메뉴 건너뛰기




Volumn 14, Issue 8_suppl, 2007, Pages 28-34

Vascular Remodeling and Extracellular Matrix Breakdown in the Uterine Spiral Arteries during Pregnancy

Author keywords

apoptosis; Artery; decidua; elastin; extracellular matrix; invasion; myometrium; proteolysis; trophoblast; vascular smooth muscle.

Indexed keywords

COLLAGEN; ELASTASE; ELASTIN; GROWTH FACTOR; PANCREATIC ELASTASE; PEPTIDE FRAGMENT; SCLEROPROTEIN; SIGNAL PEPTIDE;

EID: 38749118695     PISSN: 19337191     EISSN: 19337205     Source Type: Journal    
DOI: 10.1177/1933719107309588     Document Type: Article
Times cited : (41)

References (76)
  • 1
    • 0031955679 scopus 로고    scopus 로고
    • Decidual spiral artery remodelling begins before cellular interaction with cytotrophoblasts
    • Craven CM, Morgan T, Ward K. Decidual spiral artery remodelling begins before cellular interaction with cytotrophoblasts. Placenta. 1998;19(4):241-252.
    • (1998) Placenta. , vol.19 , Issue.4 , pp. 241-252
    • Craven, C.M.1    Morgan, T.2    Ward, K.3
  • 2
    • 0025913123 scopus 로고
    • Implantation, trophoblast differentiation and haemochorial placentation: Mechanistic evidence in vivo and in vitro
    • Aplin JD. Implantation, trophoblast differentiation and haemochorial placentation: mechanistic evidence in vivo and in vitro. J Cell Sci. 1991;99(pt 4):681-692.
    • (1991) J Cell Sci. , vol.99 , pp. 681-692
    • Aplin, J.D.1
  • 3
    • 33746500163 scopus 로고    scopus 로고
    • The uterine spiral arteries in human pregnancy: Facts and controversies
    • Pijnenborg R, Vercruysse L, Hanssens M. The uterine spiral arteries in human pregnancy: facts and controversies. Placenta. 2006;27(9-10):939-958.
    • (2006) Placenta. , vol.27 , Issue.9-10 , pp. 939-958
    • Pijnenborg, R.1    Vercruysse, L.2    Hanssens, M.3
  • 4
    • 33644669545 scopus 로고    scopus 로고
    • Late sporadic miscarriage is associated with abnormalities in spiral artery transformation and trophoblast invasion
    • Ball E, Bulmer JN, Ayis S, et al. Late sporadic miscarriage is associated with abnormalities in spiral artery transformation and trophoblast invasion. J Pathol. 2006;208(4):535-542.
    • (2006) J Pathol. , vol.208 , Issue.4 , pp. 535-542
    • Ball, E.1    Bulmer, J.N.2    Ayis, S.3
  • 5
    • 0242677605 scopus 로고    scopus 로고
    • Failure of physiologic transformation of the spiral arteries in patients with preterm labor and intact membranes
    • Kim YM, Bujold E, Chaiworapongsa T, et al. Failure of physiologic transformation of the spiral arteries in patients with preterm labor and intact membranes. Am J Obstet Gynecol. 2003;189(4):1063-1069.
    • (2003) Am J Obstet Gynecol. , vol.189 , Issue.4 , pp. 1063-1069
    • Kim, Y.M.1    Bujold, E.2    Chaiworapongsa, T.3
  • 6
    • 0035015517 scopus 로고    scopus 로고
    • Pericytes: Cell biology and pathology
    • Allt G, Lawrenson JG. Pericytes: cell biology and pathology. Cells Tissues Organs. 2001;169(1):1-11.
    • (2001) Cells Tissues Organs. , vol.169 , Issue.1 , pp. 1-11
    • Allt, G.1    Lawrenson, J.G.2
  • 7
    • 13244255527 scopus 로고    scopus 로고
    • Colocalization of the collagen-binding proteoglycans decorin, biglycan, fibromodulin and lumican with different cells in human gingiva
    • Alimohamad H, Habijanac T, Larjava H, et al. Colocalization of the collagen-binding proteoglycans decorin, biglycan, fibromodulin and lumican with different cells in human gingiva. J Periodontal Res. 2005;40(1):73-86.
    • (2005) J Periodontal Res. , vol.40 , Issue.1 , pp. 73-86
    • Alimohamad, H.1    Habijanac, T.2    Larjava, H.3
  • 8
    • 0025344461 scopus 로고
    • Modulation of extracellular matrix biosynthesis by bovine retinal pericytes in vitro: Effects of the substratum and cell density
    • Canfield AE, Allen TD, Grant ME, et al. Modulation of extracellular matrix biosynthesis by bovine retinal pericytes in vitro: effects of the substratum and cell density. J Cell Sci. 1990;96(pt 1):159-169.
    • (1990) J Cell Sci. , vol.96 , pp. 159-169
    • Canfield, A.E.1    Allen, T.D.2    Grant, M.E.3
  • 10
    • 0347418197 scopus 로고    scopus 로고
    • Collagens, modifying enzymes and their mutations in humans, flies and worms
    • Myllyharju J, Kivirikko KI. Collagens, modifying enzymes and their mutations in humans, flies and worms. Trends Genet. 2004;20(1):33-43.
