메뉴 건너뛰기




Volumn 54, Issue 21, 1994, Pages 5702-5710

A Potential Marker Protease of Invasiveness, Seprase, Is Localized on Invadopodia of Human Malignant Melanoma Cells

Author keywords

[No Author keywords available]

Indexed keywords

PROTEINASE;

EID: 0028152543     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (217)

References (49)
  • 1
    • 0023770128 scopus 로고
    • Cancer metastasis: tumor cell and host organ properties important in metastasis to specific sites. Biochim
    • Nicolson, G.L. Cancer metastasis: tumor cell and host organ properties important in metastasis to specific sites. Biochim. Biophys. Acta, 948: 175-224, 1988.
    • (1988) Biophys. Acta , vol.948 , pp. 175-224
    • Nicolson, G.L.1
  • 2
    • 0026067043 scopus 로고
    • Cancer Metastasis
    • Fidler, I.J. Cancer Metastasis. Br. Med. Bull. 47: 157-177, 1991.
    • (1991) Br. Med. Bull. , vol.47 , pp. 157-177
    • Fidler, I.J.1
  • 3
    • 0027535914 scopus 로고
    • Biology and biochemistry of proteinases in tumor invasion
    • Mignatti, P. and Rifkin, D.B. Biology and biochemistry of proteinases in tumor invasion. Physiol. Rev. 73: 161-195, 1993.
    • (1993) Physiol. Rev. , vol.73 , pp. 161-195
    • Mignatti, P.1    Rifkin, D.B.2
  • 4
    • 0027333411 scopus 로고
    • Tumor cell interactions with the extracellular matrix during invasion and metastasis
    • Stetler-Stevenson, W.G. Aznavoorian, S. and Liotta, L.A. Tumor cell interactions with the extracellular matrix during invasion and metastasis. Annu. Rev. Cell Biol. 9: 541-573, 1993.
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 541-573
    • Stetler-Stevenson, W.G.1    Aznavoorian, S.2    Liotta, L.A.3
  • 5
    • 0027683226 scopus 로고
    • Structural biochemistry and activation of matrix metalloproteases
    • Kleiner, D.E. Jr. and Stetler-Stevenson, W.G. Structural biochemistry and activation of matrix metalloproteases. Curr. Opin. Cell Biol. 5: 891-897, 1993.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 891-897
    • Kleiner, D.E.1    Stetler-Stevenson, W.G.2
  • 6
    • 0000999998 scopus 로고
    • Extracellular matrix degradation
    • In: E.D. Hay (ed.), New York: Plenum Publishing Corp.
    • Alexander, C.M. and Werb, Z. Extracellular matrix degradation. In: E.D. Hay (ed.), Cell Biology of Extracellular Matrix, pp. 255-302. New York: Plenum Publishing Corp. 1991.
    • (1991) Cell Biology of Extracellular Matrix , pp. 255-302
    • Alexander, C.M.1    Werb, Z.2
  • 8
    • 0026341460 scopus 로고
    • In vivo paracrine interaction between urokinase and its receptor: effect on tumor cell invasion
    • Ossowski, L. Clunie, G. Masucci, M.T. and Blasi, F. In vivo paracrine interaction between urokinase and its receptor: effect on tumor cell invasion. J. Cell Biol. 115: 1107-1112, 1991.
    • (1991) J. Cell Biol. , vol.115 , pp. 1107-1112
    • Ossowski, L.1    Clunie, G.2    Masucci, M.T.3    Blasi, F.4
  • 10
    • 0023575526 scopus 로고
    • Properties of a plasma membrane-associated cathepsin B-like cysteine proteinase in metastatic B16 melanoma variants
    • Rozhin, J. Robinson, D. Stevens, M.A. Lah, T.T. Honn, K.V. Ryan, R.E. and Sloane, B.F. Properties of a plasma membrane-associated cathepsin B-like cysteine proteinase in metastatic B16 melanoma variants. Cancer Res. 47: 6620-6628, 1987.
    • (1987) Cancer Res. , vol.47 , pp. 6620-6628
    • Rozhin, J.1    Robinson, D.2    Stevens, M.A.3    Lah, T.T.4    Honn, K.V.5    Ryan, R.E.6    Sloane, B.F.7
  • 11
    • 0025413403 scopus 로고
    • The role of cathepsin L in malignant transformation
