메뉴 건너뛰기




Volumn 29, Issue 5, 2008, Pages 385-390

Emerging Functions of Placental Cathepsins

Author keywords

Cathepsin; Gene family; Preeclampsia; Protease

Indexed keywords

CATHEPSIN; CATHEPSIN B; CATHEPSIN L; GELATINASE A; GELATINASE B; MATRIX METALLOPROTEINASE;

EID: 43049127731     PISSN: 01434004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.placenta.2008.02.006     Document Type: Article
Times cited : (35)

References (50)
  • 1
    • 0028201409 scopus 로고
    • Pinocytosis in the rat visceral yolk sac: potential role in amino acid nutrition during the fetal period
    • Beckman D.A., Brent R.L., and Lloyd J.B. Pinocytosis in the rat visceral yolk sac: potential role in amino acid nutrition during the fetal period. Placenta 15 (1994) 171-176
    • (1994) Placenta , vol.15 , pp. 171-176
    • Beckman, D.A.1    Brent, R.L.2    Lloyd, J.B.3
  • 2
    • 4244124716 scopus 로고    scopus 로고
    • Nutrition of the human fetus during the first trimester-a review
    • Burton G.J., Hempstock J., and Jauniaux E. Nutrition of the human fetus during the first trimester-a review. Placenta 22 Suppl. A (2001) S70-S77
    • (2001) Placenta , vol.22 , Issue.SUPPL. A
    • Burton, G.J.1    Hempstock, J.2    Jauniaux, E.3
  • 3
    • 0141838123 scopus 로고    scopus 로고
    • The human first trimester gestational sac limits rather than facilitates oxygen transfer to the foetus-a review
    • Jauniaux E., Gulbis B., and Burton G.J. The human first trimester gestational sac limits rather than facilitates oxygen transfer to the foetus-a review. Placenta 24 Suppl. A (2003) S86-S93
    • (2003) Placenta , vol.24 , Issue.SUPPL. A
    • Jauniaux, E.1    Gulbis, B.2    Burton, G.J.3
  • 4
    • 33745195720 scopus 로고    scopus 로고
    • Metalloproteinases and human placental invasiveness
    • Cohen M., Meisser A., and Bischof P. Metalloproteinases and human placental invasiveness. Placenta 27 (2006) 783-793
    • (2006) Placenta , vol.27 , pp. 783-793
    • Cohen, M.1    Meisser, A.2    Bischof, P.3
  • 5
    • 0029896682 scopus 로고    scopus 로고
    • Expression and function of matrix metalloproteinases and their inhibitors at the maternal-embryonic boundary during mouse embryo implantation
    • Alexander C.M., Hansell E.J., Behrendtsen O., Flannery M.L., Kishnani N.S., Hawkes S.P., et al. Expression and function of matrix metalloproteinases and their inhibitors at the maternal-embryonic boundary during mouse embryo implantation. Development 122 (1996) 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
  • 6
    • 3242671658 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 and -9 expression increases in Mycoplasma-infected airways but is not required for microvascular remodeling
    • Baluk P., Raymond W.W., Ator E., Coussens L.M., McDonald D.M., and Caughey G.H. Matrix metalloproteinase-2 and -9 expression increases in Mycoplasma-infected airways but is not required for microvascular remodeling. Am J Physiol Lung Cell Mol Physiol 287 (2004) L307-L317
    • (2004) Am J Physiol Lung Cell Mol Physiol , vol.287
    • Baluk, P.1    Raymond, W.W.2    Ator, E.3    Coussens, L.M.4    McDonald, D.M.5    Caughey, G.H.6
  • 7
    • 0642364446 scopus 로고    scopus 로고
    • MMP-2 and MMP-9 synergize in promoting choroidal neovascularization
    • Lambert V., Wielockx B., Munaut C., Galopin C., Jost M., Itoh T., et al. MMP-2 and MMP-9 synergize in promoting choroidal neovascularization. Faseb J 17 (2003) 2290-2292
    • (2003) Faseb J , vol.17 , pp. 2290-2292
    • Lambert, V.1    Wielockx, B.2    Munaut, C.3    Galopin, C.4    Jost, M.5    Itoh, T.6