    • (2004) Trends Genet. , vol.20 , Issue.1 , pp. 33-43
    • Myllyharju, J.1    Kivirikko, K.I.2
  • 11
    • 0021996988 scopus 로고
    • Distribution of type I, III, IV and v collagen in normal and atherosclerotic human arterial wall: Immunomorphological characteristics
    • Shekhonin BV, Domogatsky SP, Muzykantov VR, et al. Distribution of type I, III, IV and V collagen in normal and atherosclerotic human arterial wall: immunomorphological characteristics. Coll Relat Res. 1985;5(4):355-368.
    • (1985) Coll Relat Res. , vol.5 , Issue.4 , pp. 355-368
    • Shekhonin, B.V.1    Domogatsky, S.P.2    Muzykantov, V.R.3
  • 12
    • 0042347601 scopus 로고    scopus 로고
    • Extracellular matrix remodeling and matrix metalloproteinases in the vascular wall during aging and in pathological conditions
    • Jacob MP. Extracellular matrix remodeling and matrix metalloproteinases in the vascular wall during aging and in pathological conditions. Biomed Pharmacother. 2003;57(5-6): 195-202.
    • (2003) Biomed Pharmacother. , vol.57 , Issue.5-6 , pp. 195-202
    • Jacob, M.P.1
  • 13
    • 0347356370 scopus 로고    scopus 로고
    • EMILIN-1 deficiency induces elastogenesis and vascular cell defects
    • Zanetti M, Braghetta P, Sabatelli P, et al. EMILIN-1 deficiency induces elastogenesis and vascular cell defects. Mol Cell Biol. 2004;24(2):638-650.
    • (2004) Mol Cell Biol. , vol.24 , Issue.2 , pp. 638-650
    • Zanetti, M.1    Braghetta, P.2    Sabatelli, P.3
  • 14
    • 33751541732 scopus 로고    scopus 로고
    • EMILIN1 represents a major stromal element determining human trophoblast invasion of the uterine wall
    • Spessotto P, Bulla R, Danussi C, et al. EMILIN1 represents a major stromal element determining human trophoblast invasion of the uterine wall. J Cell Sci. 2006;119(pt 21): 4574-4584.
    • (2006) J Cell Sci. , vol.119 , pp. 4574-4584
    • Spessotto, P.1    Bulla, R.2    Danussi, C.3
  • 15
    • 0037370649 scopus 로고    scopus 로고
    • Angiogenesis: Vascular remodeling of the extracellular matrix involves metalloproteinases
    • Heissig B, Hattori K, Friedrich M, et al. Angiogenesis: vascular remodeling of the extracellular matrix involves metalloproteinases. Curr Opin Hematol. 2003;10(2):136-141.
    • (2003) Curr Opin Hematol , vol.10 , Issue.2 , pp. 136-141
    • Heissig, B.1    Hattori, K.2    Friedrich, M.3
  • 16
    • 0035721955 scopus 로고    scopus 로고
    • Role of the matrix metalloproteinase and plasminogen activator-plasmin systems in angiogenesis
    • Pepper MS. Role of the matrix metalloproteinase and plasminogen activator-plasmin systems in angiogenesis. Arterioscler Thromb Vasc Biol. 2001;21(7):1104-1117.
    • (2001) Arterioscler Thromb Vasc Biol. , vol.21 , Issue.7 , pp. 1104-1117
    • Pepper, M.S.1
  • 17
    • 4444304939 scopus 로고    scopus 로고
    • Regulation of matrix biology by matrix metalloproteinases
    • Mott JD, Werb Z. Regulation of matrix biology by matrix metalloproteinases. Curr Opin Cell Biol. 2004;16(5):558-564.
    • (2004) Curr Opin Cell Biol. , vol.16 , Issue.5 , pp. 558-564
    • Mott, J.D.1    Werb, Z.2
  • 18
    • 0036829020 scopus 로고    scopus 로고
    • Molecular basis of endothelial cell morphogenesis in three-dimensional extracellular matrices
    • Davis GE, Bayless KJ, Mavila A. Molecular basis of endothelial cell morphogenesis in three-dimensional extracellular matrices. Anat Rec. 2002;268(3):252-275.
    • (2002) Anat Rec. , vol.268 , Issue.3 , pp. 252-275
    • Davis, G.E.1    Bayless, K.J.2    Mavila, A.3
  • 19
    • 0037568364 scopus 로고    scopus 로고
    • Matrilysin (matrix metalloproteinase-7) mediates E-cadherin ectodomain shedding in injured lung epithelium
    • McGuire JK, Li Q, Parks WC. Matrilysin (matrix metalloproteinase-7) mediates E-cadherin ectodomain shedding in injured lung epithelium. Am J Pathol. 2003;162(6):1831-1843.
