation during wound healing and limb regeneration in the Axolotl
    • Satoh A, Bryant SV, Gardiner DM. Regulation of dermal fibroblast dedifferentiation and redifferentiation during wound healing and limb regeneration in the Axolotl. Dev. Growth Differ. 50, 743-754 (2008).
    • (2008) Dev. Growth Differ. , vol.50 , pp. 743-754
    • Satoh, A.1    Bryant, S.V.2    Gardiner, D.M.3
  • 46
    • 0032835964 scopus 로고    scopus 로고
    • Expression of Mmp-9 and related matrix metalloproteinase genes during axolotl limb regeneration
    • Yang EV, Gardiner DM, Carlson MR, Nugas CA, Bryant SV. Expression of Mmp-9 and related matrix metalloproteinase genes during axolotl limb regeneration. Dev. Dyn. 216, 2-9 (1999).
    • (1999) Dev. Dyn. , vol.216 , pp. 2-9
    • Yang, E.V.1    Gardiner, D.M.2    Carlson, M.R.3    Nugas, C.A.4    Bryant, S.V.5
  • 47
    • 0023889680 scopus 로고
    • Retinoic acid coordinately proximalizes regenerate pattern and blastema differential affinity in axolotl limbs
    • Crawford K, Stocum DL. Retinoic acid coordinately proximalizes regenerate pattern and blastema differential affinity in axolotl limbs. Development 102, 687-698 (1988).
    • (1988) Development , vol.102 , pp. 687-698
    • Crawford, K.1    Stocum, D.L.2
  • 48
    • 44749084588 scopus 로고    scopus 로고
    • Three genes control the timing, the site and the size of blastema formation in Drosophila
    • McClure KD, Sustar A, Schubiger G. Three genes control the timing, the site and the size of blastema formation in Drosophila. Dev. Biol. 319, 68-77 (2008).
    • (2008) Dev. Biol. , vol.319 , pp. 68-77
    • McClure, K.D.1    Sustar, A.2    Schubiger, G.3
  • 49
    • 0037308876 scopus 로고    scopus 로고
    • Matrix metalloproteinase activity correlates with blastema formation in the regenerating MRL mouse ear hole model
    • Gourevitch D, Clark L, Chen P, Seitz A, Samulewicz SJ, Heber-Katz E. Matrix metalloproteinase activity correlates with blastema formation in the regenerating MRL mouse ear hole model. Dev. Dyn. 226, 377-387 (2003).
    • (2003) Dev. Dyn. , vol.226 , pp. 377-387
    • Gourevitch, D.1    Clark, L.2    Chen, P.3    Seitz, A.4    Samulewicz, S.J.5    Heber-Katz, E.6
  • 50
    • 20744449197 scopus 로고    scopus 로고
    • Matrix metalloproteinase expression and function during fin regeneration in zebrafish: Analysis of MT1-MMP MMP2 and TIMP2
    • Bai S, Thummel R, Godwin AR et al. Matrix metalloproteinase expression and function during fin regeneration in zebrafish: analysis of MT1-MMP, MMP2 and TIMP2. Matrix Biol. 24, 247-260 (2005).
    • (2005) Matrix Biol , vol.24 , pp. 247-260
    • Bai, S.1    Thummel, R.2    Godwin, A.R.3
  • 52
    • 0036563345 scopus 로고    scopus 로고
    • Muscle injuries and repair: Current trends in research
    • Huard J, Li Y, Fu FH. Muscle injuries and repair: current trends in research. J. Bone Joint Surg. Am. 84, 822-832 (2002).
    • (2002) J. Bone Joint Surg. Am. , vol.84 , pp. 822-832
    • Huard, J.1    Li, Y.2    Fu, F.H.3
  • 53
    • 56249106504 scopus 로고    scopus 로고
    • Improved muscle healing after contusion injury by the inhibitory effect of suramin on myostatin, a negative regulator of muscle growth
    • Nozaki M, Li Y, Zhu J et al. Improved muscle healing after contusion injury by the inhibitory effect of suramin on myostatin, a negative regulator of muscle growth. Am. J. Sports Med. 36, 2354-2362 (2008).
    • (2008) Am. J. Sports Med. , vol.36 , pp. 2354-2362
    • Nozaki, M.1    Li, Y.2    Zhu, J.3
  • 54
    • 11144293690 scopus 로고    scopus 로고
    • The use of suramin, an antifibrotic agent, to improve muscle recovery after strain injury
    • Chan YS, Li Y, Foster W, Fu FH, Huard J. The use of suramin, an antifibrotic agent, to improve muscle recovery after strain injury. Am. J. Sports Med. 33, 43-51 (2005).
    • (2005) Am. J. Sports Med. , vol.33 , pp. 43-51
    • Chan, Y.S.1    Li, Y.2    Foster, W.3    Fu, F.H.4    Huard, J.5
  • 55
    • 34547801173 scopus 로고    scopus 로고
    • Implication of the satellite cell in dystrophic muscle fibrosis: A self-perpetuating mechanism of collagen overproduction
    • Alexakis C, Partridge T, Bou-Gharios G. Implication of the satellite cell in dystrophic muscle fibrosis: a self-perpetuating mechanism of collagen overproduction. Am. J. Physiol. Cell Physiol. 293, C661-C669 (2007).
    • (2007) Am. J. Physiol. Cell Physiol. , vol.293
    • Alexakis, C.1    Partridge, T.2    Bou-Gharios, G.3
  • 56
    • 0042933778 scopus 로고    scopus 로고
    • Improvement of muscle healing through enhancement of muscle regeneration and prevention of fibrosis
    • Sato K, Li Y, Foster W et al. Improvement of muscle healing through enhancement of muscle regeneration and prevention of fibrosis. Muscle Nerve 28, 365-372 (2003).
    • (2003) Muscle Nerve , vol.28 , pp. 365-372
    • Sato, K.1    Li, Y.2    Foster, W.3
  • 57
    • 0042889170 scopus 로고    scopus 로고
    • G-interferon as an antifibrosis agent in skeletal muscle
    • Foster W, Li Y, Usas A, Somogyi G, Huard J. g-interferon as an antifibrosis agent in skeletal muscle. J. Orthop. Res. 21, 798-804 (2003).