  • 8
    • 0141614998 scopus 로고    scopus 로고
    • Complex regulation of decidualization: a role for cytokines and proteases-a review
    • Salamonsen L.A., Dimitriadis E., Jones R.L., and Nie G. Complex regulation of decidualization: a role for cytokines and proteases-a review. Placenta 24 Suppl. A (2003) S76-S85
    • (2003) Placenta , vol.24 , Issue.SUPPL. A
    • Salamonsen, L.A.1    Dimitriadis, E.2    Jones, R.L.3    Nie, G.4
  • 9
    • 0017229840 scopus 로고
    • Bovine spleen cathepsin B1 and collagenolytic cathepsin
    • Etherington D.J. Bovine spleen cathepsin B1 and collagenolytic cathepsin. Biochem J 153 (1976) 199-209
    • (1976) Biochem J , vol.153 , pp. 199-209
    • Etherington, D.J.1
  • 10
    • 0020974156 scopus 로고
    • Inhibition of proteolysis in rat yolk sac as a cause of teratogenesis. Effects of leupeptin in vitro and in vivo
    • Freeman S.J., and Lloyd J.B. Inhibition of proteolysis in rat yolk sac as a cause of teratogenesis. Effects of leupeptin in vitro and in vivo. J Embryol Exp Morph 78 (1983) 183-193
    • (1983) J Embryol Exp Morph , vol.78 , pp. 183-193
    • Freeman, S.J.1    Lloyd, J.B.2
  • 11
    • 0025802942 scopus 로고
    • The activities of thiol proteases in the rat visceral yolk sac increase during late gestation
    • Grubb J.D., Koszalka T.R., Drabick J.J., and Metrione R.M. The activities of thiol proteases in the rat visceral yolk sac increase during late gestation. Placenta 12 (1991) 143-151
    • (1991) Placenta , vol.12 , pp. 143-151
    • Grubb, J.D.1    Koszalka, T.R.2    Drabick, J.J.3    Metrione, R.M.4
  • 12
    • 0027945536 scopus 로고
    • In vitro embryotoxicity of the cysteine proteinase inhibitors benzyloxycarbonyl-phenylalanine-alanine-diazomethane (Z-Phe-Ala-CHN2) and benzyloxycarbonyl-phenylalanine-phenylalanine-diazomethane (Z-Phe-Phe-CHN2)
    • Ambroso J.L., and Harris C. In vitro embryotoxicity of the cysteine proteinase inhibitors benzyloxycarbonyl-phenylalanine-alanine-diazomethane (Z-Phe-Ala-CHN2) and benzyloxycarbonyl-phenylalanine-phenylalanine-diazomethane (Z-Phe-Phe-CHN2). Teratology 50 (1994) 214-228
    • (1994) Teratology , vol.50 , pp. 214-228
    • Ambroso, J.L.1    Harris, C.2
  • 13
    • 0025763374 scopus 로고
    • Regulation of the expression of mitogen-regulated protein (MRP; proliferin) and cathepsin L in cultured cells and in the murine placenta
    • Nilsen-Hamilton M., Jang Y.J., Delgado M., Shim J.K., Bruns K., Chiang C.P., et al. Regulation of the expression of mitogen-regulated protein (MRP; proliferin) and cathepsin L in cultured cells and in the murine placenta. Mol Cell Endocrinol 77 (1991) 115-122
    • (1991) Mol Cell Endocrinol , vol.77 , pp. 115-122
    • Nilsen-Hamilton, M.1    Jang, Y.J.2    Delgado, M.3    Shim, J.K.4    Bruns, K.5    Chiang, C.P.6
  • 15
    • 0030850648 scopus 로고    scopus 로고
    • The expression and function of cystatin C and cathepsin B and cathepsin L during mouse embryo implantation and placentation
    • Afonso S., Romagnano L., and Babiarz B. The expression and function of cystatin C and cathepsin B and cathepsin L during mouse embryo implantation and placentation. Development 124 (1997) 3415-3425
    • (1997) Development , vol.124 , pp. 3415-3425
    • Afonso, S.1    Romagnano, L.2    Babiarz, B.3
  • 17
    • 0032540474 scopus 로고    scopus 로고
    • Cathepsin L: critical role in Ii degradation and CD4 T cell selection in the thymus
