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Volumn 1477, Issue 1-2, 2000, Pages 215-230

Cell surface complex of cathepsin B/annexin II tetramer in malignant progression

Author keywords

Annexin II tetramer; Cathepsin B; Extracellular proteolysis; Malignant progression; Proteolytic center; Serine protease

Indexed keywords

CATHEPSIN B; LIPOCORTIN 2; SERINE PROTEINASE;

EID: 0034615565     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00274-5     Document Type: Review
Times cited : (177)

References (147)
  • 1
    • 0021079540 scopus 로고
    • Tumor invasion and the extracellular matrix
    • Liotta L.A., Rao C.N., Barsky S.H. Tumor invasion and the extracellular matrix. Lab. Invest. 49:1983;636-649.
    • (1983) Lab. Invest. , vol.49 , pp. 636-649
    • Liotta, L.A.1    Rao, C.N.2    Barsky, S.H.3
  • 2
    • 0022969477 scopus 로고
    • Tumor invasion through the human amniotic membrane: Requirement for a proteinase cascade
    • Mignatti P., Robbins E., Rifkin D.B. Tumor invasion through the human amniotic membrane: requirement for a proteinase cascade. Cell. 47:1986;487-498.
    • (1986) Cell , vol.47 , pp. 487-498
    • Mignatti, P.1    Robbins, E.2    Rifkin, D.B.3
  • 4
    • 0030806173 scopus 로고    scopus 로고
    • Changing views of the role of matrix metalloproteinases in metastasis
    • Chambers A.F., Matrisian L.M. Changing views of the role of matrix metalloproteinases in metastasis. J. Natl. Cancer Inst. 89:1997;1260-1270.
    • (1997) J. Natl. Cancer Inst. , vol.89 , pp. 1260-1270
    • Chambers, A.F.1    Matrisian, L.M.2
  • 6
    • 0031719897 scopus 로고    scopus 로고
    • Cancer invasion and tissue remodeling: Common themes in proteolytic matrix degradation
    • Johnsen M., Lund L.R., Romer J., Almholt K., Dano K. Cancer invasion and tissue remodeling: common themes in proteolytic matrix degradation. Curr. Opin. Cell. Biol. 10:1998;667-671.
    • (1998) Curr. Opin. Cell. Biol. , vol.10 , pp. 667-671
    • Johnsen, M.1    Lund, L.R.2    Romer, J.3    Almholt, K.4    Dano, K.5
  • 7
    • 0031729186 scopus 로고    scopus 로고
    • The significance of matrix metalloproteinases during early stages of tumor progression
    • Lochter A., Sternlicht M.D., Werb Z., Bissell M.J. The significance of matrix metalloproteinases during early stages of tumor progression. Ann. NY Acad. Sci. 23:1998;180-193.
    • (1998) Ann. NY Acad. Sci. , vol.23 , pp. 180-193
    • Lochter, A.1    Sternlicht, M.D.2    Werb, Z.3    Bissell, M.J.4
  • 8
    • 0031884265 scopus 로고    scopus 로고
    • Cathepsin B and human tumor progression
    • Yan S.-Q., Sameni M., Sloane B.F. Cathepsin B and human tumor progression. Biol. Chem. 379:1998;113-123.
    • (1998) Biol. Chem. , vol.379 , pp. 113-123
    • Yan, S.-Q.1    Sameni, M.2    Sloane, B.F.3
  • 9
    • 0029854071 scopus 로고    scopus 로고
    • Targets for cancer therapy in the cell cycle pathway
    • Rao R.N. Targets for cancer therapy in the cell cycle pathway. Curr. Opin. Oncol. 8:1996;516-524.
    • (1996) Curr. Opin. Oncol. , vol.8 , pp. 516-524
    • Rao, R.N.1
  • 10
    • 0025052018 scopus 로고
    • Cloning and expression of the receptor for human urokinase plasminogen activator, a central molecule in cell surface, plasmin dependent proteolysis
    • Roldan A.L., Cubellis M.V., Masucci M.T., Behrendt N., Lund L.R., Dano K., Appella E., Blasi F. Cloning and expression of the receptor for human urokinase plasminogen activator, a central molecule in cell surface, plasmin dependent proteolysis. EMBO J. 9:1990;467-474.
    • (1990) EMBO J. , vol.9 , pp. 467-474
    • Roldan, A.L.1    Cubellis, M.V.2    Masucci, M.T.3    Behrendt, N.4    Lund, L.R.5    Dano, K.6    Appella, E.7    Blasi, F.8
  • 11
    • 0028023538 scopus 로고
    • An endothelial cell receptor for plasminogen/tissue plasminogen activator. I. Identity with annexin II
    • Hajjar K.A., Jacovina A.T., Chacko J. An endothelial cell receptor for plasminogen/tissue plasminogen activator. I. Identity with annexin II. J. Biol. Chem. 296:1994;21191-21197.
    • (1994) J. Biol. Chem. , vol.296 , pp. 21191-21197
    • Hajjar, K.A.1    Jacovina, A.T.2    Chacko, J.3
  • 12
    • 0029103339 scopus 로고
    • Expression of membrane-type matrix metalloproteinase in human gastric carcinomas
    • Nomura H., Sato H., Seiki M., Mai M., Okada Y. Expression of membrane-type matrix metalloproteinase in human gastric carcinomas. Cancer Res. 55:1995;3263-3266.
    • (1995) Cancer Res. , vol.55 , pp. 3263-3266
    • Nomura, H.1    Sato, H.2    Seiki, M.3    Mai, M.4    Okada, Y.5
  • 13
    • 0031048966 scopus 로고    scopus 로고
    • Proteolytic activation of the precursor of membrane type 1 matrix metalloproteinase by human plasmin. A possible cell surface activator
    • Okumura Y., Sato H., Seiki M., Kido H. Proteolytic activation of the precursor of membrane type 1 matrix metalloproteinase by human plasmin. A possible cell surface activator. FEBS Lett. 402:1997;181-184.