    • (2003) J. Orthop. Res. , vol.21 , pp. 798-804
    • Foster, W.1    Li, Y.2    Usas, A.3    Somogyi, G.4    Huard, J.5
  • 58
    • 34548072165 scopus 로고    scopus 로고
    • Decorin gene transfer promotes muscle cell differentiation and muscle regeneration
    • Li Y, Li J, Zhu J et al. Decorin gene transfer promotes muscle cell differentiation and muscle regeneration. Mol. Ther. 15, 1616-1622 (2007).
    • (2007) Mol. Ther. , vol.15 , pp. 1616-1622
    • Li, Y.1    Li, J.2    Zhu, J.3
  • 59
    • 47649130898 scopus 로고    scopus 로고
    • Angiotensin II receptor blockade administered after injury improves muscle regeneration and decreases fibrosis in normal skeletal muscle
    • Bedair HS, Karthikeyan T, Quintero A, Li Y, Huard J. Angiotensin II receptor blockade administered after injury improves muscle regeneration and decreases fibrosis in normal skeletal muscle. Am. J. Sports Med. 36, 1548-1554 (2008).
    • (2008) Am. J. Sports Med. , vol.36 , pp. 1548-1554
    • Bedair, H.S.1    Karthikeyan, T.2    Quintero, A.3    Li, Y.4    Huard, J.5
  • 60
    • 34447544484 scopus 로고    scopus 로고
    • Matrix metalloproteinase-1 therapy improves muscle healing
    • Bedair H, Liu TT, Kaar JL et al. Matrix metalloproteinase-1 therapy improves muscle healing. J. Appl. Physiol. 102, 2338-2345 (2007).
    • (2007) J. Appl. Physiol. , vol.102 , pp. 2338-2345
    • Bedair, H.1    Liu, T.T.2    Kaar, J.L.3
  • 61
    • 48449107036 scopus 로고    scopus 로고
    • Matrix metalloproteinase-1 treatment of muscle fibrosis
    • Kaar JL, Li Y, Blair HC et al. Matrix metalloproteinase-1 treatment of muscle fibrosis. Acta Biomater. 4, 1411-1420 (2008).
    • (2008) Acta Biomater , vol.4 , pp. 1411-1420
    • Kaar, J.L.1    Li, Y.2    Blair, H.C.3
  • 63
    • 0344420226 scopus 로고    scopus 로고
    • Pharmacokinetic and biodistribution properties of poly(ethylene glycol)-protein conjugates
    • Caliceti P, Veronese FM. Pharmacokinetic and biodistribution properties of poly(ethylene glycol)-protein conjugates. Adv. Drug Deliv. Rev. 55, 1261-1277 (2003).
    • (2003) Adv. Drug Deliv. Rev. , vol.55 , pp. 1261-1277
    • Caliceti, P.1    Veronese, F.M.2
  • 64
    • 19644367664 scopus 로고    scopus 로고
    • Synthetic biomaterials as instructive extracellular microenvironments for morphogenesis in tissue engineering
    • Lutolf MP, Hubbell JA. Synthetic biomaterials as instructive extracellular microenvironments for morphogenesis in tissue engineering. Nat. Biotechnol. 23, 47-55 (2005).
    • (2005) Nat. Biotechnol. , vol.23 , pp. 47-55
    • Lutolf, M.P.1    Hubbell, J.A.2
  • 65
    • 0037965624 scopus 로고    scopus 로고
    • Synthetic matrix metalloproteinasesensitive hydrogels for the conduction of tissue regeneration: Engineering cell-invasion characteristics
    • Lutolf MP, Lauer-Fields JL, Schmoekel HG et al. Synthetic matrix metalloproteinasesensitive hydrogels for the conduction of tissue regeneration: engineering cell-invasion characteristics. Proc. Natl Acad. Sci. USA 100, 5413-5418 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 5413-5418
    • Lutolf, M.P.1    Lauer-Fields, J.L.2    Schmoekel, H.G.3
  • 66
    • 54049153108 scopus 로고    scopus 로고
    • DNA delivery from matrix metalloproteinase degradable poly(ethylene glycol) hydrogels to mouse cloned mesenchymal stem cells
    • Lei Y, Segura T. DNA delivery from matrix metalloproteinase degradable poly(ethylene glycol) hydrogels to mouse cloned mesenchymal stem cells. Biomaterials 30, 254-265 (2009).
    • (2009) Biomaterials , vol.30 , pp. 254-265
    • Lei, Y.1    Segura, T.2
  • 68
    • 44849127317 scopus 로고    scopus 로고
    • L-arginine decreases inflammation and modulates the nuclear factor-kB/matrix metalloproteinase cascade in mdx muscle fibers
    • Hnia K, Gayraud J, Hugon G et al. l-arginine decreases inflammation and modulates the nuclear factor-kB/matrix metalloproteinase cascade in mdx muscle fibers. Am. J. Pathol. 172, 1509-1519 (2008).
    • (2008) Am. J. Pathol. , vol.172 , pp. 1509-1519
    • Hnia, K.1    Gayraud, J.2    Hugon, G.3
  • 69
    • 42549110017 scopus 로고    scopus 로고
    • Pattern of metalloprotease activity and myofiber regeneration in skeletal muscles of mdx mice
    • Bani C, Lagrota-Candido J, Pinheiro DF et al. Pattern of metalloprotease activity and myofiber regeneration in skeletal muscles of mdx mice. Muscle Nerve 37, 583-592 (2008).
    • (2008) Muscle Nerve , vol.37 , pp. 583-592
    • Bani, C.1    Lagrota-Candido, J.2    Pinheiro, D.F.3
  • 70
    • 42349115741 scopus 로고    scopus 로고
    • Distinct patterns of MMP-9 and MMP-2 activity in slow and fast twitch skeletal muscle regeneration in vivo
    • Zimowska M, Brzoska E, Swierczynska M, Streminska W, Moraczewski J. Distinct patterns of MMP-9 and MMP-2 activity in slow and fast twitch skeletal muscle regeneration in vivo. Int. J. Dev. Biol. 52, 307-314 (2008).