    • Kane, S.E. and Gottesman, M.M. The role of cathepsin L in malignant transformation. Semin. Cancer Biol. 1: 127-136, 1990.
    • (1990) Semin. Cancer Biol. , vol.1 , pp. 127-136
    • Kane, S.E.1    Gottesman, M.M.2
  • 12
    • 0026753602 scopus 로고
    • Correlation of tumor cytosol cathepsin D with differentiation and invasiveness of endometrial adenocarcinoma
    • Nazeer, T. Malfetano, J.H. Rosano, T.G. and Ross, J.S. Correlation of tumor cytosol cathepsin D with differentiation and invasiveness of endometrial adenocarcinoma. Am. J. Clin. Pathol. 97: 764-769, 1992.
    • (1992) Am. J. Clin. Pathol. , vol.97 , pp. 764-769
    • Nazeer, T.1    Malfetano, J.H.2    Rosano, T.G.3    Ross, J.S.4
  • 13
    • 0026779307 scopus 로고
    • Cathepsin D in breast cancer: a tissue marker associated with metastasis
    • Rochefort, H. Cathepsin D in breast cancer: a tissue marker associated with metastasis. Eur. J. Cancer, 28 A: 1780-1783, 1992.
    • (1992) Eur. J. Cancer , vol.28 , pp. 1780-1783
    • Rochefort, H.1
  • 14
    • 0027650966 scopus 로고
    • Proteases of cell adhesion proteins in cancer
    • Monsky, W.L. and Chen, W.T. Proteases of cell adhesion proteins in cancer. Semin. Cancer Biol. 4: 251-258, 1993.
    • (1993) Semin. Cancer Biol. , vol.4 , pp. 251-258
    • Monsky, W.L.1    Chen, W.T.2
  • 15
    • 0025945850 scopus 로고
    • Directed plasminogen activation at the surface of normal and malignant cells
    • Pollanen, J. Stephens, R.W. and Vaheri, A. Directed plasminogen activation at the surface of normal and malignant cells. Adv. Cancer Res. 57: 273-328, 1991.
    • (1991) Adv. Cancer Res. , vol.57 , pp. 273-328
    • Pollanen, J.1    Stephens, R.W.2    Vaheri, A.3
  • 18
    • 0023942788 scopus 로고
    • Surface receptors for urokinase plasminogen activator
    • Blasi, F. Surface receptors for urokinase plasminogen activator. Fibrinolysis, 2: 73-84, 1988.
    • (1988) Fibrinolysis , vol.2 , pp. 73-84
    • Blasi, F.1
  • 19
    • 0021248709 scopus 로고
    • Expression of transformation-associated protease(s) that degrade fibronectin at cell contact sites
    • Chen, W.T. Olden, K. Bernard, B.A. and Chu, F.F. Expression of transformation-associated protease(s) that degrade fibronectin at cell contact sites. J. Cell Biol. 98: 1546-1555, 1984.
    • (1984) J. Cell Biol. , vol.98 , pp. 1546-1555
    • Chen, W.T.1    Olden, K.2    Bernard, B.A.3    Chu, F.F.4
  • 22
    • 0025129681 scopus 로고
    • Localization of collagenase at the basal plasma membrane of a human pancreatic carcinoma cell line
    • Moll, U.M. Lane, B. Zucker, S. Suzuki, K. and Nagase, H. Localization of collagenase at the basal plasma membrane of a human pancreatic carcinoma cell line. Cancer Res. 50: 6995-7002, 1990.
    • (1990) Cancer Res. , vol.50 , pp. 6995-7002
    • Moll, U.M.1    Lane, B.2    Zucker, S.3    Suzuki, K.4    Nagase, H.5
  • 23
    • 0023158285 scopus 로고
    • Enrichment of collagen and gelatin degrading activities in the plasma membranes of human cancer cells
    • Zucker, S. Wieman, J.M. Lysik, R.M. Wilkie, D. Ramamurthy, N.S. Golub, L.M. and Lane, B. Enrichment of collagen and gelatin degrading activities in the plasma membranes of human cancer cells. Cancer Res. 47: 1608-1614, 1987.
    • (1987) Cancer Res. , vol.47 , pp. 1608-1614
    • Zucker, S.1    Wieman, J.M.2    Lysik, R.M.3    Wilkie, D.4    Ramamurthy, N.S.5    Golub, L.M.6    Lane, B.7
  • 25
    • 0026467070 scopus 로고
    • Membrane proteases: roles in tissue remodeling and tumour invasion