    • (1997) FEBS Lett. , vol.402 , pp. 181-184
    • Okumura, Y.1    Sato, H.2    Seiki, M.3    Kido, H.4
  • 14
    • 0025845425 scopus 로고
    • Cathepsin B efficiently activates the soluble and the tumor cell receptor-bound form of the proenzyme urokinase-type plasminogen activator (pro-uPA)
    • Kobayashi H., Schmitt M., Goretzki L., Chucholowski N., Calvete J., Kramer M., Gunzler W.A., Janicke F., Graeff H. Cathepsin B efficiently activates the soluble and the tumor cell receptor-bound form of the proenzyme urokinase-type plasminogen activator (pro-uPA). J. Biol. Chem. 266:1991;5147-5152.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5147-5152
    • Kobayashi, H.1    Schmitt, M.2    Goretzki, L.3    Chucholowski, N.4    Calvete, J.5    Kramer, M.6    Gunzler, W.A.7    Janicke, F.8    Graeff, H.9
  • 15
    • 0027179188 scopus 로고
    • Effects of membrane-associated cathepsin B on the activation of receptor-bound prourokinase and subsequent invasion of reconstituted basement membranes
    • Kobayashi H., Moniwa N., Sugimura M., Shinohara H., Ohi H., Terao T. Effects of membrane-associated cathepsin B on the activation of receptor-bound prourokinase and subsequent invasion of reconstituted basement membranes. Biochim. Biophys. Acta. 1178:1993;55-62.
    • (1993) Biochim. Biophys. Acta , vol.1178 , pp. 55-62
    • Kobayashi, H.1    Moniwa, N.2    Sugimura, M.3    Shinohara, H.4    Ohi, H.5    Terao, T.6
  • 16
    • 0033152980 scopus 로고    scopus 로고
    • Identification and characterization of human MT5-MMP, a new membrane-bound activator of progelatinase a overexpressed in brain tumors
    • Llano E., Pendas A.M., Freije J.P., Nakano A., Knauper V., Murphy G., Lopez-Otin C. Identification and characterization of human MT5-MMP, a new membrane-bound activator of progelatinase a overexpressed in brain tumors. Cancer Res. 59:1999;2570-2576.
    • (1999) Cancer Res. , vol.59 , pp. 2570-2576
    • Llano, E.1    Pendas, A.M.2    Freije, J.P.3    Nakano, A.4    Knauper, V.5    Murphy, G.6    Lopez-Otin, C.7
  • 21
    • 0025076798 scopus 로고
    • Collagen-binding proteins of mammary epithelial cells are related to Ca2(+)- And phospholipid-binding annexins
    • Wirl G., Schwartz-Albiez R. Collagen-binding proteins of mammary epithelial cells are related to Ca2(+)- and phospholipid-binding annexins. J. Cell. Physiol. 144:1990;511-522.
    • (1990) J. Cell. Physiol. , vol.144 , pp. 511-522
    • Wirl, G.1    Schwartz-Albiez, R.2
  • 22
    • 0028305739 scopus 로고
    • Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C
    • Chung C.Y., Erickson H.P. Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C. J. Cell Biol. 126:1994;539-548.
    • (1994) J. Cell Biol. , vol.126 , pp. 539-548
    • Chung, C.Y.1    Erickson, H.P.2
  • 23
    • 0017822028 scopus 로고
    • Differences in the secretion of the proteinase cathepsin B at the edges of human breast carcinomas and fibroadenomas
    • Poole A.R., Tiltman K.J., Recklies A.D., Stoker T.A.M. Differences in the secretion of the proteinase cathepsin B at the edges of human breast carcinomas and fibroadenomas. Nature. 273:1980;545-547.
    • (1980) Nature , vol.273 , pp. 545-547
    • Poole, A.R.1    Tiltman, K.J.2    Recklies, A.D.3    Stoker, T.A.M.4
  • 24
    • 0018841721 scopus 로고
    • Secretion of proteinases from malignant and nonmalignant human breast tissue
    • Recklies A.D., Tiltman K.J., Stoker T.A.M., Poole A.R. Secretion of proteinases from malignant and nonmalignant human breast tissue. Cancer Res. 40:1980;550-556.
    • (1980) Cancer Res. , vol.40 , pp. 550-556
    • Recklies, A.D.1    Tiltman, K.J.2    Stoker, T.A.M.3    Poole, A.R.4
  • 25
    • 0019806629 scopus 로고
    • A latent thiol proteinase from ascitic fluid of patients with neoplasia
    • Mort J.S., Leduc M., Recklies A. A latent thiol proteinase from ascitic fluid of patients with neoplasia. Biochim. Biophys. Acta. 662:1981;173-180.
    • (1981) Biochim. Biophys. Acta , vol.662 , pp. 173-180
    • Mort, J.S.1    Leduc, M.2    Recklies, A.3
  • 26
    • 0020441726 scopus 로고
    • A cysteine proteinase secreted from human breast tumors is immunologically related to cathepsin B
    • Recklies A.D., Poole A.R., Mort J.S. A cysteine proteinase secreted from human breast tumors is immunologically related to cathepsin B. Biochem. J. 207:1982;633-636.
    • (1982) Biochem. J. , vol.207 , pp. 633-636
    • Recklies, A.D.1    Poole, A.R.2    Mort, J.S.3
  • 27
    • 0019797924 scopus 로고
    • Lysosomal cathepsin B: Correlation with metastatic potential
    • Sloane B.F., Dunn J.R., Honn K.V. Lysosomal cathepsin B: correlation with metastatic potential. Science. 212:1981;1151-1153.
