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Volumn 77, Issue 3, 2007, Pages 433-441

Heparanase expression and function during early pregnancy in mice

Author keywords

Decidua; Embryo; Endometrium; Heparanase; Implantation; Mice; Pregnancy; Trophoblast

Indexed keywords

GLYCOSIDASE INHIBITOR; HEPARANASE; PI 88; UNCLASSIFIED DRUG;

EID: 34548217637     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod.107.061317     Document Type: Article
Times cited : (25)

References (67)
  • 1
    • 0037150686 scopus 로고    scopus 로고
    • Deciphering the cross-talk of implantation: Advances and challenges
    • Paria BC, Reese J, Das SK, Dey SK. Deciphering the cross-talk of implantation: advances and challenges. Science 2002; 296:2185-2188.
    • (2002) Science , vol.296 , pp. 2185-2188
    • Paria, B.C.1    Reese, J.2    Das, S.K.3    Dey, S.K.4
  • 2
    • 0035011761 scopus 로고    scopus 로고
    • Implantation: Molecular basis of embryo-uterine dialogue
    • Paria BC, Song H, Dey SK. Implantation: molecular basis of embryo-uterine dialogue. Int J Dev Biol 2001; 45:597-605.
    • (2001) Int J Dev Biol , vol.45 , pp. 597-605
    • Paria, B.C.1    Song, H.2    Dey, S.K.3
  • 4
    • 0026755575 scopus 로고
    • Penetration of the uterine epithelial basement membrane during blastocyst implantation in the mouse
    • Blankenship TN, Given RL. Penetration of the uterine epithelial basement membrane during blastocyst implantation in the mouse. Anat Rec 1992; 233:196-204.
    • (1992) Anat Rec , vol.233 , pp. 196-204
    • Blankenship, T.N.1    Given, R.L.2
  • 5
    • 0036169742 scopus 로고    scopus 로고
    • Evidence for coordinated interaction of cyclin D3 with p21 and cdk6 in directing the development of uterine stromal cell decidualization and polyploidy during implantation
    • Tan J, Raja S, Davis MK, Tawfik O, Dey SK, Das SK. Evidence for coordinated interaction of cyclin D3 with p21 and cdk6 in directing the development of uterine stromal cell decidualization and polyploidy during implantation. Mech Dev 2002; 111:99-113.
    • (2002) Mech Dev , vol.111 , pp. 99-113
    • Tan, J.1    Raja, S.2    Davis, M.K.3    Tawfik, O.4    Dey, S.K.5    Das, S.K.6
  • 6
    • 33748471504 scopus 로고    scopus 로고
    • Uterine angiogenesis during implantation and decidualization in mice
    • Matsumoto H, Sato E. Uterine angiogenesis during implantation and decidualization in mice. Reproductive Medicine and Biology 2006; 5:81-86.
    • (2006) Reproductive Medicine and Biology , vol.5 , pp. 81-86
    • Matsumoto, H.1    Sato, E.2
  • 7
    • 0029896682 scopus 로고    scopus 로고
    • Expression and function of matrix metalloproteinases and their inhibitors at the maternal-embryonic boundary during mouse embryo implantation
    • Alexander CM, Hansell EJ, Behrendtsen O, Flannery ML, Kishnani NS, Hawkes SP, Werb Z. Expression and function of matrix metalloproteinases and their inhibitors at the maternal-embryonic boundary during mouse embryo implantation. Development 1996; 122:1723-1736.
    • (1996) Development , vol.122 , pp. 1723-1736
    • Alexander, C.M.1    Hansell, E.J.2    Behrendtsen, O.3    Flannery, M.L.4    Kishnani, N.S.5    Hawkes, S.P.6    Werb, Z.7
  • 8
    • 26444523020 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase-26 (MMP-26) mRNA in mouse uterus during the estrous cycle and early pregnancy
    • Liu G, Zhang X, Lin H, Li Q, Wang H, Ni J, Amy Sang QX, Zhu C. Expression of matrix metalloproteinase-26 (MMP-26) mRNA in mouse uterus during the estrous cycle and early pregnancy. Life Sci 2005; 77: 3355-3365.