    • Chen, W.T. Membrane proteases: roles in tissue remodeling and tumour invasion. Curr. Opin. Cell Biol. 4: 802-809, 1992.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 802-809
    • Chen, W.T.1
  • 26
    • 0023667821 scopus 로고
    • Fibronectin-degrading proteases from the membranes of transformed cells
    • Chen, J.M. and Chen, W.T. Fibronectin-degrading proteases from the membranes of transformed cells. Cell, 48: 193-203, 1987.
    • (1987) Cell , vol.48 , pp. 193-203
    • Chen, J.M.1    Chen, W.T.2
  • 27
    • 0023094112 scopus 로고
    • Proteases occurring in the cell membrane: a possible cell receptor for the Bowman-Birk type of protease inhibitors
    • Yavelow, J. Caggana, M. and Beck, K.A. Proteases occurring in the cell membrane: a possible cell receptor for the Bowman-Birk type of protease inhibitors. Cancer Res. 47: 1598-1601, 1987.
    • (1987) Cancer Res. , vol.47 , pp. 1598-1601
    • Yavelow, J.1    Caggana, M.2    Beck, K.A.3
  • 28
    • 0025029188 scopus 로고
    • A 170-kDa membrane-bound protease is associated with the expression of invasiveness by human malignant melanoma cells
    • Aoyama, A. and Chen, W.T. A 170-kDa membrane-bound protease is associated with the expression of invasiveness by human malignant melanoma cells. Proc. Natl. Acad. Sci. USA, 87: 8296-8300, 1990.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8296-8300
    • Aoyama, A.1    Chen, W.T.2
  • 29
    • 0024414571 scopus 로고
    • Proteolytic activity of specialized surface protrusions formed at rosette contact sites of transformed cells
    • Chen, W.T. Proteolytic activity of specialized surface protrusions formed at rosette contact sites of transformed cells. J. Exp. Zool. 251: 167-185, 1989.
    • (1989) J. Exp. Zool. , vol.251 , pp. 167-185
    • Chen, W.T.1
  • 30
    • 0025853849 scopus 로고
    • Cellular invasion into matrix beads: localization of beta 1 integrins and fibronectin to the invadopodia
    • Mueller, S.C. and Chen, W.T. Cellular invasion into matrix beads: localization of beta 1 integrins and fibronectin to the invadopodia. J. Cell Sci. 99: 213-225, 1991.
    • (1991) J. Cell Sci. , vol.99 , pp. 213-225
    • Mueller, S.C.1    Chen, W.T.2
  • 31
    • 0026457798 scopus 로고
    • Tyrosine phosphorylation of membrane proteins mediates cellular invasion by transformed cells
    • Mueller, S.C. Yeh, Y. and Chen, W.T. Tyrosine phosphorylation of membrane proteins mediates cellular invasion by transformed cells. J. Cell Biol. 119: 1309-1325, 1992.
    • (1992) J. Cell Biol. , vol.119 , pp. 1309-1325
    • Mueller, S.C.1    Yeh, Y.2    Chen, W.T.3
  • 32
    • 0028115933 scopus 로고
    • Invadopodia promote proteolysis of a wide variety of extracellular matrix proteins
    • Kelly, T. Mueller, S.C. Yeh, Y. and Chen, W.T. Invadopodia promote proteolysis of a wide variety of extracellular matrix proteins. J. Cell. Physiol. 158: 299-308, 1994.
    • (1994) J. Cell. Physiol. , vol.158 , pp. 299-308
    • Kelly, T.1    Mueller, S.C.2    Yeh, Y.3    Chen, W.T.4
  • 33
    • 0021833967 scopus 로고
    • Local degradation of fibronectin at sites of expression of the transforming gene product pp. 60src
    • Chen, W.T. Chen, J.M. Parsons, S.J. and Parsons, J.T. Local degradation of fibronectin at sites of expression of the transforming gene product pp. 60src. Nature (Lond.), 316: 156-158, 1985.
    • (1985) Nature (Lond.) , vol.316 , pp. 156-158
    • Chen, W.T.1    Chen, J.M.2    Parsons, S.J.3    Parsons, J.T.4
  • 34
    • 0024150623 scopus 로고
    • Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge, K. Fath, K. Kelly, T. Nuckolls, G. and Turner, C. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell Biol. 4: 487-525, 1988.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, G.4    Turner, C.5
  • 35
    • 0023931317 scopus 로고
    • A new experimental metastasis model in athymic nude mice, the human malignant melanoma LOX
    • Fodstad, O. Aamdal, S. McMenamin, M. Nesland, J.M. and Pihl, A. A new experimental metastasis model in athymic nude mice, the human malignant melanoma LOX. Int. J. Cancer, 41: 442-449, 1988.
    • (1988) Int. J. Cancer , vol.41 , pp. 442-449
    • Fodstad, O.1    Aamdal, S.2    McMenamin, M.3    Nesland, J.M.4    Pihl, A.5
  • 36
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier, C. Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 256: 1604-1607, 1981.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 37
    • 0015606478 scopus 로고
    • Human cathepsin B1: purification and some properties of the enzyme
    • Barrett, A.J. Human cathepsin B1: purification and some properties of the enzyme. Biochem. J. 131: 809-822, 1973.
    • (1973) Biochem. J. , vol.131 , pp. 809-822
    • Barrett, A.J.1
  • 38
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.), 227: 680-685, 1970.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 39
    • 0023872138 scopus 로고
    • Transmembrane orientation of the fibronectin receptor complex (integrin) demonstrated directly by a combination of immunocytochemical approaches
    • Mueller, S.C. Hasegawa, T. Yamada, S.S. Yamada, K.M. and Chen, W.T. Transmembrane orientation of the fibronectin receptor complex (integrin) demonstrated directly by a combination of immunocytochemical approaches. J. Histochem. Cytochem. 36: 297-306, 1988.
    • (1988) J. Histochem. Cytochem. , vol.36 , pp. 297-306
    • Mueller, S.C.1    Hasegawa, T.2    Yamada, S.S.3    Yamada, K.M.4    Chen, W.T.5
  • 41
    • 0022619989 scopus 로고
    • Invasion of reconstituted basement membrane matrix by metastatic human tumor cells
    • Kramer, R.H. Bensch, K.G. and Wong, J. Invasion of reconstituted basement membrane matrix by metastatic human tumor cells. Cancer Res. 46: 1980-1989, 1986.
    • (1986) Cancer Res. , vol.46 , pp. 1980-1989
    • Kramer, R.H.1    Bensch, K.G.2    Wong, J.3
  • 45
    • 0026027556 scopus 로고
    • Cancer metastasis and angiogenesis: an imbalance of positive and negative regulation
    • Liotta, L.A. Steeg, P.S. and Stetler-Stevenson, W.G. Cancer metastasis and angiogenesis: an imbalance of positive and negative regulation. Cell, 64: 327-336, 1991.
    • (1991) Cell , vol.64 , pp. 327-336
    • Liotta, L.A.1    Steeg, P.S.2    Stetler-Stevenson, W.G.3
  • 47
    • 0027190807 scopus 로고
    • Cellular activation of the 72 kDa type IV procollagenase/TIMP-2 complex
    • Brown, P.D. Kleiner, D.E. Unsworth, E.J. and Stetler-Stevenson, W.G. Cellular activation of the 72 kDa type IV procollagenase/TIMP-2 complex. Kidney Int. 143: 163-170, 1992.
    • (1992) Kidney Int. , vol.143 , pp. 163-170
    • Brown, P.D.1    Kleiner, D.E.2    Unsworth, E.J.3    Stetler-Stevenson, W.G.4
  • 48
    • 0026521973 scopus 로고
    • The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases
    • Murphy, G. Willenbrock, F. Ward, R.V. Cockett, M.I. Eaton, D. and Docherty, A.J.P. The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinases. Biochem. J. 283: 637-641, 1992.
    • (1992) Biochem. J. , vol.283 , pp. 637-641
    • Murphy, G.1    Willenbrock, F.2    Ward, R.V.3    Cockett, M.I.4    Eaton, D.5    Docherty, A.J.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.