    • (1981) Science , vol.212 , pp. 1151-1153
    • Sloane, B.F.1    Dunn, J.R.2    Honn, K.V.3
  • 28
  • 29
    • 0025863290 scopus 로고
    • Stage-specific increases in cathepsin B messenger RNA content in human colorectal carcinoma
    • Murnane M.J., Sheahan K., Ozdemirli M., Shuja S. Stage-specific increases in cathepsin B messenger RNA content in human colorectal carcinoma. Cancer Res. 51:1991;1137-1142.
    • (1991) Cancer Res. , vol.51 , pp. 1137-1142
    • Murnane, M.J.1    Sheahan, K.2    Ozdemirli, M.3    Shuja, S.4
  • 32
    • 0028145293 scopus 로고
    • Cathepsin B expression in colorectal carcinomas correlates with tumor progression and shortened patient survival
    • Campo E., Munoz J., Miquel R., Palacin A., Cardesa A., Sloane B.F., Emmert-Buck M. Cathepsin B expression in colorectal carcinomas correlates with tumor progression and shortened patient survival. Am. J. Pathol. 145:1994;301-309.
    • (1994) Am. J. Pathol. , vol.145 , pp. 301-309
    • Campo, E.1    Munoz, J.2    Miquel, R.3    Palacin, A.4    Cardesa, A.5    Sloane, B.F.6    Emmert-Buck, M.7
  • 33
    • 0029097797 scopus 로고
    • Immunolocalization of cathepsin B in human glioma: Implications for tumor invasion, angiogenesis
    • Mikkelsen T., Yan P.S., Ho K.L., Sameni M., Sloane B.F., Rosenblum M.L. Immunolocalization of cathepsin B in human glioma: implications for tumor invasion, angiogenesis. J. Neurosurg. 83:1995;285-290.
    • (1995) J. Neurosurg. , vol.83 , pp. 285-290
    • Mikkelsen, T.1    Yan, P.S.2    Ho, K.L.3    Sameni, M.4    Sloane, B.F.5    Rosenblum, M.L.6
  • 37
    • 0030200892 scopus 로고    scopus 로고
    • Physical mapping of chromosome 8p22 markers and their homozygous deletion in a metastatic prostate cancer
    • Bova G.S., MacGrogan D., Levy A., Pin S.S., Bookstein R., Isaacs W.B. Physical mapping of chromosome 8p22 markers and their homozygous deletion in a metastatic prostate cancer. Genomics. 35:1996;46-54.
    • (1996) Genomics , vol.35 , pp. 46-54
    • Bova, G.S.1    MacGrogan, D.2    Levy, A.3    Pin, S.S.4    Bookstein, R.5    Isaacs, W.B.6
  • 39
    • 0027531160 scopus 로고
    • Localization of a biotinylated cathepsin B oligonucleotide probe in human prostate including invasive cells and invasive edges by in situ hybridization
    • Sinha A.A., Gleason D.F., DeLeon O.F., Wilson M.J., Sloane B.F. Localization of a biotinylated cathepsin B oligonucleotide probe in human prostate including invasive cells and invasive edges by in situ hybridization. Anat. Rec. 235:1993;233-240.
    • (1993) Anat. Rec. , vol.235 , pp. 233-240
    • Sinha, A.A.1    Gleason, D.F.2    Deleon, O.F.3    Wilson, M.J.4    Sloane, B.F.5
  • 41
    • 84973703216 scopus 로고
    • Clinicopathologic significance of cathepsin B and urokinase-type plasminogen activator immunostaining in colorectal adenocarcinoma
    • Visscher D.W., Sloane B., Sakr W., Sameni M., Weaver D., Bouwman D., Crissman J.D. Clinicopathologic significance of cathepsin B and urokinase-type plasminogen activator immunostaining in colorectal adenocarcinoma. Int. J. Surg. Pathol. 1:1994;227-234.
    • (1994) Int. J. Surg. Pathol. , vol.1 , pp. 227-234
    • Visscher, D.W.1    Sloane, B.2    Sakr, W.3    Sameni, M.4    Weaver, D.5    Bouwman, D.6    Crissman, J.D.7
  • 43
    • 0003126050 scopus 로고    scopus 로고
    • Molecular regulation, membrane association and secretion of tumor cathepsin B
    • Frosch B.A., Berquin I., Emmert-Buck M.R., Moin K., Sloane B.F. Molecular regulation, membrane association and secretion of tumor cathepsin B. APMIS. 107:1999;28-37.
    • (1999) APMIS , vol.107 , pp. 28-37
    • Frosch, B.A.1    Berquin, I.2    Emmert-Buck, M.R.3    Moin, K.4    Sloane, B.F.5
  • 45
    • 0024599360 scopus 로고
    • Immunodetection of cathepsins B and L present in and secreted from human pre-malignant and malignant colorectal tumour cell lines
    • Maciewicz R.A., Wardale R.J., Etherington D.J., Paraskeva C. Immunodetection of cathepsins B and L present in and secreted from human pre-malignant and malignant colorectal tumour cell lines. Int. J. Cancer. 43:1989;478-486.
    • (1989) Int. J. Cancer , vol.43 , pp. 478-486
    • Maciewicz, R.A.1    Wardale, R.J.2    Etherington, D.J.3    Paraskeva, C.4
  • 46
    • 0024615085 scopus 로고
    • The secretion of high molecular weight cathepsin B from cultured human liver cancers
    • Ohsawa T., Higashi T., Tsuji T. The secretion of high molecular weight cathepsin B from cultured human liver cancers. Acta Med. Okayama. 43:1989;9-15.