    • (2003) Am J Pathol. , vol.162 , Issue.6 , pp. 1831-1843
    • McGuire, J.K.1    Li, Q.2    Parks, W.C.3
  • 20
    • 22344449179 scopus 로고    scopus 로고
    • Ischemiainduced cleavage of cadherins in NRK cells: Evidence for a role of metalloproteinases
    • Covington MD, Bayless KJ, Burghardt RC, et al. Ischemiainduced cleavage of cadherins in NRK cells: evidence for a role of metalloproteinases. Am J Physiol Renal Physiol. 2005; 289(2):F280-F288.
    • (2005) Am J Physiol Renal Physiol. , vol.289 , Issue.2 , pp. F280-F288
    • Covington, M.D.1    Bayless, K.J.2    Burghardt, R.C.3
  • 21
    • 0036405405 scopus 로고    scopus 로고
    • ADAM15 is an adherens junction molecule whose surface expression can be driven by VE-cadherin
    • Ham C, Levkau B, Raines EW, et al. ADAM15 is an adherens junction molecule whose surface expression can be driven by VE-cadherin. Exp Cell Res. 2002;279(2):239-247.
    • (2002) Exp Cell Res. , vol.279 , Issue.2 , pp. 239-247
    • Ham, C.1    Levkau, B.2    Raines, E.W.3
  • 22
    • 0041631044 scopus 로고    scopus 로고
    • Potential role for ADAM15 in pathological neovascularization in mice
    • Horiuchi K, Weskamp G, Lum L, et al. Potential role for ADAM15 in pathological neovascularization in mice. Mol Cell Biol. 2003;23(16):5614-5624.
    • (2003) Mol Cell Biol. , vol.23 , Issue.16 , pp. 5614-5624
    • Horiuchi, K.1    Weskamp, G.2    Lum, L.3
  • 23
    • 3042590902 scopus 로고    scopus 로고
    • Endothelial cell-to-cell junctions: Molecular organization and role in vascular homeostasis
    • Bazzoni G, Dejana E. Endothelial cell-to-cell junctions: molecular organization and role in vascular homeostasis. Physiol Rev. 2004;84(3):869-901.
    • (2004) Physiol Rev. , vol.84 , Issue.3 , pp. 869-901
    • Bazzoni, G.1    Dejana, E.2
  • 24
    • 1842632667 scopus 로고    scopus 로고
    • Endothelial cell-cell junctions: Happy together
    • Dejana E. Endothelial cell-cell junctions: happy together. Nat Rev Mol Cell Biol. 2004;5(4):261-270.
    • (2004) Nat Rev Mol Cell Biol. , vol.5 , Issue.4 , pp. 261-270
    • Dejana, E.1
  • 25
    • 0029826806 scopus 로고    scopus 로고
    • Membrane-type matrix metalloproteinase-1 expression at the site of human placentation
    • Nawrocki B, Polette M, Marchand V, et al. Membrane-type matrix metalloproteinase-1 expression at the site of human placentation. Placenta. 1996;17(8):565-572.
    • (1996) Placenta. , vol.17 , Issue.8 , pp. 565-572
    • Nawrocki, B.1    Polette, M.2    Marchand, V.3
  • 26
    • 0344631076 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their inhibitors in gestational trophoblastic diseases and normal placenta
    • Vegh GL, Selcuk Tuncer Z, Fulop V, et al. Matrix metalloproteinases and their inhibitors in gestational trophoblastic diseases and normal placenta. Gynecol Oncol. 1999;75(2):248-253.
    • (1999) Gynecol Oncol. , vol.75 , Issue.2 , pp. 248-253
    • Vegh, G.L.1    Selcuk Tuncer, Z.2    Fulop, V.3
  • 27
    • 33845605792 scopus 로고    scopus 로고
    • Interferon-gamma inhibits extravillous trophoblast cell invasion by a mechanism that involves both changes in apoptosis and protease levels
    • Lash GE, Otun HA, Innes BA, et al. Interferon-gamma inhibits extravillous trophoblast cell invasion by a mechanism that involves both changes in apoptosis and protease levels. FASEB J. 2006;20(14):2512-2518.
    • (2006) FASEB J. , vol.20 , Issue.14 , pp. 2512-2518
    • Lash, G.E.1    Otun, H.A.2    Innes, B.A.3
  • 28
    • 0028180451 scopus 로고
    • Interleukin-1 beta regulates human cytotrophoblast metalloproteinase activity and invasion in vitro
    • Librach CL, Feigenbaum SL, Bass KE, et al. Interleukin-1 beta regulates human cytotrophoblast metalloproteinase activity and invasion in vitro. J Biol Chem. 1994;269(25):17125-17131.
    • (1994) J Biol Chem. , vol.269 , Issue.25 , pp. 17125-17131
    • Librach, C.L.1    Feigenbaum, S.L.2    Bass, K.E.3
  • 29
    • 0025891874 scopus 로고
    • 92-kD type IV collagenase mediates invasion of human cytotrophoblasts
    • Librach CL, Werb Z, Fitzgerald ML, et al. 92-kD type IV collagenase mediates invasion of human cytotrophoblasts. J Cell Biol. 1991;113(2):437-449.