    • (2008) Int. J. Dev. Biol. , vol.52 , pp. 307-314
    • Zimowska, M.1    Brzoska, E.2    Swierczynska, M.3    Streminska, W.4    Moraczewski, J.5
  • 71
    • 34447620885 scopus 로고    scopus 로고
    • Activation and localization of matrix metalloproteinase-2 and -9 in the skeletal muscle of the muscular dystrophy dog (CXMDJ)
    • Fukushima K, Nakamura A, Ueda H et al. Activation and localization of matrix metalloproteinase-2 and -9 in the skeletal muscle of the muscular dystrophy dog (CXMDJ). BMC Musculoskelet. Disord. 8, 54 (2007).
    • (2007) BMC Musculoskelet. Disord. , vol.8 , pp. 54
    • Fukushima, K.1    Nakamura, A.2    Ueda, H.3
  • 72
    • 33750325693 scopus 로고    scopus 로고
    • Multifunctional roles of MT1-MMP in myofiber formation and morphostatic maintenance of skeletal muscle
    • Ohtake Y, Tojo H, Seiki M. Multifunctional roles of MT1-MMP in myofiber formation and morphostatic maintenance of skeletal muscle. J. Cell Sci. 119, 3822-3832 (2006).
    • (2006) J. Cell Sci. , vol.119 , pp. 3822-3832
    • Ohtake, Y.1    Tojo, H.2    Seiki, M.3
  • 73
    • 35848930382 scopus 로고    scopus 로고
    • Overexpression of osteoactivin protects skeletal muscle from severe degeneration caused by long-term denervation in mice
    • Furochi H, Tamura S, Takeshima K et al. Overexpression of osteoactivin protects skeletal muscle from severe degeneration caused by long-term denervation in mice. J. Med. Invest. 54, 248-254 (2007).
    • (2007) J. Med. Invest. , vol.54 , pp. 248-254
    • Furochi, H.1    Tamura, S.2    Takeshima, K.3
  • 75
    • 54949105397 scopus 로고    scopus 로고
    • Repair and neurorehabilitation strategies for spinal cord injury
    • Ruff RL, McKerracher L, Selzer ME. Repair and neurorehabilitation strategies for spinal cord injury. Ann. NY Acad. Sci. 1142, 1-20 (2008).
    • (2008) Ann. NY Acad. Sci. , vol.1142 , pp. 1-20
    • Ruff, R.L.1    McKerracher, L.2    Selzer, M.E.3
  • 76
    • 40849137609 scopus 로고    scopus 로고
    • Comparison of blood-nerve barrier disruption and matrix metalloprotease-9 expression in injured central and peripheral nerves in mice
    • n Examines how MMP9 expression varied between injuries to the central and peripheral nervous systems.
    • Liu LY, Zheng H, Xiao HL et al. Comparison of blood-nerve barrier disruption and matrix metalloprotease-9 expression in injured central and peripheral nerves in mice. Neurosci. Lett. 434, 155-159 (2008). n Examines how MMP9 expression varied between injuries to the central and peripheral nervous systems.
    • (2008) Neurosci. Lett. , vol.434 , pp. 155-159
    • Liu, L.Y.1    Zheng, H.2    Xiao, H.L.3
  • 77
    • 60249091457 scopus 로고    scopus 로고
    • The role of biodegradable engineered scaffolds seeded with Schwann cells for spinal cord regeneration
    • Tabesh H, Amoabediny G, Nik NS et al. The role of biodegradable engineered scaffolds seeded with Schwann cells for spinal cord regeneration. Neurochem. Int. 54, 73-83 (2009).
    • (2009) Neurochem. Int. , vol.54 , pp. 73-83
    • Tabesh, H.1    Amoabediny, G.2    Nik, N.S.3
  • 78
    • 33845332735 scopus 로고    scopus 로고
    • The cellular inflammatory response in human spinal cords after injury
    • Fleming JC, Norenberg MD, Ramsay DA et al. The cellular inflammatory response in human spinal cords after injury. Brain 129, 3249-3269 (2006).
    • (2006) Brain , vol.129 , pp. 3249-3269
    • Fleming, J.C.1    Norenberg, M.D.2    Ramsay, D.A.3
  • 79
    • 33749174156 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 facilitates wound healing events that promote functional recovery after spinal cord injury
    • Hsu JY, McKeon R, Goussev S et al. Matrix metalloproteinase-2 facilitates wound healing events that promote functional recovery after spinal cord injury. J. Neurosci. 26, 9841-9850 (2006).
    • (2006) J. Neurosci. , vol.26 , pp. 9841-9850
    • Hsu, J.Y.1    McKeon, R.2    Goussev, S.3
  • 80
    • 65549167522 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 is involved in myelination of dorsal root ganglia neurons
    • Lehmann HC, Kohne A, Bernal F et al. Matrix metalloproteinase-2 is involved in myelination of dorsal root ganglia neurons. Glia 57, 479-489 (2009).
    • (2009) Glia , vol.57 , pp. 479-489
    • Lehmann, H.C.1    Kohne, A.2    Bernal, F.3
  • 82
    • 70349153456 scopus 로고    scopus 로고
    • MMP-9 controls Schwann cell proliferation and phenotypic remodeling via IGF-1 and ErbB receptor-mediated activation of MEK/ERK pathway
    • Chattopadhya S, Shubayev VI. MMP-9 controls Schwann cell proliferation and phenotypic remodeling via IGF-1 and ErbB receptor-mediated activation of MEK/ERK pathway. Glia 57(12), 1316-1325 (2009).
    • (2009) Glia , vol.57 , Issue.12 , pp. 1316-1325
    • Chattopadhya, S.1    Shubayev, V.I.2
  • 83
    • 57449109542 scopus 로고    scopus 로고
    • Axon regeneration inhibitors
    • Yang LJ, Schnaar RL. Axon regeneration inhibitors. Neurol. Res. 30, 1047-1052 (2008).
    • (2008) Neurol. Res. , vol.30 , pp. 1047-1052
    • Yang, L.J.1    Schnaar, R.L.2
  • 84
    • 35348972941 scopus 로고    scopus 로고
    • Neural MMP-28 expression precedes myelination during development and peripheral nerve repair
    • Werner SR, Mescher AL, Neff AW et al. Neural MMP-28 expression precedes myelination during development and peripheral nerve repair. Dev. Dyn. 236, 2852-2864 (2007).