    • (1989) Acta Med. Okayama , vol.43 , pp. 9-15
    • Ohsawa, T.1    Higashi, T.2    Tsuji, T.3
  • 47
    • 0023890834 scopus 로고
    • Biosynthesis of lysosomal cathepsins B and H in cultured rat hepatocytes
    • Nishimura Y., Amano J., Sato H., Tsuji H., Kato K. Biosynthesis of lysosomal cathepsins B and H in cultured rat hepatocytes. Arch. Biochem. Biophys. 262:1988;159-170.
    • (1988) Arch. Biochem. Biophys. , vol.262 , pp. 159-170
    • Nishimura, Y.1    Amano, J.2    Sato, H.3    Tsuji, H.4    Kato, K.5
  • 48
    • 0028618307 scopus 로고
    • Pericellular pH affects distribution and secretion of cathepsin B in malignant cells
    • Rozhin J., Sameni M., Ziegler G., Sloane B.F. Pericellular pH affects distribution and secretion of cathepsin B in malignant cells. Cancer Res. 54:1994;6517-6525.
    • (1994) Cancer Res. , vol.54 , pp. 6517-6525
    • Rozhin, J.1    Sameni, M.2    Ziegler, G.3    Sloane, B.F.4
  • 49
    • 0027931667 scopus 로고
    • A lipoxygenase metabolite, 12-(S)-HETE, stimulates protein kinase C-mediated release of cathepsin B from malignant cells
    • Honn K.V., Timar J., Rozhin J., Bazaz R., Sameni M., Ziegler G., Sloane B.F. A lipoxygenase metabolite, 12-(S)-HETE, stimulates protein kinase C-mediated release of cathepsin B from malignant cells. Exp. Cell Res. 214:1994;120-130.
    • (1994) Exp. Cell Res. , vol.214 , pp. 120-130
    • Honn, K.V.1    Timar, J.2    Rozhin, J.3    Bazaz, R.4    Sameni, M.5    Ziegler, G.6    Sloane, B.F.7
  • 50
    • 0028273525 scopus 로고
    • Membrane association of cathepsin B can be induced by transfection of human breast epithelial cells with c-Ha-ras oncogene
    • Sloane B.F., Moin K., Sameni M., Tait L.R., Rozhin J., Ziegler G. Membrane association of cathepsin B can be induced by transfection of human breast epithelial cells with c-Ha-ras oncogene. J. Cell Sci. 107:1994;373-384.
    • (1994) J. Cell Sci. , vol.107 , pp. 373-384
    • Sloane, B.F.1    Moin, K.2    Sameni, M.3    Tait, L.R.4    Rozhin, J.5    Ziegler, G.6
  • 51
    • 0030007677 scopus 로고    scopus 로고
    • Marked increases in cathepsin B and L activities distinguish papillary carcinoma of the thyroid from normal thyroid or thyroid with non-neoplastic disease
    • Shuja S., Murnane M.J. Marked increases in cathepsin B and L activities distinguish papillary carcinoma of the thyroid from normal thyroid or thyroid with non-neoplastic disease. Int. J. Cancer. 16:1996;420-426.
    • (1996) Int. J. Cancer , vol.16 , pp. 420-426
    • Shuja, S.1    Murnane, M.J.2
  • 52
    • 0027946430 scopus 로고
    • Cathepsin B, a cysteine protease implicated in metastatic progression, is also expressed during regression of the rat prostate and mammary glands
    • Guenette R.S., Mooibroek M., Wong K., Wong P., Tenniswood M. Cathepsin B, a cysteine protease implicated in metastatic progression, is also expressed during regression of the rat prostate and mammary glands. Eur. J. Biochem. 226:1994;311-321.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 311-321
    • Guenette, R.S.1    Mooibroek, M.2    Wong, K.3    Wong, P.4    Tenniswood, M.5
  • 53
    • 0026575258 scopus 로고
    • Degradation of extracellular-matrix proteins by human cathepsin B from normal and tumor tissues
    • Emmert-Buck M.R., Karustis D.G., Day N.A., Honn K.V., Sloane B.F. Degradation of extracellular-matrix proteins by human cathepsin B from normal and tumor tissues. Biochem. J. 282:1992;273-278.
    • (1992) Biochem. J. , vol.282 , pp. 273-278
    • Emmert-Buck, M.R.1    Karustis, D.G.2    Day, N.A.3    Honn, K.V.4    Sloane, B.F.5
  • 55
    • 0029759530 scopus 로고    scopus 로고
    • Proteolysis regulates exposure of the IIICS-1 adhesive sequence in plasma fibronectin
    • Ugarova T.P., Ljubimov A.V., Deng L., Plow E.F. Proteolysis regulates exposure of the IIICS-1 adhesive sequence in plasma fibronectin. Biochemistry. 35:1996;10913-10921.
    • (1996) Biochemistry , vol.35 , pp. 10913-10921
    • Ugarova, T.P.1    Ljubimov, A.V.2    Deng, L.3    Plow, E.F.4
  • 56
    • 0017644625 scopus 로고
    • Further studies on the activation of procollagenase, the latent precursor of bone collagenase
    • Eeckhout Y., Vaes G. Further studies on the activation of procollagenase, the latent precursor of bone collagenase. Biochem. J. 166:1977;21-31.
    • (1977) Biochem. J. , vol.166 , pp. 21-31
    • Eeckhout, Y.1    Vaes, G.2
  • 57
    • 0031882595 scopus 로고    scopus 로고
    • Cathepsin B expression and its correlation with tumor-associated laminin and tumor progression in gastric cancer
    • Khan A., Krishna M., Baker S.P., Malhothra R., Banner B.F. Cathepsin B expression and its correlation with tumor-associated laminin and tumor progression in gastric cancer. Arch. Pathol. Lab. Med. 122:1998;172-177.