    • (1991) J Cell Biol. , vol.113 , Issue.2 , pp. 437-449
    • Librach, C.L.1    Werb, Z.2    Fitzgerald, M.L.3
  • 30
    • 0025176677 scopus 로고
    • Endothelium-dependent mechanical properties of the carotid artery in WKY and SHR: Role of angiotensin converting enzyme inhibition
    • Levy BI, Benessiano J, Poitevin P, et al. Endothelium-dependent mechanical properties of the carotid artery in WKY and SHR: role of angiotensin converting enzyme inhibition. Circ Res. 1990;66(2):321-328.
    • (1990) Circ Res. , vol.66 , Issue.2 , pp. 321-328
    • Levy, B.I.1    Benessiano, J.2    Poitevin, P.3
  • 31
    • 0035678978 scopus 로고    scopus 로고
    • Pulse pressure, endothelium function, and arterial stiffness in spontaneously hypertensive rats
    • Safar M, Chamiot-Clerc P, Dagher G, et al. Pulse pressure, endothelium function, and arterial stiffness in spontaneously hypertensive rats. Hypertension. 2001;38(6):1416-1421.
    • (2001) Hypertension. , vol.38 , Issue.6 , pp. 1416-1421
    • Safar, M.1    Chamiot-Clerc, P.2    Dagher, G.3
  • 32
    • 0036989784 scopus 로고    scopus 로고
    • Regulation of differentiated properties of vascular smooth muscle cells in atherosclerosis: Role of extracellular matrix
    • Yamamoto K, Yamamoto M, Yamamoto N, et al. Regulation of differentiated properties of vascular smooth muscle cells in atherosclerosis: role of extracellular matrix. Connect Tissue. 2002;34:317-325.
    • (2002) Connect Tissue. , vol.34 , pp. 317-325
    • Yamamoto, K.1    Yamamoto, M.2    Yamamoto, N.3
  • 33
    • 34147130611 scopus 로고    scopus 로고
    • Invasive trophoblasts stimulate vascular smooth muscle cell apoptosis by a fas liganddependent mechanism
    • Harris LK, Keogh RJ, Wareing M, et al. Invasive trophoblasts stimulate vascular smooth muscle cell apoptosis by a fas liganddependent mechanism. Am J Pathol. 2006;169(5):1863-1874.
    • (2006) Am J Pathol. , vol.169 , Issue.5 , pp. 1863-1874
    • Harris, L.K.1    Keogh, R.J.2    Wareing, M.3
  • 34
    • 34147105930 scopus 로고    scopus 로고
    • Fetal-derived trophoblast utilize the apoptotic cytokine TNF-related apoptosisinducing ligand (TRAIL) to induce smooth muscle cell death
    • Keogh RJ, Harris LK, Freeman A, et al. Fetal-derived trophoblast utilize the apoptotic cytokine TNF-related apoptosisinducing ligand (TRAIL) to induce smooth muscle cell death. Circ Res. 2007;100(6):834-841.
    • (2007) Circ Res. , vol.100 , Issue.6 , pp. 834-841
    • Keogh, R.J.1    Harris, L.K.2    Freeman, A.3
  • 35
    • 15744372765 scopus 로고    scopus 로고
    • Clinical measurement of arterial stiffness obtained from noninvasive pressure waveforms
    • Nichols WW. Clinical measurement of arterial stiffness obtained from noninvasive pressure waveforms. Am J Hypertens. 2005;18(1 pt 2):3S-10S.
    • (2005) Am J Hypertens. , vol.18 , Issue.1 , pp. 3S-10S
    • Nichols, W.W.1
  • 36
    • 33644643244 scopus 로고    scopus 로고
    • Elastin fragments drive disease progression in a murine model of emphysema
    • Houghton AM, Quintero PA, Perkins DL, et al. Elastin fragments drive disease progression in a murine model of emphysema. J Clin Invest. 2006;116(3):753-759.
    • (2006) J Clin Invest. , vol.116 , Issue.3 , pp. 753-759
    • Houghton, A.M.1    Quintero, P.A.2    Perkins, D.L.3
  • 37
    • 0028027046 scopus 로고
    • Nature and the multiple functions of the 67-kD elastin-/laminin binding protein
    • Hinek A. Nature and the multiple functions of the 67-kD elastin-/laminin binding protein. Cell Adhes Commun. 1994; 2(3):185-193.
    • (1994) Cell Adhes Commun. , vol.2 , Issue.3 , pp. 185-193
    • Hinek, A.1
  • 38
    • 0037160109 scopus 로고    scopus 로고
    • Signaling pathways transduced through the elastin receptor facilitate proliferation of arterial smooth muscle cells
    • Mochizuki S, Brassart B, Hinek A. Signaling pathways transduced through the elastin receptor facilitate proliferation of arterial smooth muscle cells. J Biol Chem. 2002;277(47): 44854-44863.
    • (2002) J Biol Chem. , vol.277 , Issue.47 , pp. 44854-44863
    • Mochizuki, S.1    Brassart, B.2    Hinek, A.3
  • 39
    • 0025037821 scopus 로고
    • Altered phosphatidylinositol breakdown after K-elastin stimulation in PMNLs of elderly
    • Varga Z, Jacob MP, Csongor J, et al. Altered phosphatidylinositol breakdown after K-elastin stimulation in PMNLs of elderly. Mech Ageing Dev. 1990;52(1):61-70.