    • (2005) Life Sci , vol.77 , pp. 3355-3365
    • Liu, G.1    Zhang, X.2    Lin, H.3    Li, Q.4    Wang, H.5    Ni, J.6    Amy Sang, Q.X.7    Zhu, C.8
  • 9
    • 0030800833 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in the mouse uterus during the peri-implantation period
    • Das SK, Yano S, Wang J, Edwards DR, Nagase H, Dey SK. Expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in the mouse uterus during the peri-implantation period. Dev Genet 1997; 21:44-54.
    • (1997) Dev Genet , vol.21 , pp. 44-54
    • Das, S.K.1    Yano, S.2    Wang, J.3    Edwards, D.R.4    Nagase, H.5    Dey, S.K.6
  • 11
    • 0031657808 scopus 로고    scopus 로고
    • Matrix proteoglycans: From molecular design to cellular function
    • Iozzo RV. Matrix proteoglycans: from molecular design to cellular function. Annu Rev Biochem 1998; 67:609-652.
    • (1998) Annu Rev Biochem , vol.67 , pp. 609-652
    • Iozzo, R.V.1
  • 12
    • 0034959158 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans: Intricate molecules with intriguing functions
    • Iozzo RV. Heparan sulfate proteoglycans: intricate molecules with intriguing functions. J Clin Invest 2001; 108:165-167.
    • (2001) J Clin Invest , vol.108 , pp. 165-167
    • Iozzo, R.V.1
  • 13
    • 0029379849 scopus 로고
    • In the clutches of proteoglycans: How does heparan sulfate regulate FGF binding?
    • Rapraeger AC. In the clutches of proteoglycans: how does heparan sulfate regulate FGF binding? Chem Biol 1995; 2:645-649.
    • (1995) Chem Biol , vol.2 , pp. 645-649
    • Rapraeger, A.C.1
  • 14
    • 0035782873 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans in invasion and metastasis
    • Sanderson RD. Heparan sulfate proteoglycans in invasion and metastasis. Semin Cell Dev Biol 2001; 12:89-98.
    • (2001) Semin Cell Dev Biol , vol.12 , pp. 89-98
    • Sanderson, R.D.1
  • 15
    • 0035443744 scopus 로고    scopus 로고
    • Role of heparan sulfate in fibroblast growth factor signalling: A structural view
    • Pellegrini L. Role of heparan sulfate in fibroblast growth factor signalling: a structural view. Curr Opin Struct Biol 2001; 11:629-634.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 629-634
    • Pellegrini, L.1
  • 16
    • 0021354360 scopus 로고
    • Metastatic melanoma cell heparanase. Characterization of heparan sulfate degradation fragments produced by B16 melanoma endoglucuronidase
    • Nakajima M, Irimura T, Di Ferrante N, Nicolson GL. Metastatic melanoma cell heparanase. Characterization of heparan sulfate degradation fragments produced by B16 melanoma endoglucuronidase. J Biol Chem 1984; 259:2283-2290.
    • (1984) J Biol Chem , vol.259 , pp. 2283-2290
    • Nakajima, M.1    Irimura, T.2    Di Ferrante, N.3    Nicolson, G.L.4
  • 17
    • 0034937208 scopus 로고    scopus 로고
    • Heparanases: Endoglycosidases that degrade heparan sulfate proteoglycans
    • Bame KJ. Heparanases: endoglycosidases that degrade heparan sulfate proteoglycans. Glycobiology 2001; 11:91R-98R.
    • (2001) Glycobiology , vol.11
    • Bame, K.J.1
  • 18
    • 0033200324 scopus 로고    scopus 로고
    • Evidence that platelet and tumour heparanases are similar enzymes
    • Freeman C, Browne AM, Parish CR. Evidence that platelet and tumour heparanases are similar enzymes. Biochem J 1999; 342(Pt 2):361-368.