    • (2007) Dev. Dyn. , vol.236 , pp. 2852-2864
    • Werner, S.R.1    Mescher, A.L.2    Neff, A.W.3
  • 85
    • 6344252618 scopus 로고    scopus 로고
    • Key metalloproteinases are expressed by specific cell types in experimental autoimmune encephalomyelitis
    • Toft-Hansen H, Nuttall RK, Edwards DR, Owens T. Key metalloproteinases are expressed by specific cell types in experimental autoimmune encephalomyelitis. J. Immunol. 173, 5209-5218 (2004).
    • (2004) J. Immunol. , vol.173 , pp. 5209-5218
    • Toft-Hansen, H.1    Nuttall, R.K.2    Edwards, D.R.3    Owens, T.4
  • 86
    • 34248392684 scopus 로고    scopus 로고
    • Microglial activation and its implications in the brain diseases
    • Dheen ST, Kaur C, Ling EA. Microglial activation and its implications in the brain diseases. Curr. Med. Chem. 14, 1189-1197 (2007).
    • (2007) Curr. Med. Chem. , vol.14 , pp. 1189-1197
    • Dheen, S.T.1    Kaur, C.2    Ling, E.A.3
  • 87
    • 36148965872 scopus 로고    scopus 로고
    • Downregulation of membrane type-matrix metalloproteinases in the inflamed or injured central nervous system
    • Toft-Hansen H, Babcock AA, Millward JM, Owens T. Downregulation of membrane type-matrix metalloproteinases in the inflamed or injured central nervous system. J. Neuroinflammation 4, 24 (2007).
    • (2007) J. Neuroinflammation , vol.4 , pp. 24
    • Toft-Hansen, H.1    Babcock, A.A.2    Millward, J.M.3    Owens, T.4
  • 88
    • 0030934532 scopus 로고    scopus 로고
    • Wound healing - Aiming for perfect skin regeneration
    • Martin P. Wound healing - aiming for perfect skin regeneration. Science 276, 75-81 (1997).
    • (1997) Science , vol.276 , pp. 75-81
    • Martin, P.1
  • 89
    • 0031784503 scopus 로고    scopus 로고
    • Patterns of matrix metalloproteinase and TIMP expression in chronic ulcers
    • Saarialho-Kere UK. Patterns of matrix metalloproteinase and TIMP expression in chronic ulcers. Arch. Dermatol. Res. 290(Suppl.), S47-S54 (1998).
    • (1998) Arch. Dermatol. Res. , vol.290 , Issue.SUPPL.
    • Saarialho-Kere, U.K.1
  • 90
    • 0028262145 scopus 로고
    • Expression of matrix metalloproteinase-2 and -9 during early human wound healing
    • Salo T, Makela M, Kylmaniemi M, Autio-Harmainen H, Larjava H. Expression of matrix metalloproteinase-2 and -9 during early human wound healing. Lab. Invest. 70, 176-182 (1994).
    • (1994) Lab. Invest. , vol.70 , pp. 176-182
    • Salo, T.1    Makela, M.2    Kylmaniemi, M.3    Autio-Harmainen, H.4    Larjava, H.5
  • 91
    • 0026492897 scopus 로고
    • Distinct localization of collagenase and tissue inhibitor of metalloproteinases expression in wound healing associated with ulcerative pyogenic granuloma
    • Saarialho-Kere UK, Chang ES, Welgus HG, Parks WC. Distinct localization of collagenase and tissue inhibitor of metalloproteinases expression in wound healing associated with ulcerative pyogenic granuloma. J. Clin. Invest. 90, 1952-1957 (1992).
    • (1992) J. Clin. Invest. , vol.90 , pp. 1952-1957
    • Saarialho-Kere, U.K.1    Chang, E.S.2    Welgus, H.G.3    Parks, W.C.4
  • 92
    • 0025058397 scopus 로고
    • Enhanced synthesis of collagenase by human keratinocytes cultured on type i or type IV collagen
    • Petersen MJ, Woodley DT, Stricklin GP, O'Keefe EJ. Enhanced synthesis of collagenase by human keratinocytes cultured on type I or type IV collagen. J. Invest. Dermatol. 94, 341-346 (1990).
    • (1990) J. Invest. Dermatol. , vol.94 , pp. 341-346
    • Petersen, M.J.1    Woodley, D.T.2    Stricklin, G.P.3    O'Keefe, E.J.4
  • 94
    • 0032800451 scopus 로고    scopus 로고
    • Differential expression of tissue inhibitors of metalloproteinases (TIMP-1, -2, -3, and -4) in normal and aberrant wound healing
    • Vaalamo M, Leivo T, Saarialho-Kere U. Differential expression of tissue inhibitors of metalloproteinases (TIMP-1, -2, -3, and -4) in normal and aberrant wound healing. Hum. Pathol. 30, 795-802 (1999).
    • (1999) Hum. Pathol. , vol.30 , pp. 795-802
    • Vaalamo, M.1    Leivo, T.2    Saarialho-Kere, U.3
  • 95
    • 59149104284 scopus 로고    scopus 로고
    • Proteinases in cutaneous wound healing
    • Toriseva M, Kahari VM. Proteinases in cutaneous wound healing. Cell Mol. Life Sci. 66, 203-224 (2009).
    • (2009) Cell Mol. Life Sci. , vol.66 , pp. 203-224
    • Toriseva, M.1    Kahari, V.M.2
  • 96
    • 0009809218 scopus 로고    scopus 로고
    • Biochemical analysis of acute and chronic wound environments
    • Tarnuzzer RW, Schultz GS. Biochemical analysis of acute and chronic wound environments. Wound Repair Regen. 4, 321-325 (1996).
    • (1996) Wound Repair Regen , vol.4 , pp. 321-325
    • Tarnuzzer, R.W.1    Schultz, G.S.2
  • 97
    • 0027202705 scopus 로고
    • Wound fluid from chronic leg ulcers contains elevated levels of metalloproteinases MMP-2 and MMP-9
    • Wysocki AB, Staiano-Coico L, Grinnell F. Wound fluid from chronic leg ulcers contains elevated levels of metalloproteinases MMP-2 and MMP-9. J. Invest. Dermatol. 101, 64-68 (1993).
    • (1993) J. Invest. Dermatol. , vol.101 , pp. 64-68
    • Wysocki, A.B.1    Staiano-Coico, L.2    Grinnell, F.3
  • 98
    • 0032952556 scopus 로고    scopus 로고
    • Enhanced expression of human metalloelastase (MMP-12) in cutaneous granulomas and macrophage migration
    • Vaalamo M, Kariniemi AL, Shapiro SD, Saarialho-Kere U. Enhanced expression of human metalloelastase (MMP-12) in cutaneous granulomas and macrophage migration. J. Invest. Dermatol. 112, 499-505 (1999).