    • (1990) Mech Ageing Dev. , vol.52 , Issue.1 , pp. 61-70
    • Varga, Z.1    Jacob, M.P.2    Csongor, J.3
  • 40
    • 0031767365 scopus 로고    scopus 로고
    • Role of the elastin-laminin receptor in the cardiovascular system
    • Faury G. Role of the elastin-laminin receptor in the cardiovascular system. Pathol Biol (Paris). 1998;46(7):517-526.
    • (1998) Pathol Biol (Paris). , vol.46 , Issue.7 , pp. 517-526
    • Faury, G.1
  • 41
    • 0028935701 scopus 로고
    • Effect of elastin peptides on vascular tone
    • Faury G, Ristori MT, Verdetti J, et al. Effect of elastin peptides on vascular tone. J Vasc Res. 1995;32(2):112-119.
    • (1995) J Vasc Res. , vol.32 , Issue.2 , pp. 112-119
    • Faury, G.1    Ristori, M.T.2    Verdetti, J.3
  • 42
    • 0029936393 scopus 로고    scopus 로고
    • Functional interplay between interleukin-1 receptor and elastin binding protein regulates fibronectin production in coronary artery smooth muscle cells
    • Hinek A, Molossi S, Rabinovitch M. Functional interplay between interleukin-1 receptor and elastin binding protein regulates fibronectin production in coronary artery smooth muscle cells. Exp Cell Res. 1996;225(1):122-131.
    • (1996) Exp Cell Res. , vol.225 , Issue.1 , pp. 122-131
    • Hinek, A.1    Molossi, S.2    Rabinovitch, M.3
  • 43
    • 1442274622 scopus 로고    scopus 로고
    • Elastin-derived peptides upregulate matrix metalloproteinase-2-mediated melanoma cell invasion through elastin-binding protein
    • Ntayi C, Labrousse AL, Debret R, et al. Elastin-derived peptides upregulate matrix metalloproteinase-2-mediated melanoma cell invasion through elastin-binding protein. J Invest Dermatol. 2004;122(2):256-265.
    • (2004) J Invest Dermatol. , vol.122 , Issue.2 , pp. 256-265
    • Ntayi, C.1    Labrousse, A.L.2    Debret, R.3
  • 44
    • 0032446984 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase-2 (gelatinase A, MMP-2), membranetype matrix metalloproteinase-1 (MT1-MMP) and tissue inhibitor of metalloproteinases-2 (TIMP-2) expression by elastin-derived peptides in human HT-1080 fibrosarcoma cell line
    • Brassart B, Randoux A, Hornebeck W, et al. Regulation of matrix metalloproteinase-2 (gelatinase A, MMP-2), membranetype matrix metalloproteinase-1 (MT1-MMP) and tissue inhibitor of metalloproteinases-2 (TIMP-2) expression by elastin-derived peptides in human HT-1080 fibrosarcoma cell line. Clin Exp Metastasis. 1998;16(6):489-500.
    • (1998) Clin Exp Metastasis. , vol.16 , Issue.6 , pp. 489-500
    • Brassart, B.1    Randoux, A.2    Hornebeck, W.3
  • 45
    • 0017457406 scopus 로고
    • Elastogenesis and elastinolytic activity in human breast cancer
    • Hornebeck W, Derouette JC, Brechemier D, et al. Elastogenesis and elastinolytic activity in human breast cancer. Biomedicine. 1977;26(1):48-52.
    • (1977) Biomedicine. , vol.26 , Issue.1 , pp. 48-52
    • Hornebeck, W.1    Derouette, J.C.2    Brechemier, D.3
  • 46
    • 0028006969 scopus 로고
    • Thrombolytic therapy of acute myocardial infarction alters collagen metabolism
    • Host NB, Hansen SS, Jensen LT, et al. Thrombolytic therapy of acute myocardial infarction alters collagen metabolism. Cardiology. 1994;85(5):323-333.
    • (1994) Cardiology , vol.85 , Issue.5 , pp. 323-333
    • Host, N.B.1    Hansen, S.S.2    Jensen, L.T.3
  • 47
    • 0025092262 scopus 로고
    • Serum aminoterminal type III procollagen peptide reflects repair after acute myocardial infarction
    • Jensen LT, Horslev-Petersen K, Toft P, et al. Serum aminoterminal type III procollagen peptide reflects repair after acute myocardial infarction. Circulation. 1990;81(1):52-57.
    • (1990) Circulation. , vol.81 , Issue.1 , pp. 52-57
    • Jensen, L.T.1    Horslev-Petersen, K.2    Toft, P.3
  • 48
    • 0025797786 scopus 로고
    • Thrombolytic therapy with streptokinase stimulates collagen breakdown
    • Peuhkurinen KJ, Risteli L, Melkko JT, et al. Thrombolytic therapy with streptokinase stimulates collagen breakdown. Circulation. 1991;83(6):1969-1975.