    • (1998) Arch. Pathol. Lab. Med. , vol.122 , pp. 172-177
    • Khan, A.1    Krishna, M.2    Baker, S.P.3    Malhothra, R.4    Banner, B.F.5
  • 58
    • 0000412776 scopus 로고
    • The prognostic implications of the cathepsin B expression in pulmonary adenocarcinomas
    • Higashiyama M., Doi O., Kodama K., Yokouchi H., Tateishi R. The prognostic implications of the cathepsin B expression in pulmonary adenocarcinomas. Jpn. J. Cancer Clin. 37:1991;1151-1157.
    • (1991) Jpn. J. Cancer Clin. , vol.37 , pp. 1151-1157
    • Higashiyama, M.1    Doi, O.2    Kodama, K.3    Yokouchi, H.4    Tateishi, R.5
  • 59
    • 0028304720 scopus 로고
    • Immunohistochemical study of cathepsin B. Prognostic significance in human lung cancer
    • Sukoh N., Abe S., Ogura S., Isobe H., Takekawa H., Inoue K., Kawakami Y. Immunohistochemical study of cathepsin B. Prognostic significance in human lung cancer. Cancer. 74:1994;46-51.
    • (1994) Cancer , vol.74 , pp. 46-51
    • Sukoh, N.1    Abe, S.2    Ogura, S.3    Isobe, H.4    Takekawa, H.5    Inoue, K.6    Kawakami, Y.7
  • 60
    • 0027463459 scopus 로고
    • Cathepsin B expression in tumour cells and laminin distribution in pulmonary adenocarcinoma
    • Higashiyama M., Doi O., Kodama K., Yokouchi H., Tateishi R. Cathepsin B expression in tumour cells and laminin distribution in pulmonary adenocarcinoma. J. Clin. Pathol. 46:1993;18-22.
    • (1993) J. Clin. Pathol. , vol.46 , pp. 18-22
    • Higashiyama, M.1    Doi, O.2    Kodama, K.3    Yokouchi, H.4    Tateishi, R.5
  • 61
    • 0342960649 scopus 로고    scopus 로고
    • Cathepsin B and tumor-associated laminin expression in the progression of colorectal adenoma to carcinoma
    • Khan A., Kirshna M., Baker S.P., Malhothra R., Banner B.F. Cathepsin B and tumor-associated laminin expression in the progression of colorectal adenoma to carcinoma. Mod. Pathol. 46:1998;18-22.
    • (1998) Mod. Pathol. , vol.46 , pp. 18-22
    • Khan, A.1    Kirshna, M.2    Baker, S.P.3    Malhothra, R.4    Banner, B.F.5
  • 62
    • 0030177259 scopus 로고    scopus 로고
    • Suicidal tumor proteases
    • Sloane B.F. Suicidal tumor proteases. Nature Biotechnol. 14:1996;826-827.
    • (1996) Nature Biotechnol. , vol.14 , pp. 826-827
    • Sloane, B.F.1
  • 65
    • 0033567263 scopus 로고    scopus 로고
    • Exocytosis of active cathepsin B: Enzyme activity at pH 7.0, inhibition and molecular mass
    • Linebaugh B.E., Sameni M., Day N.A., Sloane B.F., Keppler D. Exocytosis of active cathepsin B: enzyme activity at pH 7.0, inhibition and molecular mass. Eur. J. Biochem. 264:1999;100-109.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 100-109
    • Linebaugh, B.E.1    Sameni, M.2    Day, N.A.3    Sloane, B.F.4    Keppler, D.5
  • 66
    • 0030775075 scopus 로고    scopus 로고
    • Annexin gene structures and molecular evolutionary genetics
    • Morgan O.R., Fernandez M.P. Annexin gene structures and molecular evolutionary genetics. Cell. Mol. Life Sci. 53:1997;508-511.
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 508-511
    • Morgan, O.R.1    Fernandez, M.P.2
  • 67
    • 0028844290 scopus 로고
    • Annexin II tetramer: Structure and function
    • Waisman D.M. Annexin II tetramer: structure and function. Mol. Cell. Biochem. 149/150:1995;301-322.
    • (1995) Mol. Cell. Biochem. , vol.149-150 , pp. 301-322
    • Waisman, D.M.1
  • 68
    • 0031157808 scopus 로고    scopus 로고
    • Annexins: What are they good for?
    • Mollenhauer J. Annexins: what are they good for? Cell. Mol. Life Sci. 53:1997;506-507.
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 506-507
    • Mollenhauer, J.1
  • 70
    • 0028324464 scopus 로고
    • Annexins: The problem of assessing the biological role for a gene family of multifunctional calcium- And phospholipid-binding proteins
    • Raynal P., Pollard H.B. Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins. Biochim. Biophys. Acta. 1197:1994;63-93.
    • (1994) Biochim. Biophys. Acta , vol.1197 , pp. 63-93
    • Raynal, P.1    Pollard, H.B.2
  • 71
    • 0025855150 scopus 로고
    • The protein-tyrosine kinase substrate, calpactin I heavy chain (p36), is part of the primer recognition protein complex that interacts with DNA polymerase alpha
    • Jindal H.K., Chaney W.G., Anderson C.W., Davis R.G., Vishwanatha J.K. The protein-tyrosine kinase substrate, calpactin I heavy chain (p36), is part of the primer recognition protein complex that interacts with DNA polymerase alpha. J. Biol. Chem. 266:1991;5169-5176.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5169-5176
    • Jindal, H.K.1    Chaney, W.G.2    Anderson, C.W.3    Davis, R.G.4    Vishwanatha, J.K.5
  • 72
    • 0021299594 scopus 로고
    • Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders; Calcium-dependent binding to non-erythroid spectrin and F-actin
    • Weber K., Gerke V. Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders; calcium-dependent binding to non-erythroid spectrin and F-actin. EMBO J. 3:1984;227-233.