    • Nakagawa T., Roth W., Wong P., Nelson A., Farr A., Deussing J., et al. Cathepsin L: critical role in Ii degradation and CD4 T cell selection in the thymus. Science 280 (1998) 450-453
    • (1998) Science , vol.280 , pp. 450-453
    • Nakagawa, T.1    Roth, W.2    Wong, P.3    Nelson, A.4    Farr, A.5    Deussing, J.6
  • 19
    • 0033572317 scopus 로고    scopus 로고
    • Expression of cysteine proteases in extraembryonic tissues during mouse embryogenesis
    • Sol-Church K., Shipley J., Beckman D.A., and Mason R.W. Expression of cysteine proteases in extraembryonic tissues during mouse embryogenesis. Arch Biochem Biophys 372 (1999) 375-381
    • (1999) Arch Biochem Biophys , vol.372 , pp. 375-381
    • Sol-Church, K.1    Shipley, J.2    Beckman, D.A.3    Mason, R.W.4
  • 20
    • 0032835452 scopus 로고    scopus 로고
    • a novel murine cysteine protease of the papain family with a placenta-restricted expression
    • Tisljar K., Deussing J., Peters C., and Cathepsin J. a novel murine cysteine protease of the papain family with a placenta-restricted expression. FEBS Lett 459 (1999) 299-304
    • (1999) FEBS Lett , vol.459 , pp. 299-304
    • Tisljar, K.1    Deussing, J.2    Peters, C.3    Cathepsin, J.4
  • 24
    • 0035707911 scopus 로고    scopus 로고
    • Identification and characterization of a dense cluster of placenta-specific cysteine peptidase genes and related genes on mouse chromosome 13
    • Deussing J., Kouadio M., Rehman S., Werber I., Schwinde A., and Peters C. Identification and characterization of a dense cluster of placenta-specific cysteine peptidase genes and related genes on mouse chromosome 13. Genomics 79 (2002) 225-240
    • (2002) Genomics , vol.79 , pp. 225-240
    • Deussing, J.1    Kouadio, M.2    Rehman, S.3    Werber, I.4    Schwinde, A.5    Peters, C.6
  • 25
    • 0034634395 scopus 로고    scopus 로고
    • The evolutionary fate and consequences of duplicate genes
    • Lynch M., and Conery J.S. The evolutionary fate and consequences of duplicate genes. Science 290 (2000) 1151-1155
    • (2000) Science , vol.290 , pp. 1151-1155
    • Lynch, M.1    Conery, J.S.2
  • 27
    • 0024225853 scopus 로고
    • Isolation and characterization of a novel trophoblast-specific cDNA in the mouse
    • Lescisin K.R., Varmuza S., and Rossant J. Isolation and characterization of a novel trophoblast-specific cDNA in the mouse. Genes Dev 2 (1988) 1639-1646
    • (1988) Genes Dev , vol.2 , pp. 1639-1646
    • Lescisin, K.R.1    Varmuza, S.2    Rossant, J.3
  • 28
    • 0028818379 scopus 로고
    • A novel regulatory region is required for trophoblast-specific transcription in transgenic mice
    • Calzonetti T., Stevenson L., and Rossant J. A novel regulatory region is required for trophoblast-specific transcription in transgenic mice. Dev Biol 171 (1995) 615-626
    • (1995) Dev Biol , vol.171 , pp. 615-626
    • Calzonetti, T.1    Stevenson, L.2    Rossant, J.3
  • 29
    • 2942550705 scopus 로고    scopus 로고
    • The Hand1, Stra13 and Gcm1 transcription factors override FGF signaling to promote terminal differentiation of trophoblast stem cells
    • Hughes M., Dobric N., Scott I.C., Su L., Starovic M., St-Pierre B., et al. The Hand1, Stra13 and Gcm1 transcription factors override FGF signaling to promote terminal differentiation of trophoblast stem cells. Dev Biol 271 (2004) 26-37
    • (2004) Dev Biol , vol.271 , pp. 26-37
    • Hughes, M.1    Dobric, N.2    Scott, I.C.3    Su, L.4    Starovic, M.5    St-Pierre, B.6
  • 30
    • 0034213313 scopus 로고    scopus 로고
    • cDNA subtraction cloning reveals novel genes whose temporal and spatial expression indicates association with trophoblast invasion