    • (1999) Biochem J , vol.342 , Issue.PART 2 , pp. 361-368
    • Freeman, C.1    Browne, A.M.2    Parish, C.R.3
  • 19
    • 0024793675 scopus 로고
    • Human mononuclear cells contain an endoglycosidase specific for heparan sulphate glycosaminoglycan demonstrable with the use of a specific solid-phase metabolically radiolabeled substrate
    • Sewell RF, Brenchley PE, Mallick NP. Human mononuclear cells contain an endoglycosidase specific for heparan sulphate glycosaminoglycan demonstrable with the use of a specific solid-phase metabolically radiolabeled substrate. Biochem J 1989; 264:777-783.
    • (1989) Biochem J , vol.264 , pp. 777-783
    • Sewell, R.F.1    Brenchley, P.E.2    Mallick, N.P.3
  • 21
    • 0022382680 scopus 로고
    • Degradation of heparan sulfate in the subendothelial extracellular matrix by a readily released heparanase from human neutrophils. Possible role in invasion through basement membranes
    • Matzner Y, Bar-Ner M, Yahalom J, Ishai-Michaeli R, Fuks Z, Vlodavsky I. Degradation of heparan sulfate in the subendothelial extracellular matrix by a readily released heparanase from human neutrophils. Possible role in invasion through basement membranes. J Clin Invest 1985; 76:1306-1313.
    • (1985) J Clin Invest , vol.76 , pp. 1306-1313
    • Matzner, Y.1    Bar-Ner, M.2    Yahalom, J.3    Ishai-Michaeli, R.4    Fuks, Z.5    Vlodavsky, I.6
  • 22
    • 0030687573 scopus 로고    scopus 로고
    • Major co-localization of the extracellular-matrix degradative enzymes heparanase and gelatinase in tertiary granules of human neutrophils
    • Mollinedo F, Nakajima M, Llorens A, Barbosa E, Callejo S, Gajate C, Fabra A. Major co-localization of the extracellular-matrix degradative enzymes heparanase and gelatinase in tertiary granules of human neutrophils. Biochem J 1997; 327(Pt 3):917-923.
    • (1997) Biochem J , vol.327 , Issue.PART 3 , pp. 917-923
    • Mollinedo, F.1    Nakajima, M.2    Llorens, A.3    Barbosa, E.4    Callejo, S.5    Gajate, C.6    Fabra, A.7
  • 25
  • 27
    • 0033588093 scopus 로고    scopus 로고
    • Human heparanase. Purification, characterization, cloning, and expression
    • Toyoshima M, Nakajima M. Human heparanase. Purification, characterization, cloning, and expression. J Biol Chem 1999; 274:24153-24160.
    • (1999) J Biol Chem , vol.274 , pp. 24153-24160
    • Toyoshima, M.1    Nakajima, M.2
  • 30
    • 0028916622 scopus 로고
    • Molecular behavior adapts to context: Heparanase functions as an extracellular matrix-degrading enzyme or as a T cell adhesion molecule, depending on the local pH
    • Gilat D, Hershkoviz R, Goldkom I, Cahalon L, Korner G, Vlodavsky I, Lider O. Molecular behavior adapts to context: heparanase functions as an extracellular matrix-degrading enzyme or as a T cell adhesion molecule, depending on the local pH. J Exp Med 1995; 181:1929-1934.
    • (1995) J Exp Med , vol.181 , pp. 1929-1934
    • Gilat, D.1    Hershkoviz, R.2    Goldkom, I.3    Cahalon, L.4    Korner, G.5    Vlodavsky, I.6    Lider, O.7
  • 32
    • 0034904048 scopus 로고    scopus 로고
    • Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis
    • Vlodavsky I, Friedmann Y. Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis. J Clin Invest 2001; 108: 341-347.