    • (1999) J. Invest. Dermatol. , vol.112 , pp. 499-505
    • Vaalamo, M.1    Kariniemi, A.L.2    Shapiro, S.D.3    Saarialho-Kere, U.4
  • 99
    • 34547526317 scopus 로고    scopus 로고
    • Regenerative healing in fetal skin: A review of the literature
    • Wilgus TA. Regenerative healing in fetal skin: a review of the literature. Ostomy. Wound Manage. 53, 16-33 (2007).
    • (2007) Ostomy. Wound Manage. , vol.53 , pp. 16-33
    • Wilgus, T.A.1
  • 100
    • 0037981628 scopus 로고    scopus 로고
    • Scarless fetal wounds are associated with an increased matrix metalloproteinase-to-tissue-derived inhibitor of metalloproteinase ratio
    • Dang CM, Beanes SR, Lee H, Zhang X, Soo C, Ting K. Scarless fetal wounds are associated with an increased matrix metalloproteinase-to-tissue-derived inhibitor of metalloproteinase ratio. Plast. Reconstr. Surg. 111, 2273-2285 (2003).
    • (2003) Plast. Reconstr. Surg. , vol.111 , pp. 2273-2285
    • Dang, C.M.1    Beanes, S.R.2    Lee, H.3    Zhang, X.4    Soo, C.5    Ting, K.6
  • 101
    • 46049091539 scopus 로고    scopus 로고
    • Neurotrophic regulation of epidermal dedifferentiation during wound healing and limb regeneration in the axolotl (Ambystoma mexicanum)
    • Satoh A, Graham GM, Bryant SV, Gardiner DM. Neurotrophic regulation of epidermal dedifferentiation during wound healing and limb regeneration in the axolotl (Ambystoma mexicanum). Dev. Biol. 319, 321-335 (2008).
    • (2008) Dev. Biol. , vol.319 , pp. 321-335
    • Satoh, A.1    Graham, G.M.2    Bryant, S.V.3    Gardiner, D.M.4
  • 102
    • 33751006970 scopus 로고    scopus 로고
    • Matrix metalloproteinase 9 (MMP-9) is upregulated during scarless wound healing in athymic nude mice
    • Manuel JA, Gawronska-Kozak B. Matrix metalloproteinase 9 (MMP-9) is upregulated during scarless wound healing in athymic nude mice. Matrix Biol. 25, 505-514 (2006).
    • (2006) Matrix Biol. , vol.25 , pp. 505-514
    • Manuel, J.A.1    Gawronska-Kozak, B.2
  • 103
    • 34147115103 scopus 로고    scopus 로고
    • Differential expression of matrix metalloproteinases and tissue-derived inhibitors of metalloproteinase in fetal and adult skins
    • Chen W, Fu X, Ge S, Sun T, Sheng Z. Differential expression of matrix metalloproteinases and tissue-derived inhibitors of metalloproteinase in fetal and adult skins. Int. J. Biochem. Cell Biol. 39, 997-1005 (2007).
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 997-1005
    • Chen, W.1    Fu, X.2    Ge, S.3    Sun, T.4    Sheng, Z.5
  • 104
    • 38849145080 scopus 로고    scopus 로고
    • Effects of basic fibroblast growth factor on the expression of extracellular matrix and matrix metalloproteinase-1 in wound healing
    • Xie J, Bian H, Qi S et al. Effects of basic fibroblast growth factor on the expression of extracellular matrix and matrix metalloproteinase-1 in wound healing. Clin. Exp. Dermatol. 33, 176-182 (2008).
    • (2008) Clin. Exp. Dermatol. , vol.33 , pp. 176-182
    • Xie, J.1    Bian, H.2    Qi, S.3
  • 105
    • 52149094789 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2 improves the transplanted adipocyte survival in mice
    • Kuramochi D, Unoki H, Bujo H et al. Matrix metalloproteinase 2 improves the transplanted adipocyte survival in mice. Eur. J. Clin. Invest. 38, 752-759 (2008).
    • (2008) Eur. J. Clin. Invest. , vol.38 , pp. 752-759
    • Kuramochi, D.1    Unoki, H.2    Bujo, H.3
  • 106
    • 1842583836 scopus 로고    scopus 로고
    • Gene expression profiles from hypertrophic scar fibroblasts before and after IL-6 stimulation
    • Dasu MR, Hawkins HK, Barrow RE, Xue H, Herndon DN. Gene expression profiles from hypertrophic scar fibroblasts before and after IL-6 stimulation. J. Pathol. 202, 476-485 (2004).
    • (2004) J. Pathol. , vol.202 , pp. 476-485
    • Dasu, M.R.1    Hawkins, H.K.2    Barrow, R.E.3    Xue, H.4    Herndon, D.N.5
  • 107
    • 1342324179 scopus 로고    scopus 로고
    • TGF b-like regulation of matrix metalloproteinases by anti-transforming growth factor-b, and anti-transforming growth factor-b1 antibodies in dermal fibroblasts: Implications for wound healing
    • Philips N, Keller T, Gonzalez S. TGF b-like regulation of matrix metalloproteinases by anti-transforming growth factor-b, and anti-transforming growth factor-b1 antibodies in dermal fibroblasts: implications for wound healing. Wound Repair Regen. 12, 53-59 (2004).
    • (2004) Wound Repair Regen , vol.12 , pp. 53-59
    • Philips, N.1    Keller, T.2    Gonzalez, S.3
  • 108
    • 63249134788 scopus 로고    scopus 로고
    • Effects of bicyclol on liver regeneration after partial hepatectomy in rats
    • Yao XM, Zhao J, Li Y. Effects of bicyclol on liver regeneration after partial hepatectomy in rats. Dig. Dis. Sci. 54, 774-781 (2009).
    • (2009) Dig. Dis. Sci. , vol.54 , pp. 774-781
    • Yao, X.M.1    Zhao, J.2    Li, Y.3
  • 109
    • 0026033871 scopus 로고
    • Human liver regeneration after major hepatectomy. A study of liver volume by computed tomography
    • Chen MF, Hwang TL, Hung CF. Human liver regeneration after major hepatectomy. A study of liver volume by computed tomography. Ann. Surg. 213, 227-229 (1991).