    • Hemberger M., Himmelbauer H., Ruschmann J., Zeitz C., and Fundele R. cDNA subtraction cloning reveals novel genes whose temporal and spatial expression indicates association with trophoblast invasion. Dev Biol 222 (2000) 158-169
    • (2000) Dev Biol , vol.222 , pp. 158-169
    • Hemberger, M.1    Himmelbauer, H.2    Ruschmann, J.3    Zeitz, C.4    Fundele, R.5
  • 31
    • 28444475153 scopus 로고    scopus 로고
    • Placental cathepsin M is alternatively spliced and exclusively expressed in the spongiotrophoblast layer
    • Bode S., Peters C., and Deussing J.M. Placental cathepsin M is alternatively spliced and exclusively expressed in the spongiotrophoblast layer. Biochim Biophys Acta 1731 (2005) 160-167
    • (2005) Biochim Biophys Acta , vol.1731 , pp. 160-167
    • Bode, S.1    Peters, C.2    Deussing, J.M.3
  • 32
    • 0034254481 scopus 로고    scopus 로고
    • Cathepsin-6, a novel cysteine proteinase showing homology with and co-localized expression with cathepsin J/P in the labyrinthine layer of mouse placenta
    • Nakajima A., Kataoka K., Takata Y., and Huh N.H. Cathepsin-6, a novel cysteine proteinase showing homology with and co-localized expression with cathepsin J/P in the labyrinthine layer of mouse placenta. Biochem J 349 (2000) 689-692
    • (2000) Biochem J , vol.349 , pp. 689-692
    • Nakajima, A.1    Kataoka, K.2    Takata, Y.3    Huh, N.H.4
  • 34
    • 34447540379 scopus 로고    scopus 로고
    • Expression of cathepsin p mRNA, protein and activity in the rat choriocarcinoma cell line, rcho-1, during giant cell transformation
    • Hassanein M., Korant B.D., Lu G., and Mason R.W. Expression of cathepsin p mRNA, protein and activity in the rat choriocarcinoma cell line, rcho-1, during giant cell transformation. Placenta 28 (2007) 912-919
    • (2007) Placenta , vol.28 , pp. 912-919
    • Hassanein, M.1    Korant, B.D.2    Lu, G.3    Mason, R.W.4
  • 35
    • 0025840501 scopus 로고
    • Trophoblast cell differentiation: establishment, characterization, and modulation of a rat trophoblast cell line expressing members of the placental prolactin family
    • Faria T.N., and Soares M.J. Trophoblast cell differentiation: establishment, characterization, and modulation of a rat trophoblast cell line expressing members of the placental prolactin family. Endocrinology 129 (1991) 2895-2906
    • (1991) Endocrinology , vol.129 , pp. 2895-2906
    • Faria, T.N.1    Soares, M.J.2
  • 36
    • 34047214754 scopus 로고    scopus 로고
    • Diverse subtypes and developmental origins of trophoblast giant cells in the mouse placenta
    • Simmons D.G., Fortier A.L., and Cross J.C. Diverse subtypes and developmental origins of trophoblast giant cells in the mouse placenta. Dev Biol 304 (2007) 567-578
    • (2007) Dev Biol , vol.304 , pp. 567-578
    • Simmons, D.G.1    Fortier, A.L.2    Cross, J.C.3
  • 37
    • 18344376711 scopus 로고    scopus 로고
    • Dilated cardiomyopathy in mice deficient for the lysosomal cysteine peptidase cathepsin L
    • Stypmann J., Glaser K., Roth W., Tobin D.J., Petermann I., Matthias R., et al. Dilated cardiomyopathy in mice deficient for the lysosomal cysteine peptidase cathepsin L. Proc Natl Acad Sci USA 99 (2002) 6234-6239
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6234-6239
    • Stypmann, J.1    Glaser, K.2    Roth, W.3    Tobin, D.J.4    Petermann, I.5    Matthias, R.6
  • 38
    • 0036097449 scopus 로고    scopus 로고
    • The lysosomal protease cathepsin L is an important regulator of keratinocyte and melanocyte differentiation during hair follicle morphogenesis and cycling