    • (2001) J Clin Invest , vol.108 , pp. 341-347
    • Vlodavsky, I.1    Friedmann, Y.2
  • 37
    • 0034050073 scopus 로고    scopus 로고
    • Heparanase expression in invasive trophoblasts and acute vascular damage
    • Dempsey LA, Plummer TB, Coombes SL, Platt JL. Heparanase expression in invasive trophoblasts and acute vascular damage. Glycobiology 2000; 10:467-475.
    • (2000) Glycobiology , vol.10 , pp. 467-475
    • Dempsey, L.A.1    Plummer, T.B.2    Coombes, S.L.3    Platt, J.L.4
  • 40
    • 10744232455 scopus 로고    scopus 로고
    • Transgenic expression of mammalian heparanase uncovers physiological functions of heparan sulfate in tissue morphogenesis, vascularization, and feeding behavior
    • Zcharia E, Metzger S, Chajek-Shaul T, Aingorn H, Elkin M, Friedmann Y, Weinstein T, Li JP, Lindahl U, Vlodavsky I. Transgenic expression of mammalian heparanase uncovers physiological functions of heparan sulfate in tissue morphogenesis, vascularization, and feeding behavior. FASEB J 2004; 18:252-263.
    • (2004) FASEB J , vol.18 , pp. 252-263
    • Zcharia, E.1    Metzger, S.2    Chajek-Shaul, T.3    Aingorn, H.4    Elkin, M.5    Friedmann, Y.6    Weinstein, T.7    Li, J.P.8    Lindahl, U.9    Vlodavsky, I.10
  • 43
    • 33846280793 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of an alternatively spliced variant of human heparanase
    • Nasser NJ, Avivi A, Shushy M, Vlodavsky I, Nevo E. Cloning, expression, and characterization of an alternatively spliced variant of human heparanase. Biochem Biophys Res Commun 2007; 354:33-38.
    • (2007) Biochem Biophys Res Commun , vol.354 , pp. 33-38
    • Nasser, N.J.1    Avivi, A.2    Shushy, M.3    Vlodavsky, I.4    Nevo, E.5
  • 45
    • 20444394457 scopus 로고    scopus 로고
    • A functional heparan sulfate mimetic implicates both heparanase and heparan sulfate in tumor angiogenesis and invasion in a mouse model of multistage cancer
    • Joyce JA, Freeman C, Meyer-Morse N, Parish CR, Hanahan D. A functional heparan sulfate mimetic implicates both heparanase and heparan sulfate in tumor angiogenesis and invasion in a mouse model of multistage cancer. Oncogene 2005; 24:4037-4051.
    • (2005) Oncogene , vol.24 , pp. 4037-4051
    • Joyce, J.A.1    Freeman, C.2    Meyer-Morse, N.3    Parish, C.R.4    Hanahan, D.5
  • 46
    • 0028216364 scopus 로고
    • Heparin-binding EGF-like growth factor gene is induced in the mouse uterus temporally by the blastocyst solely at the site of its apposition: A possible ligand for interaction with blastocyst EGF-receptor in implantation
    • Das SK, Wang XN, Paria BC, Damm D, Abraham JA, Klagsbrun M, Andrews GK, Dey SK. Heparin-binding EGF-like growth factor gene is induced in the mouse uterus temporally by the blastocyst solely at the site of its apposition: a possible ligand for interaction with blastocyst EGF-receptor in implantation. Development 1994; 120:1071-1083.
    • (1994) Development , vol.120 , pp. 1071-1083
    • Das, S.K.1    Wang, X.N.2    Paria, B.C.3    Damm, D.4    Abraham, J.A.5    Klagsbrun, M.6    Andrews, G.K.7    Dey, S.K.8
  • 47
    • 0021258357 scopus 로고
    • Biosynthesis of heparan sulfate proteoglycan by human colon carcinoma cells and its localization at the cell surface
    • Iozzo RV. Biosynthesis of heparan sulfate proteoglycan by human colon carcinoma cells and its localization at the cell surface. J Cell Biol 1984; 99: 403-417.