    • (1991) Circulation. , vol.83 , Issue.6 , pp. 1969-1975
    • Peuhkurinen, K.J.1    Risteli, L.2    Melkko, J.T.3
  • 49
    • 17944382123 scopus 로고    scopus 로고
    • Long-term changes in collagen formation expressed by serum carboxyterminal propeptide of type-I procollagen and relation to left ventricular function after acute myocardial infarction
    • Poulsen SH, Host NB, Egstrup K. Long-term changes in collagen formation expressed by serum carboxyterminal propeptide of type-I procollagen and relation to left ventricular function after acute myocardial infarction. Cardiology. 2001;96(1):45-50.
    • (2001) Cardiology. , vol.96 , Issue.1 , pp. 45-50
    • Poulsen, S.H.1    Host, N.B.2    Egstrup, K.3
  • 50
    • 10344258050 scopus 로고    scopus 로고
    • The contribution of vascular basement membranes and extracellular matrix to the mechanics of tumor angiogenesis
    • Sund M, Xie L, Kalluri R. The contribution of vascular basement membranes and extracellular matrix to the mechanics of tumor angiogenesis. Apmis. 2004;112(7-8):450-462.
    • (2004) Apmis , vol.112 , Issue.7-8 , pp. 450-462
    • Sund, M.1    Xie, L.2    Kalluri, R.3
  • 51
    • 0031671855 scopus 로고    scopus 로고
    • Matrix metalloproteinase degradation of extracellular matrix: Biological consequences
    • Shapiro SD. Matrix metalloproteinase degradation of extracellular matrix: biological consequences. Curr Opin Cell Biol. 1998;10(5):602-608.
    • (1998) Curr Opin Cell Biol. , vol.10 , Issue.5 , pp. 602-608
    • Shapiro, S.D.1
  • 52
    • 0033563237 scopus 로고    scopus 로고
    • Fibrillin degradation by matrix metalloproteinases: Implications for connective tissue remodelling
    • Ashworth JL, Murphy G, Rock MJ, et al. Fibrillin degradation by matrix metalloproteinases: implications for connective tissue remodelling. Biochem J. 1999;340 (pt 1):171-181.
    • (1999) Biochem J. , vol.340 , pp. 171-181
    • Ashworth, J.L.1    Murphy, G.2    Rock, M.J.3
  • 53
    • 0027958825 scopus 로고
    • Catabolism of intact fibrillin microfibrils by neutrophil elastase, chymotrypsin and trypsin
    • Kielty CM, Woolley DE, Whittaker SP, et al. Catabolism of intact fibrillin microfibrils by neutrophil elastase, chymotrypsin and trypsin. FEBS Lett. 1994;351(1):85-89.
    • (1994) FEBS Lett. , vol.351 , Issue.1 , pp. 85-89
    • Kielty, C.M.1    Woolley, D.E.2    Whittaker, S.P.3
  • 54
    • 0032765385 scopus 로고    scopus 로고
    • Eve and beyond, retro and prospective insights
    • Rabinovitch M. EVE and beyond, retro and prospective insights. Am J Physiol. 1999;277(1 pt 1):L5-L12.
    • (1999) Am J Physiol. , vol.277 , Issue.1 , pp. L5-L12
    • Rabinovitch, M.1
  • 55
    • 27744440521 scopus 로고    scopus 로고
    • Caspases from apoptotic myocytes degrade extracellular matrix: A novel remodeling paradigm
    • Cowan KN, Leung WC, Mar C, et al. Caspases from apoptotic myocytes degrade extracellular matrix: A novel remodeling paradigm. FASEB J. 2005;19(13):1848-1850.
    • (2005) FASEB J. , vol.19 , Issue.13 , pp. 1848-1850
    • Cowan, K.N.1    Leung, W.C.2    Mar, C.3
  • 56
    • 0030970119 scopus 로고    scopus 로고
    • Emerging roles for cysteine proteases in human biology
    • Chapman HA, Riese RJ, Shi GP. Emerging roles for cysteine proteases in human biology. Annu Rev Physiol. 1997;59:63-88.
    • (1997) Annu Rev Physiol. , vol.59 , pp. 63-88
    • Chapman, H.A.1    Riese, R.J.2    Shi, G.P.3
  • 57
    • 0019451911 scopus 로고
    • Isolation and partial characterization of an elastase-like protease from rat aorta smooth muscle cells: Possible role in the regulation of elastin biosynthesis
    • Hornebeck W, Brechemier D, Bourdillon MC, et al. Isolation and partial characterization of an elastase-like protease from rat aorta smooth muscle cells: possible role in the regulation of elastin biosynthesis. Connect Tissue Res. 1981;8(3-4):245-249.
    • (1981) Connect Tissue Res. , vol.8 , Issue.3-4 , pp. 245-249
    • Hornebeck, W.1    Brechemier, D.2    Bourdillon, M.C.3
  • 58
    • 0020569945 scopus 로고
    • Hypoxic injury to human alveolar macrophages accelerates release of previously bound neutrophil elastase: Implications for lung connective tissue injury including pulmonary emphysema
    • Campbell EJ, Wald MS. Hypoxic injury to human alveolar macrophages accelerates release of previously bound neutrophil elastase: implications for lung connective tissue injury including pulmonary emphysema. Am Rev Respir Dis. 1983; 127(5):631-635.