    • (1991) Ann. Surg. , vol.213 , pp. 227-229
    • Chen, M.F.1    Hwang, T.L.2    Hung, C.F.3
  • 110
    • 0037308337 scopus 로고    scopus 로고
    • Delivery of matrix metalloproteinase-1 attenuates established liver fibrosis in the rat
    • Iimuro Y, Nishio T, Morimoto T et al. Delivery of matrix metalloproteinase-1 attenuates established liver fibrosis in the rat. Gastroenterology 124, 445-458 (2003).
    • (2003) Gastroenterology , vol.124 , pp. 445-458
    • Iimuro, Y.1    Nishio, T.2    Morimoto, T.3
  • 111
    • 0031915552 scopus 로고    scopus 로고
    • Fibrogenic effect of oxidative stress on rat hepatic stellate cells
    • Svegliati-Baroni G, D'Ambrosio L, Ferretti G et al. Fibrogenic effect of oxidative stress on rat hepatic stellate cells. Hepatology 27, 720-726 (1998).
    • (1998) Hepatology , vol.27 , pp. 720-726
    • Svegliati-Baroni, G.1    D'Ambrosio, L.2    Ferretti, G.3
  • 113
    • 34250322265 scopus 로고    scopus 로고
    • A matrix metalloproteinase-9 activation cascade by hepatic stellate cells in trans-differentiation in the threedimensional extracellular matrix
    • Han YP, Yan C, Zhou L, Qin L, Tsukamoto H. A matrix metalloproteinase-9 activation cascade by hepatic stellate cells in trans-differentiation in the threedimensional extracellular matrix. J. Biol. Chem. 282, 12928-12939 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 12928-12939
    • Han, Y.P.1    Yan, C.2    Zhou, L.3    Qin, L.4    Tsukamoto, H.5
  • 114
    • 57549096359 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases 2 and 9 in donor liver, cirrhotic liver, and acute rejection after human liver transplantation
    • Kirimlioglu H, Kirimlioglu V, Yilmaz S. Expression of matrix metalloproteinases 2 and 9 in donor liver, cirrhotic liver, and acute rejection after human liver transplantation. Transplant Proc. 40, 3574-3577 (2008).
    • (2008) Transplant Proc , vol.40 , pp. 3574-3577
    • Kirimlioglu, H.1    Kirimlioglu, V.2    Yilmaz, S.3
  • 115
    • 56649123397 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase-2 and -9 and of tissue inhibitor of matrix metalloproteinase-1 in liver regeneration from oval cells in rat
    • Pham Van T, Couchie D, Martin-Garcia N, Laperche Y, Zafrani ES, Mavier P. Expression of matrix metalloproteinase-2 and -9 and of tissue inhibitor of matrix metalloproteinase-1 in liver regeneration from oval cells in rat. Matrix Biol. 27, 674-681 (2008).
    • (2008) Matrix Biol , vol.27 , pp. 674-681
    • Van, P.T.1    Couchie, D.2    Martin-Garcia, N.3    Laperche, Y.4    Zafrani, E.S.5    Mavier, P.6
  • 116
    • 16644402719 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase-2 and -14 persists during early resolution of experimental liver fibrosis and might contribute to fibrolysis
    • Zhou X, Hovell CJ, Pawley S et al. Expression of matrix metalloproteinase-2 and -14 persists during early resolution of experimental liver fibrosis and might contribute to fibrolysis. Liver Int. 24, 492-501 (2004).
    • (2004) Liver Int , vol.24 , pp. 492-501
    • Zhou, X.1    Hovell, C.J.2    Pawley, S.3
  • 117
    • 33748920475 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 is an important factor in hepatic regeneration after partial hepatectomy in mice
    • Olle EW, Ren X, McClintock SD et al. Matrix metalloproteinase-9 is an important factor in hepatic regeneration after partial hepatectomy in mice. Hepatology 44, 540-549 (2006).
    • (2006) Hepatology , vol.44 , pp. 540-549
    • Olle, E.W.1    Ren, X.2    McClintock, S.D.3
  • 118
    • 40149092333 scopus 로고    scopus 로고
    • A critical role for matrix metalloproteinases in liver regeneration
    • Alwayn IP, Verbesey JE, Kim S et al. A critical role for matrix metalloproteinases in liver regeneration. J. Surg. Res. 145, 192-198 (2008).
    • (2008) J. Surg. Res. , vol.145 , pp. 192-198
    • Alwayn, I.P.1    Verbesey, J.E.2    Kim, S.3
  • 119
    • 0032835380 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 activation in human hepatic fibrosis regulation by cell-matrix interactions
    • Preaux AM, Mallat A, Nhieu JT, D'Ortho MP, Hembry RM, Mavier P. Matrix metalloproteinase-2 activation in human hepatic fibrosis regulation by cell-matrix interactions. Hepatology 30, 944-950 (1999).
    • (1999) Hepatology , vol.30 , pp. 944-950
    • Preaux, A.M.1    Mallat, A.2    Nhieu, J.T.3    D'Ortho, M.P.4    Hembry, R.M.5    Mavier, P.6
  • 120
    • 33645798836 scopus 로고    scopus 로고
    • Inhibition of hepatic fibrogenesis by matrix metalloproteinase-9 mutants in mice
    • Roderfeld M, Weiskirchen R, Wagner S et al. Inhibition of hepatic fibrogenesis by matrix metalloproteinase-9 mutants in mice. FASEB J. 20, 444-454 (2006).
    • (2006) FASEB J. , vol.20 , pp. 444-454
    • Roderfeld, M.1    Weiskirchen, R.2    Wagner, S.3
  • 121
    • 34047187004 scopus 로고    scopus 로고
    • Modified synthetic siRNA targeting tissue inhibitor of metalloproteinase-2 inhibits hepatic fibrogenesis in rats
    • Hu YB, Li DG, Lu HM. Modified synthetic siRNA targeting tissue inhibitor of metalloproteinase-2 inhibits hepatic fibrogenesis in rats. J. Gene Med. 9, 217-229 (2007).