    • (1984) EMBO J. , vol.3 , pp. 227-233
    • Weber, K.1    Gerke, V.2
  • 73
    • 0021306419 scopus 로고
    • Biochemical characterization of a 34-kilodalton normal cellular substrate of pp60v-src and an associated 6-kilodalton protein
    • Erikson E., Tomasiewicz H.G., Erikson R.L. Biochemical characterization of a 34-kilodalton normal cellular substrate of pp60v-src and an associated 6-kilodalton protein. Mol. Cell Biol. 4:1984;77-85.
    • (1984) Mol. Cell Biol. , vol.4 , pp. 77-85
    • Erikson, E.1    Tomasiewicz, H.G.2    Erikson, R.L.3
  • 74
    • 0011972017 scopus 로고
    • Two related but distinct forms of the Mr 36,000 tyrosine kinase substrate (calpactin) that interact with phospholipid and actin in a Ca2+-dependent manner
    • Glenney J. Two related but distinct forms of the Mr 36,000 tyrosine kinase substrate (calpactin) that interact with phospholipid and actin in a Ca2+-dependent manner. Proc. Natl. Acad. Sci. USA. 83:1986;4258-4262.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4258-4262
    • Glenney, J.1
  • 75
    • 0022996716 scopus 로고
    • Association of the S-100-related calpactin I light chain with the NH2-terminal tail of the 36-kDa heavy chain
    • Glenny J.R., Woodgett J.R., Isacke C.M., Hunter T. Association of the S-100-related calpactin I light chain with the NH2-terminal tail of the 36-kDa heavy chain. J. Biol. Chem. 261:1986;10485-10488.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10485-10488
    • Glenny, J.R.1    Woodgett, J.R.2    Isacke, C.M.3    Hunter, T.4
  • 76
    • 0024062670 scopus 로고
    • P36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 regulatory subunit via a short amino-terminal amphiphatic helix
    • Johnsson N., Marriott G., Weber K. p36, the major cytoplasmic substrate of src tyrosine protein kinase, binds to its p11 regulatory subunit via a short amino-terminal amphiphatic helix. EMBO J. 7:1988;2435-2442.
    • (1988) EMBO J. , vol.7 , pp. 2435-2442
    • Johnsson, N.1    Marriott, G.2    Weber, K.3
  • 77
    • 0022491787 scopus 로고
    • Binding sites for calcium, lipid and p11 on p36, the substrate of retroviral tyrosine-specific protein kinases
    • Johnson N., Vandekerckhove J., Van-Damme J., Weber K. Binding sites for calcium, lipid and p11 on p36, the substrate of retroviral tyrosine-specific protein kinases. FEBS Lett. 198:1986;361-364.
    • (1986) FEBS Lett. , vol.198 , pp. 361-364
    • Johnson, N.1    Vandekerckhove, J.2    Van-Damme, J.3    Weber, K.4
  • 79
    • 0024280336 scopus 로고
    • Calpactin in exocytosis
    • Burgoyne R.D. Calpactin in exocytosis. Nature. 331:1988;20.
    • (1988) Nature , vol.331 , pp. 20
    • Burgoyne, R.D.1
  • 80
    • 0027158668 scopus 로고
    • Annexin II is a major component of fusogenic endosomal vesicles
    • Gruenberg J., Emans N. Annexin II is a major component of fusogenic endosomal vesicles. Trends Cell Biol. 3:1993;224-227.
    • (1993) Trends Cell Biol. , vol.3 , pp. 224-227
    • Gruenberg, J.1    Emans, N.2
  • 81
    • 0025109633 scopus 로고
    • CDNA structure and expression of calpactin, a peptide involved in Ca2(+)-dependent cell aggregation in sponges
    • Robitzki A., Schroder H.C., Ugarkovic D., Gramzow M., Fritsche U., Batel R., Muller W.E. cDNA structure and expression of calpactin, a peptide involved in Ca2(+)-dependent cell aggregation in sponges. Biochem. J. 271:1990;415-420.
    • (1990) Biochem. J. , vol.271 , pp. 415-420
    • Robitzki, A.1    Schroder, H.C.2    Ugarkovic, D.3    Gramzow, M.4    Fritsche, U.5    Batel, R.6    Muller, W.E.7
  • 82
    • 0029669991 scopus 로고    scopus 로고
    • The S100 family of EF-hand calcium-binding proteins: Functions and pathology
    • Schafer B.W., Heizmann C.W. The S100 family of EF-hand calcium-binding proteins: functions and pathology. Trends Biochem. Sci. 21:1996;134-140.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 134-140
    • Schafer, B.W.1    Heizmann, C.W.2
  • 83
    • 0022157945 scopus 로고
    • The regulatory chain in the p36-kd substrate complex of viral tyrosine-specific protein kinases is related in sequence to the S-100 protein of glial cells
    • Weber K., Gerke V. The regulatory chain in the p36-kd substrate complex of viral tyrosine-specific protein kinases is related in sequence to the S-100 protein of glial cells. EMBO J. 4:1985;2917-2920.
    • (1985) EMBO J. , vol.4 , pp. 2917-2920
    • Weber, K.1    Gerke, V.2
  • 84
    • 0026799425 scopus 로고
    • A calcyclin-associated protein is a newly identified member of the Ca2+/phospholipid-binding proteins, annexin family
    • Tokumitsu H., Mizutani A., Minami H., Kobayashi R., Hidaka H. A calcyclin-associated protein is a newly identified member of the Ca2+/phospholipid-binding proteins, annexin family. J. Biol. Chem. 267:1992;8919-8924.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8919-8924
    • Tokumitsu, H.1    Mizutani, A.2    Minami, H.3    Kobayashi, R.4    Hidaka, H.5
  • 85
    • 0030052283 scopus 로고    scopus 로고
    • Calcium-dependent binding of S100C to the N-terminal domain of annexin I
    • Mailliard W.S., Haigler H.T., Schlaepfer D.D. Calcium-dependent binding of S100C to the N-terminal domain of annexin I. J. Biol. Chem. 271:1996;719-725.