    • (1983) Am Rev Respir Dis. , vol.127 , Issue.5 , pp. 631-635
    • Campbell, E.J.1    Wald, M.S.2
  • 59
    • 0019159671 scopus 로고
    • Degradation of connective tissue matrices by macrophages. I. Proteolysis of elastin, glycoproteins, and collagen by proteinases isolated from macrophages
    • Werb Z, Banda MJ, Jones PA. Degradation of connective tissue matrices by macrophages. I. Proteolysis of elastin, glycoproteins, and collagen by proteinases isolated from macrophages. J Exp Med. 1980;152(5):1340-1357.
    • (1980) J Exp Med. , vol.152 , Issue.5 , pp. 1340-1357
    • Werb, Z.1    Banda, M.J.2    Jones, P.A.3
  • 60
    • 0016663144 scopus 로고
    • Separation of human blood platelet elastase and proelastase by affinity chromatography
    • Legrand Y, Pignaud G, Caen JP, et al. Separation of human blood platelet elastase and proelastase by affinity chromatography. Biochem Biophys Res Commun. 1975;63(1):224-231.
    • (1975) Biochem Biophys Res Commun. , vol.63 , Issue.1 , pp. 224-231
    • Legrand, Y.1    Pignaud, G.2    Caen, J.P.3
  • 62
    • 18144414713 scopus 로고    scopus 로고
    • Expression and importance of matrix metalloproteinase 2 and 9 (MMP-2 and-9) in human trophoblast invasion
    • Staun-Ram E, Goldman S, Gabarin D, et al. Expression and importance of matrix metalloproteinase 2 and 9 (MMP-2 and-9) in human trophoblast invasion. Reprod Biol Endocrinol. 2004; 2:59-71.
    • (2004) Reprod Biol Endocrinol. , vol.2 , pp. 59-71
    • Staun-Ram, E.1    Goldman, S.2    Gabarin, D.3
  • 63
    • 26444444756 scopus 로고    scopus 로고
    • Role of cathepsins and cystatins in patients with recurrent miscarriage
    • Nakanishi T, Ozaki Y, Blomgren K, et al. Role of cathepsins and cystatins in patients with recurrent miscarriage. Mol Hum Reprod. 2005;11(5):351-355.
    • (2005) Mol Hum Reprod. , vol.11 , Issue.5 , pp. 351-355
    • Nakanishi, T.1    Ozaki, Y.2    Blomgren, K.3
  • 64
    • 0030068937 scopus 로고    scopus 로고
    • The structural basis for the elastolytic activity of the 92-kDa and 72-kDa gelatinases: Role of the fibronectin type II-like repeats
    • Shipley JM, Doyle GA, Fliszar CJ, et al. The structural basis for the elastolytic activity of the 92-kDa and 72-kDa gelatinases: role of the fibronectin type II-like repeats. J Biol Chem. 1996;271(8):4335-4341.
    • (1996) J Biol Chem. , vol.271 , Issue.8 , pp. 4335-4341
    • Shipley, J.M.1    Doyle, G.A.2    Fliszar, C.J.3
  • 65
    • 0032145836 scopus 로고    scopus 로고
    • Expression of the elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells
    • Sukhova GK, Shi GP, Simon DI, et al. Expression of the elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells. J Clin Invest. 1998;102(3):576-583.
    • (1998) J Clin Invest. , vol.102 , Issue.3 , pp. 576-583
    • Sukhova, G.K.1    Shi, G.P.2    Simon, D.I.3
  • 66
    • 0037058855 scopus 로고    scopus 로고
    • Increased expression of membrane type 3-matrix metalloproteinase in human atherosclerotic plaque: Role of activated macrophages and inflammatory cytokines
    • Uzui H, Harpf A, Liu M, et al. Increased expression of membrane type 3-matrix metalloproteinase in human atherosclerotic plaque: role of activated macrophages and inflammatory cytokines. Circulation. 2002;106(24):3024-3030.
    • (2002) Circulation. , vol.106 , Issue.24 , pp. 3024-3030
    • Uzui, H.1    Harpf, A.2    Liu, M.3
  • 67
    • 0037782348 scopus 로고    scopus 로고
    • Neutrophil elastase in human atherosclerotic plaques: Production by macrophages
    • Dollery CM, Owen CA, Sukhova GK, et al. Neutrophil elastase in human atherosclerotic plaques: production by macrophages. Circulation. 2003;107(22):2829-2836.
    • (2003) Circulation. , vol.107 , Issue.22 , pp. 2829-2836
    • Dollery, C.M.1    Owen, C.A.2    Sukhova, G.K.3
  • 68
    • 0033105848 scopus 로고    scopus 로고
    • The distribution of macrophages in spiral arteries of the placental bed in preeclampsia differs from that in healthy patients
    • Reister F, Frank HG, Heyl W, et al. The distribution of macrophages in spiral arteries of the placental bed in preeclampsia differs from that in healthy patients. Placenta. 1999; 20(2-3):229-233.