    • (1984) J Cell Biol , vol.99 , pp. 403-417
    • Iozzo, R.V.1
  • 48
    • 0030768320 scopus 로고    scopus 로고
    • Neurotrophin stimulation of human melanoma cell invasion: Selected enhancement of heparanase activity and heparanase degradation of specific heparan sulfate subpopulations
    • Marchetti D, Nicolson GL. Neurotrophin stimulation of human melanoma cell invasion: selected enhancement of heparanase activity and heparanase degradation of specific heparan sulfate subpopulations. Adv Enzyme Regul 1997; 37:111-134.
    • (1997) Adv Enzyme Regul , vol.37 , pp. 111-134
    • Marchetti, D.1    Nicolson, G.L.2
  • 49
    • 0035907101 scopus 로고    scopus 로고
    • Large-scale preparation of the oligosaccharide phosphate fraction of Pichia holstii NRRL Y-2448 phosphomannan for use in the manufacture of PI-88
    • Ferro V, Fewings K, Palermo MC, Li C. Large-scale preparation of the oligosaccharide phosphate fraction of Pichia holstii NRRL Y-2448 phosphomannan for use in the manufacture of PI-88. Carbohydr Res 2001; 332:183-189.
    • (2001) Carbohydr Res , vol.332 , pp. 183-189
    • Ferro, V.1    Fewings, K.2    Palermo, M.C.3    Li, C.4
  • 51
    • 0033565247 scopus 로고    scopus 로고
    • Identification of sulfated oligosaccharide-based inhibitors of tumor growth and metastasis using novel in vitro assays for angiogenesis and heparanase activity
    • Parish CR, Freeman C, Brown KJ, Francis DJ, Cowden WB. Identification of sulfated oligosaccharide-based inhibitors of tumor growth and metastasis using novel in vitro assays for angiogenesis and heparanase activity. Cancer Res 1999; 59:3433-3441.
    • (1999) Cancer Res , vol.59 , pp. 3433-3441
    • Parish, C.R.1    Freeman, C.2    Brown, K.J.3    Francis, D.J.4    Cowden, W.B.5
  • 52
    • 0027483498 scopus 로고
    • Heparan sulfate proteoglycan (perlecan) expression by mouse embryos during acquisition of attachment competence
    • Carson DD, Tang JP, Julian J. Heparan sulfate proteoglycan (perlecan) expression by mouse embryos during acquisition of attachment competence. Dev Biol 1993; 155:97-106.
    • (1993) Dev Biol , vol.155 , pp. 97-106
    • Carson, D.D.1    Tang, J.P.2    Julian, J.3
  • 53
    • 0031128276 scopus 로고    scopus 로고
    • Expression of heparan sulfate proteoglycan (perlecan) in the mouse blastocyst is regulated during normal and delayed implantation
    • Smith SE, French MM, Julian J, Paria BC, Dey SK, Carson DD. Expression of heparan sulfate proteoglycan (perlecan) in the mouse blastocyst is regulated during normal and delayed implantation. Dev Biol 1997; 184:38-47.
    • (1997) Dev Biol , vol.184 , pp. 38-47
    • Smith, S.E.1    French, M.M.2    Julian, J.3    Paria, B.C.4    Dey, S.K.5    Carson, D.D.6
  • 54
    • 0033620651 scopus 로고    scopus 로고
    • Expression of the heparan sulfate proteoglycan, perlecan, during mouse embryogenesis and perlecan chondrogenic activity in vitro
    • French MM, Smith SE, Akanbi K, Sanford T, Hecht J, Farach-Carson MC, Carson DD. Expression of the heparan sulfate proteoglycan, perlecan, during mouse embryogenesis and perlecan chondrogenic activity in vitro. J Cell Biol 1999; 145:1103-1115.