    • (2007) J. Gene Med. , vol.9 , pp. 217-229
    • Hu, Y.B.1    Li, D.G.2    Lu, H.M.3
  • 122
    • 16244389638 scopus 로고    scopus 로고
    • Metalloproteinase inhibitor TIMP-1 affects hepatocyte cell cycle via HGF activation in murine liver regeneration
    • Mohammed FF, Pennington CJ, Kassiri Z et al. Metalloproteinase inhibitor TIMP-1 affects hepatocyte cell cycle via HGF activation in murine liver regeneration. Hepatology 41, 857-867 (2005).
    • (2005) Hepatology , vol.41 , pp. 857-867
    • Mohammed, F.F.1    Pennington, C.J.2    Kassiri, Z.3
  • 123
    • 4444229437 scopus 로고    scopus 로고
    • Abnormal TNF activity in Timp3-/- mice leads to chronic hepatic inflammation and failure of liver regeneration
    • Mohammed FF, Smookler DS, Taylor SE et al. Abnormal TNF activity in Timp3-/- mice leads to chronic hepatic inflammation and failure of liver regeneration. Nat. Genet. 36, 969-977 (2004).
    • (2004) Nat. Genet. , vol.36 , pp. 969-977
    • Mohammed, F.F.1    Smookler, D.S.2    Taylor, S.E.3
  • 124
    • 59349092010 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinases improves left ventricular function in mice lacking osteopontin after myocardial infarction
    • Krishnamurthy P, Peterson JT, Subramanian V, Singh M, Singh K. Inhibition of matrix metalloproteinases improves left ventricular function in mice lacking osteopontin after myocardial infarction. Mol. Cell Biochem. 322, 53-62 (2009).
    • (2009) Mol. Cell Biochem. , vol.322 , pp. 53-62
    • Krishnamurthy, P.1    Peterson, J.T.2    Subramanian, V.3    Singh, M.4    Singh, K.5
  • 125
    • 32444441006 scopus 로고    scopus 로고
    • Effect of matrix metalloproteinase inhibition by doxycycline on myocardial healing and remodeling after myocardial infarction
    • Tessone A, Feinberg MS, Barbash IM et al. Effect of matrix metalloproteinase inhibition by doxycycline on myocardial healing and remodeling after myocardial infarction. Cardiovasc. Drugs Ther. 19, 383-390 (2005).
    • (2005) Cardiovasc. Drugs Ther. , vol.19 , pp. 383-390
    • Tessone, A.1    Feinberg, M.S.2    Barbash, I.M.3
  • 126
    • 0036947187 scopus 로고    scopus 로고
    • Integration of concepts: Cardiac extracellular matrix remodeling after myocardial infarction
    • Cleutjens JP, Creemers EE. Integration of concepts: cardiac extracellular matrix remodeling after myocardial infarction. J. Card. Fail. 8, S344-S338 (2002).
    • (2002) J. Card. Fail. , vol.8
    • Cleutjens, J.P.1    Creemers, E.E.2
  • 127
  • 129
    • 3042719731 scopus 로고    scopus 로고
    • Molecular and cellular events at the site of myocardial infarction: From the perspective of rebuilding myocardial tissue
    • Lu L, Zhang JQ, Ramires FJ, Sun Y. Molecular and cellular events at the site of myocardial infarction: from the perspective of rebuilding myocardial tissue. Biochem. Biophys. Res. Commun. 320, 907-913 (2004).
    • (2004) Biochem. Biophys. Res. Commun. , vol.320 , pp. 907-913
    • Lu, L.1    Zhang, J.Q.2    Ramires, F.J.3    Sun, Y.4
  • 130
  • 131
    • 28844434938 scopus 로고    scopus 로고
    • The enzymatic degradation of scaffolds and their replacement by vascularized extracellular matrix in the murine myocardium
    • van Amerongen MJ, Harmsen MC, Petersen AH, Kors G, van Luyn MJ. The enzymatic degradation of scaffolds and their replacement by vascularized extracellular matrix in the murine myocardium. Biomaterials 27, 2247-2257 (2006).
    • (2006) Biomaterials , vol.27 , pp. 2247-2257
    • Van Amerongen, M.J.1    Harmsen, M.C.2    Petersen, A.H.3    Kors, G.4    Van Luyn, M.J.5
  • 132
    • 55149121805 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibition attenuates atrial remodeling and vulnerability to atrial fibrillation in a canine model of heart failure
    • Moe GW, Laurent G, Doumanovskaia L, Konig A, Hu X, Dorian P. Matrix metalloproteinase inhibition attenuates atrial remodeling and vulnerability to atrial fibrillation in a canine model of heart failure. J. Card. Fail. 14, 768-776 (2008).
    • (2008) J. Card. Fail. , vol.14 , pp. 768-776
    • Moe, G.W.1    Laurent, G.2    Doumanovskaia, L.3    Konig, A.4    Hu, X.5    Dorian, P.6
  • 133
    • 58149148261 scopus 로고    scopus 로고
    • Captopril attenuates matrix metalloproteinase-2 and -9 in monocrotaline-induced right ventricular hypertrophy in rats
    • Okada M, Kikuzuki R, Harada T, Hori Y, Yamawaki H, Hara Y. Captopril attenuates matrix metalloproteinase-2 and -9 in monocrotaline-induced right ventricular hypertrophy in rats. J. Pharmacol. Sci. 108, 487-494 (2008).
    • (2008) J. Pharmacol. Sci. , vol.108 , pp. 487-494
    • Okada, M.1    Kikuzuki, R.2    Harada, T.3    Hori, Y.4    Yamawaki, H.5    Hara, Y.6
  • 134
    • 59849089688 scopus 로고    scopus 로고
    • IL-10 inhibits inflammation and attenuates left ventricular remodeling after myocardial infarction via activation of STAT3 and suppression of HuR
    • Krishnamurthy P, Rajasingh J, Lambers E, Qin G, Losordo DW, Kishore R. IL-10 inhibits inflammation and attenuates left ventricular remodeling after myocardial infarction via activation of STAT3 and suppression of HuR. Circ. Res. 104, E9-E18 (2009).
    • (2009) Circ. Res. , vol.104
    • Krishnamurthy, P.1    Rajasingh, J.2    Lambers, E.3    Qin, G.4    Losordo, D.W.5    Kishore, R.6
  • 135
    • 60649100035 scopus 로고    scopus 로고
    • Matrix metalloproteinase suppression induced by clarithromycin in murine cardiac allografts
    • Ogawa M, Suzuki J, Takayama K, Isobe M. Matrix metalloproteinase suppression induced by clarithromycin in murine cardiac allografts. Transplant Proc. 41, 395-397 (2009).