    • Tobin D.J., Foitzik K., Reinheckel T., Mecklenburg L., Botchkarev V.A., Peters C., et al. The lysosomal protease cathepsin L is an important regulator of keratinocyte and melanocyte differentiation during hair follicle morphogenesis and cycling. Am J Pathol 160 (2002) 1807-1821
    • (2002) Am J Pathol , vol.160 , pp. 1807-1821
    • Tobin, D.J.1    Foitzik, K.2    Reinheckel, T.3    Mecklenburg, L.4    Botchkarev, V.A.5    Peters, C.6
  • 39
    • 8744307040 scopus 로고    scopus 로고
    • Cathepsin L protease (CPL-1) is essential for yolk processing during embryogenesis in Caenorhabditis elegans
    • Britton C., and Murray L. Cathepsin L protease (CPL-1) is essential for yolk processing during embryogenesis in Caenorhabditis elegans. J Cell Sci 117 (2004) 5133-5143
    • (2004) J Cell Sci , vol.117 , pp. 5133-5143
    • Britton, C.1    Murray, L.2
  • 41
    • 34547666652 scopus 로고    scopus 로고
    • Development of a specific inhibitor for the placental protease, cathepsin P
    • Hassanein M., Xue F., Seto C.T., and Mason R.W. Development of a specific inhibitor for the placental protease, cathepsin P. Arch Biochem Biophys 464 (2007) 288-292
    • (2007) Arch Biochem Biophys , vol.464 , pp. 288-292
    • Hassanein, M.1    Xue, F.2    Seto, C.T.3    Mason, R.W.4
  • 43
    • 43049100827 scopus 로고    scopus 로고
    • Processing of endoplasmic reticulum proteins by placenta specific proteases
    • Hassanein M., Glazewski L., Bojja A., Lu G., and Mason R.W. Processing of endoplasmic reticulum proteins by placenta specific proteases. Placenta 28 (2007) A77
    • (2007) Placenta , vol.28
    • Hassanein, M.1    Glazewski, L.2    Bojja, A.3    Lu, G.4    Mason, R.W.5
  • 44
    • 0032445492 scopus 로고    scopus 로고
    • Vasostatin, a calreticulin fragment, inhibits angiogenesis and suppresses tumor growth
    • Pike S.E., Yao L., Jones K.D., Cherney B., Appella E., Sakaguchi K., et al. Vasostatin, a calreticulin fragment, inhibits angiogenesis and suppresses tumor growth. J Exp Med 188 (1998) 2349-2356
    • (1998) J Exp Med , vol.188 , pp. 2349-2356
    • Pike, S.E.1    Yao, L.2    Jones, K.D.3    Cherney, B.4    Appella, E.5    Sakaguchi, K.6
  • 45
    • 43049089469 scopus 로고    scopus 로고
    • Cathepsin proteases have distinct roles in trophoblast function and vascular remodelling
    • Hemberger M., Delourme A., Screen M., Dean W., and Cross J.C. Cathepsin proteases have distinct roles in trophoblast function and vascular remodelling. Placenta 28 (2007) A62
    • (2007) Placenta , vol.28
    • Hemberger, M.1    Delourme, A.2    Screen, M.3    Dean, W.4    Cross, J.C.5
  • 46
    • 40849142271 scopus 로고    scopus 로고
    • Characteristics and significance of trophoblast giant cells
    • Hemberger M. Characteristics and significance of trophoblast giant cells. Placenta 22 (2008) S4-S9
    • (2008) Placenta , vol.22
    • Hemberger, M.1
  • 47
    • 0141831692 scopus 로고    scopus 로고
    • Cathepsin V is involved in the degradation of invariant chain in human thymus and is overexpressed in myasthenia gravis
    • Tolosa E., Li W., Yasuda Y., Wienhold W., Denzin L.K., Lautwein A., et al. Cathepsin V is involved in the degradation of invariant chain in human thymus and is overexpressed in myasthenia gravis. J Clin Invest 112 (2003) 517-526
    • (2003) J Clin Invest , vol.112 , pp. 517-526
    • Tolosa, E.1    Li, W.2    Yasuda, Y.3    Wienhold, W.4    Denzin, L.K.5    Lautwein, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.