    • (1999) Placenta. , vol.20 , Issue.2-3 , pp. 229-233
    • Reister, F.1    Frank, H.G.2    Heyl, W.3
  • 69
    • 0034679718 scopus 로고    scopus 로고
    • Interferon gamma contributes to initiation of uterine vascular modification, decidual integrity, and uterine natural killer cell maturation during normal murine pregnancy
    • Ashkar AA, Di Santo JP, Croy BA. Interferon gamma contributes to initiation of uterine vascular modification, decidual integrity, and uterine natural killer cell maturation during normal murine pregnancy. J Exp Med. 2000;192(2):259-270.
    • (2000) J Exp Med. , vol.192 , Issue.2 , pp. 259-270
    • Ashkar, A.A.1    Di Santo, J.P.2    Croy, B.A.3
  • 70
    • 0142243189 scopus 로고    scopus 로고
    • Alpha-2 macroglobulin controls trophoblast positioning in mouse implantation sites
    • Esadeg S, He H, Pijnenborg R, et al. Alpha-2 macroglobulin controls trophoblast positioning in mouse implantation sites. Placenta. 2003;24(10):912-921.
    • (2003) Placenta. , vol.24 , Issue.10 , pp. 912-921
    • Esadeg, S.1    He, H.2    Pijnenborg, R.3
  • 71
    • 0035830852 scopus 로고    scopus 로고
    • Altered processing of fibronectin in mice lacking heparin: A role for heparin-dependent mast cell chymase in fibronectin degradation
    • Tchougounova E, Forsberg E, Angelborg G, et al. Altered processing of fibronectin in mice lacking heparin: A role for heparin-dependent mast cell chymase in fibronectin degradation. J Biol Chem. 2001;276(6):3772-3777.
    • (2001) J Biol Chem. , vol.276 , Issue.6 , pp. 3772-3777
    • Tchougounova, E.1    Forsberg, E.2    Angelborg, G.3
  • 72
    • 0030897985 scopus 로고    scopus 로고
    • Cleavage of type i procollagen by human mast cell chymase initiates collagen fibril formation and generates a unique carboxylterminal propeptide
    • Kofford MW, Schwartz LB, Schechter NM, et al. Cleavage of type I procollagen by human mast cell chymase initiates collagen fibril formation and generates a unique carboxylterminal propeptide. J Biol Chem. 1997;272(11):7127-7131.
    • (1997) J Biol Chem. , vol.272 , Issue.11 , pp. 7127-7131
    • Kofford, M.W.1    Schwartz, L.B.2    Schechter, N.M.3
  • 73
    • 33644852315 scopus 로고    scopus 로고
    • Mast cells, histamine and development of the placental vascular network in pregnancies complicated by preeclampsia and intrauterine growth retardation [in Polish]
    • Szewczyk G, Szewczyk A, Pyzlak M, et al. Mast cells, histamine and development of the placental vascular network in pregnancies complicated by preeclampsia and intrauterine growth retardation [in Polish]. Ginekol Pol. 2005;76(9):727-734.
    • (2005) Ginekol Pol. , vol.76 , Issue.9 , pp. 727-734
    • Szewczyk, G.1    Szewczyk, A.2    Pyzlak, M.3
  • 74
    • 26244459286 scopus 로고    scopus 로고
    • Application of novel tissue microarrays to investigate expression of tryptase, chymase and KIT protein in placental mast cells
    • Noack F, Kruger S, Thorns C, et al. Application of novel tissue microarrays to investigate expression of tryptase, chymase and KIT protein in placental mast cells. Arch Gynecol Obstet. 2005;272(3):223-228.
    • (2005) Arch Gynecol Obstet. , vol.272 , Issue.3 , pp. 223-228
    • Noack, F.1    Kruger, S.2    Thorns, C.3
  • 75
    • 18244386001 scopus 로고    scopus 로고
    • Production of human mast cell chymase in human myometrium and placenta in cases of normal pregnancy and preeclampsia
    • Mitani R, Maeda K, Fukui R, et al. Production of human mast cell chymase in human myometrium and placenta in cases of normal pregnancy and preeclampsia. Eur J Obstet Gynecol Reprod Biol. 2002;101(2):155-160.
    • (2002) Eur J Obstet Gynecol Reprod Biol. , vol.101 , Issue.2 , pp. 155-160
    • Mitani, R.1    Maeda, K.2    Fukui, R.3
  • 76
    • 0029682495 scopus 로고    scopus 로고
    • Induction of primary cutaneous melanocytic neoplasms in urokinase-type plasminogen activator (uPA)-deficient and wild-type mice: Cellular blue nevi invade but do not progress to malignant melanoma in uPA-deficient animals
    • Shapiro RL, Duquette JG, Roses DF, et al. Induction of primary cutaneous melanocytic neoplasms in urokinase-type plasminogen activator (uPA)-deficient and wild-type mice: cellular blue nevi invade but do not progress to malignant melanoma in uPA-deficient animals. Cancer Res. 1996;56(15):3597-3604.
    • (1996) Cancer Res. , vol.56 , Issue.15 , pp. 3597-3604
    • Shapiro, R.L.1    Duquette, J.G.2    Roses, D.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.