    • (2009) Transplant Proc , vol.41 , pp. 395-397
    • Ogawa, M.1    Suzuki, J.2    Takayama, K.3    Isobe, M.4
  • 136
    • 0033955876 scopus 로고    scopus 로고
    • Effects of gene deletion of the tissue inhibitor of the matrix metalloproteinase-type 1 (TIMP-1) on left ventricular geometry and function in mice
    • Roten L, Nemoto S, Simsic J et al. Effects of gene deletion of the tissue inhibitor of the matrix metalloproteinase-type 1 (TIMP-1) on left ventricular geometry and function in mice. J. Mol. Cell Cardiol. 32, 109-120 (2000).
    • (2000) J. Mol. Cell Cardiol. , vol.32 , pp. 109-120
    • Roten, L.1    Nemoto, S.2    Simsic, J.3
  • 137
    • 0037371608 scopus 로고    scopus 로고
    • Mechanisms of renal cell repair and regeneration after acute renal failure
    • Nony PA, Schnellmann RG. Mechanisms of renal cell repair and regeneration after acute renal failure. J. Pharmacol. Exp. Ther. 304, 905-912 (2003).
    • (2003) J. Pharmacol. Exp. Ther. , vol.304 , pp. 905-912
    • Nony, P.A.1    Schnellmann, R.G.2
  • 138
    • 63449086757 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Their potential role in the pathogenesis of diabetic nephropathy
    • Thrailkill KM, Clay Bunn R, Fowlkes JL. Matrix metalloproteinases: their potential role in the pathogenesis of diabetic nephropathy. Endocrine 35, 1-10 (2009).
    • (2009) Endocrine , vol.35 , pp. 1-10
    • Thrailkill, K.M.1    Clay Bunn, R.2    Fowlkes, J.L.3
  • 139
    • 60749109564 scopus 로고    scopus 로고
    • Characterization of the transcriptional regulation of the human MT1-MMP gene and association of risk reduction for focal-segmental glomerulosclerosis with two functional promoter SNPs
    • Munkert A, Helmchen U, Kemper MJ, Bubenheim M, Stahl RA, Harendza S. Characterization of the transcriptional regulation of the human MT1-MMP gene and association of risk reduction for focal-segmental glomerulosclerosis with two functional promoter SNPs. Nephrol. Dial. Transplant 24, 735-742 (2009).
    • (2009) Nephrol. Dial. Transplant , vol.24 , pp. 735-742
    • Munkert, A.1    Helmchen, U.2    Kemper, M.J.3    Bubenheim, M.4    Stahl, R.A.5    Harendza, S.6
  • 140
    • 60649113094 scopus 로고    scopus 로고
    • Could mycophenolate mofetil combined with benazapril delay tubulointerstitial fibrosis in 5/6 nephrectomized rats?
    • Liu WH, Tang NN, Zhang QD. Could mycophenolate mofetil combined with benazapril delay tubulointerstitial fibrosis in 5/6 nephrectomized rats? Chin. Med. J. (Engl.) 122, 199-204 (2009).
    • (2009) Chin. Med. J. (Engl.) , vol.122 , pp. 199-204
    • Liu, W.H.1    Tang, N.N.2    Zhang, Q.D.3
  • 141
    • 0037385862 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 and tissue inhibitor of metalloproteinases-1 in acute pyelonephritis and renal scarring
    • Chromek M, Tullus K, O Hertting et al. Matrix metalloproteinase-9 and tissue inhibitor of metalloproteinases-1 in acute pyelonephritis and renal scarring. Pediatr. Res. 53, 698-705 (2003).
    • (2003) Pediatr. Res. , vol.53 , pp. 698-705
    • Chromek, M.1    Tullus, K.2    Hertting, O.3
  • 142
    • 65449170025 scopus 로고    scopus 로고
    • Rosiglitazone protects diabetic rats against kidney injury through the suppression of renal matrix metalloproteinase-9 expression
    • Yao XM, Ye SD, Chen Y et al. Rosiglitazone protects diabetic rats against kidney injury through the suppression of renal matrix metalloproteinase-9 expression. Diabetes Obes. Metab. 11, 519-522 (2009).
    • (2009) Diabetes Obes. Metab. , vol.11 , pp. 519-522
    • Yao, X.M.1    Ye, S.D.2    Chen, Y.3
  • 143
    • 63349099519 scopus 로고    scopus 로고
    • Antioxidant treatment reduces matrix metalloproteinase-2-induced vascular changes in renovascular hypertension
    • Castro MM, Rizzi E, Rodrigues GJ et al. Antioxidant treatment reduces matrix metalloproteinase-2-induced vascular changes in renovascular hypertension. Free Radic. Biol. Med. 46, 1298-1307 (2009).
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 1298-1307
    • Castro, M.M.1    Rizzi, E.2    Rodrigues, G.J.3
  • 144
    • 44449103298 scopus 로고    scopus 로고
    • Matrix metalloproteinase-1 promotes prostate tumor growth and metastasis
    • Pulukuri SM, Rao JS. Matrix metalloproteinase-1 promotes prostate tumor growth and metastasis. Int. J. Oncol. 32, 757-765 (2008).
    • (2008) Int. J. Oncol. , vol.32 , pp. 757-765
    • Pulukuri, S.M.1    Rao, J.S.2
  • 145
    • 33644545381 scopus 로고    scopus 로고
    • Tumour microenvironment - Opinion: Validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy
    • Overall CM, Kleifeld O. Tumour microenvironment - opinion: validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy. Nat. Rev. Cancer 6, 227-239 (2006).
    • (2006) Nat. Rev. Cancer , vol.6 , pp. 227-239
    • Overall, C.M.1    Kleifeld, O.2
  • 146
    • 33744938426 scopus 로고    scopus 로고
    • Matrix metalloproteases in aberrant fibrotic tissue remodeling
    • Pardo A, Selman M. Matrix metalloproteases in aberrant fibrotic tissue remodeling. Proc. Am. Thorac. Soc. 3, 383-388 (2006).
    • (2006) Proc. Am. Thorac. Soc. , vol.3 , pp. 383-388
    • Pardo, A.1    Selman, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.