    • (1996) J. Biol. Chem. , vol.271 , pp. 719-725
    • Mailliard, W.S.1    Haigler, H.T.2    Schlaepfer, D.D.3
  • 86
    • 0029786326 scopus 로고    scopus 로고
    • The association of annexin I with early endosomes is regulated by Ca2+ and requires an intact N-terminal domain
    • Seemann J., Weber K., Osborn M., Pardon R.G., Gerke V. The association of annexin I with early endosomes is regulated by Ca2+ and requires an intact N-terminal domain. Mol. Biol. Cell. 7:1996;1359-1374.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1359-1374
    • Seemann, J.1    Weber, K.2    Osborn, M.3    Pardon, R.G.4    Gerke, V.5
  • 88
    • 0027203055 scopus 로고
    • Six S100 genes are clustered on human chromosome 1q21: Identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E
    • Engelkamp D., Schafer B.W., Mattei M.G., Erne P., Heizmann C.W. Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E. Proc. Natl. Acad. Sci. USA. 9:1993;6547-6551.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.9 , pp. 6547-6551
    • Engelkamp, D.1    Schafer, B.W.2    Mattei, M.G.3    Erne, P.4    Heizmann, C.W.5
  • 89
    • 0027369284 scopus 로고
    • S-100 protein remains a practical marker for melanocytic and other tumours
    • Cochran A.J., Lu H.F., Li P.X., Saxton R., Wen D.R. S-100 protein remains a practical marker for melanocytic and other tumours. Melanoma Res. 3:1993;325-330.
    • (1993) Melanoma Res. , vol.3 , pp. 325-330
    • Cochran, A.J.1    Lu, H.F.2    Li, P.X.3    Saxton, R.4    Wen, D.R.5
  • 90
    • 0027479439 scopus 로고
    • Induction of the metastatic phenotype by transfection of a benign rat mammary epithelial cell line with the gene for p9Ka, a rat calcium-binding protein, but not with the oncogene EJ-ras-1
    • Davies B.R., Davies M.P., Gibbs F.E., Barraclough R., Rudland P.S. Induction of the metastatic phenotype by transfection of a benign rat mammary epithelial cell line with the gene for p9Ka, a rat calcium-binding protein, but not with the oncogene EJ-ras-1. Oncogene. 8:1993;999-1008.
    • (1993) Oncogene , vol.8 , pp. 999-1008
    • Davies, B.R.1    Davies, M.P.2    Gibbs, F.E.3    Barraclough, R.4    Rudland, P.S.5
  • 91
    • 0025220692 scopus 로고
    • The growth-regulated gene 1B6 is identified as the heavy chain of calpactin I
    • Keutzer J.C., Hirschhorn R.R. The growth-regulated gene 1B6 is identified as the heavy chain of calpactin I. Exp. Cell Res. 188:1990;153-159.
    • (1990) Exp. Cell Res. , vol.188 , pp. 153-159
    • Keutzer, J.C.1    Hirschhorn, R.R.2
  • 92
    • 0029585757 scopus 로고
    • Cloning of putative growth regulatory genes from primary human keratinocytes by subtractive hybridization
    • Vellucci V.F., Germino F.J., Reiss M. Cloning of putative growth regulatory genes from primary human keratinocytes by subtractive hybridization. Gene. 166:1995;213-220.
    • (1995) Gene , vol.166 , pp. 213-220
    • Vellucci, V.F.1    Germino, F.J.2    Reiss, M.3
  • 93
    • 0027133635 scopus 로고
    • Annexin II expression is regulated during mammalian cell cycle
    • Chiang Y., Schneiderman M.H., Vishwanatha J.K. Annexin II expression is regulated during mammalian cell cycle. Cancer Res. 53:1993;6017-6021.
    • (1993) Cancer Res. , vol.53 , pp. 6017-6021
    • Chiang, Y.1    Schneiderman, M.H.2    Vishwanatha, J.K.3
  • 94
    • 0027140743 scopus 로고
    • Enhanced expression of annexin II in human pancreatic carcinoma cells and primary pancreatic cancers
    • Vishwanatha J.K., Chiang Y., Kumble K.D., Hollingsworth M.A., Pour P.M. Enhanced expression of annexin II in human pancreatic carcinoma cells and primary pancreatic cancers. Carcinogenesis. 14:1993;2575-2579.
    • (1993) Carcinogenesis , vol.14 , pp. 2575-2579
    • Vishwanatha, J.K.1    Chiang, Y.2    Kumble, K.D.3    Hollingsworth, M.A.4    Pour, P.M.5
  • 95
    • 0026587708 scopus 로고
    • Enhanced levels of annexins in pancreatic carcinoma cells of Syrian hamsters and their intrapancreatic allografts
    • Kumble K.D., Hirota M., Pour P.M., Vishwanatha J.K. Enhanced levels of annexins in pancreatic carcinoma cells of Syrian hamsters and their intrapancreatic allografts. Cancer Res. 52:1992;163-167.