    • (1999) J Cell Biol , vol.145 , pp. 1103-1115
    • French, M.M.1    Smith, S.E.2    Akanbi, K.3    Sanford, T.4    Hecht, J.5    Farach-Carson, M.C.6    Carson, D.D.7
  • 55
    • 0028606792 scopus 로고
    • The immunolocalization of basic fibroblast growth factor in the mouse uterus during the initial stages of embryo implantation
    • Wordinger RJ, Smith KJ, Bell C, Chang IF. The immunolocalization of basic fibroblast growth factor in the mouse uterus during the initial stages of embryo implantation. Growth Factors 1994; 11:175-186.
    • (1994) Growth Factors , vol.11 , pp. 175-186
    • Wordinger, R.J.1    Smith, K.J.2    Bell, C.3    Chang, I.F.4
  • 56
    • 0026409751 scopus 로고
    • Changes in the immunolocalization of bFGF in the mouse endometrium during implantation
    • Wordinger RJ, Moss AE, Chang IF, Jackson T. Changes in the immunolocalization of bFGF in the mouse endometrium during implantation. Ann N Y Acad Sci 1991; 638:491-493.
    • (1991) Ann N Y Acad Sci , vol.638 , pp. 491-493
    • Wordinger, R.J.1    Moss, A.E.2    Chang, I.F.3    Jackson, T.4
  • 57
    • 0345731236 scopus 로고    scopus 로고
    • HB-EGF directs stromal cell polyploidy and decidualization via cyclin D3 during implantation
    • Tan Y, Li M, Cox S, Davis MK, Tawfik O, Paria BC, Das SK. HB-EGF directs stromal cell polyploidy and decidualization via cyclin D3 during implantation. Dev Biol 2004; 265:181-195.
    • (2004) Dev Biol , vol.265 , pp. 181-195
    • Tan, Y.1    Li, M.2    Cox, S.3    Davis, M.K.4    Tawfik, O.5    Paria, B.C.6    Das, S.K.7
  • 65
    • 2542494203 scopus 로고    scopus 로고
    • Heparanase induces endothelial cell migration via protein kinase B/Akt activation
    • Gingis-Velitski S, Zetser A, Flugelman MY, Vlodavsky I, Ilan N. Heparanase induces endothelial cell migration via protein kinase B/Akt activation. J Biol Chem 2004; 279:23536-23541.
    • (2004) J Biol Chem , vol.279 , pp. 23536-23541
    • Gingis-Velitski, S.1    Zetser, A.2    Flugelman, M.Y.3    Vlodavsky, I.4    Ilan, N.5
  • 66
    • 1542319836 scopus 로고    scopus 로고
    • Heparanase degrades syndecan-1 and perlecan heparan sulfate: Functional implications for tumor cell invasion
    • Reiland J, Sanderson RD, Waguespack M, Barker SA, Long R, Carson DD, Marchetti D. Heparanase degrades syndecan-1 and perlecan heparan sulfate: functional implications for tumor cell invasion. J Biol Chem 2004; 279:8047-8055.
    • (2004) J Biol Chem , vol.279 , pp. 8047-8055
    • Reiland, J.1    Sanderson, R.D.2    Waguespack, M.3    Barker, S.A.4    Long, R.5    Carson, D.D.6    Marchetti, D.7
  • 67
    • 33745949315 scopus 로고    scopus 로고
    • FGF2 binding, signaling, and angiogenesis are modulated by heparanase in metastatic melanoma cells
    • Reiland J, Kempf D, Roy M, Denkins Y, Marchetti D. FGF2 binding, signaling, and angiogenesis are modulated by heparanase in metastatic melanoma cells. Neoplasia 2006; 8:596-606.
    • (2006) Neoplasia , vol.8 , pp. 596-606
    • Reiland, J.1    Kempf, D.2    Roy, M.3    Denkins, Y.4    Marchetti, D.5


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