    • (1992) Cancer Res. , vol.52 , pp. 163-167
    • Kumble, K.D.1    Hirota, M.2    Pour, P.M.3    Vishwanatha, J.K.4
  • 96
    • 0026513632 scopus 로고
    • Elevated expression of annexin II (lipocortin II, p36) in a multidrug resistant small cell lung cancer cell line
    • Cole S.P., Pinkoski M.J., Bhardwaj G., Deeley R.G. Elevated expression of annexin II (lipocortin II, p36) in a multidrug resistant small cell lung cancer cell line. Br. J. Cancer. 65:1992;498-502.
    • (1992) Br. J. Cancer , vol.65 , pp. 498-502
    • Cole, S.P.1    Pinkoski, M.J.2    Bhardwaj, G.3    Deeley, R.G.4
  • 97
    • 0027092615 scopus 로고
    • Developmental regulation of annexin II (lipocortin 2) in human brain and expression in high grade glioma
    • Reeves S.A., Chavez-Kappel C., Davis R., Rosenblum M., Isreal M.A. Developmental regulation of annexin II (lipocortin 2) in human brain and expression in high grade glioma. Cancer Res. 52:1992;6871-6876.
    • (1992) Cancer Res. , vol.52 , pp. 6871-6876
    • Reeves, S.A.1    Chavez-Kappel, C.2    Davis, R.3    Rosenblum, M.4    Isreal, M.A.5
  • 98
    • 0028633553 scopus 로고
    • Annexin II marks astrocytic brain tumors of high histologic grade
    • Roseman B.J., Bollen A., Hsu J., Lamborn K., Isreal M.A. Annexin II marks astrocytic brain tumors of high histologic grade. Oncol. Res. 6:1994;561-567.
    • (1994) Oncol. Res. , vol.6 , pp. 561-567
    • Roseman, B.J.1    Bollen, A.2    Hsu, J.3    Lamborn, K.4    Isreal, M.A.5
  • 99
    • 0030580097 scopus 로고    scopus 로고
    • Altered expression of annexin II in human B-cell lymphoma cell lines
    • Chiang Y., Davis R.G., Vishwanatha J.K. Altered expression of annexin II in human B-cell lymphoma cell lines. Biochim. Biophys. Acta. 1313:1996;295-301.
    • (1996) Biochim. Biophys. Acta , vol.1313 , pp. 295-301
    • Chiang, Y.1    Davis, R.G.2    Vishwanatha, J.K.3
  • 100
    • 0025358852 scopus 로고
    • Enhanced expression of the protein kinase substrate p36 in human hepatocellular carcinoma
    • Frohlich M., Motte P., Galvin K., Takahashi H., Wands J., Ozturk M. Enhanced expression of the protein kinase substrate p36 in human hepatocellular carcinoma. Mol. Cell. Biol. 10:1990;3216-3223.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 3216-3223
    • Frohlich, M.1    Motte, P.2    Galvin, K.3    Takahashi, H.4    Wands, J.5    Ozturk, M.6
  • 101
    • 0027167655 scopus 로고
    • Formation of the annexin II2p112 complex upon differentiation of F9 teratocarcinoma cells
    • Harder T., Thiel C., Gerke V. Formation of the annexin II2p112 complex upon differentiation of F9 teratocarcinoma cells. J. Cell Sci. 104:1993;1109-1117.
    • (1993) J. Cell Sci. , vol.104 , pp. 1109-1117
    • Harder, T.1    Thiel, C.2    Gerke, V.3
  • 102
    • 0025744090 scopus 로고
    • Increases in p11 and annexin II proteins correlate with differentiation in the PC12 pheochromocytoma
    • Fox M.T., Prentice D.A., Hughes J.P. Increases in p11 and annexin II proteins correlate with differentiation in the PC12 pheochromocytoma. Biochem. Biophys. Res. Commun. 177:1991;1188-1193.
    • (1991) Biochem. Biophys. Res. Commun. , vol.177 , pp. 1188-1193
    • Fox, M.T.1    Prentice, D.A.2    Hughes, J.P.3
  • 103
    • 9844242902 scopus 로고    scopus 로고
    • Inhibition of phytohaemagglutinin-induced lymphoproliferation by soluble annexin II in sera from patients with renal cell carcinoma
    • Aarli A., Skeie J.T., Kristoffersen E.K., Bakke A., Ulvestad E. Inhibition of phytohaemagglutinin-induced lymphoproliferation by soluble annexin II in sera from patients with renal cell carcinoma. APMIS. 105:1997;699-704.
    • (1997) APMIS , vol.105 , pp. 699-704
    • Aarli, A.1    Skeie, J.T.2    Kristoffersen, E.K.3    Bakke, A.4    Ulvestad, E.5
  • 104
    • 0030802482 scopus 로고    scopus 로고
    • Isolation of novel HLA-DR restricted potential tumor-associated antigens from the melanoma cell line FM3
    • Halder T., Pawelec G., Kirkin A.F., Zeuthen J., Meyer H.E., Kun L., Kalbacher H. Isolation of novel HLA-DR restricted potential tumor-associated antigens from the melanoma cell line FM3. Cancer Res. 57:1997;3238-3244.
    • (1997) Cancer Res. , vol.57 , pp. 3238-3244
    • Halder, T.1    Pawelec, G.2    Kirkin, A.F.3    Zeuthen, J.4    Meyer, H.E.5    Kun, L.6    Kalbacher, H.7
  • 105
    • 0031690656 scopus 로고    scopus 로고
    • Tumour-specific MHC-class-II-restricted responses after in vitro sensitization to synthetic peptides corresponding to gp100 and annexin II eluted from melanoma cells
    • Li K., Adibzadeh M., Halder T., Kalbacher H., Heinzel S., Muller C.Zeuthen,J., Pawelec G. Tumour-specific MHC-class-II-restricted responses after in vitro sensitization to synthetic peptides corresponding to gp100 and annexin II eluted from melanoma cells. Cancer Immunol. Immunother. 47:1998;32-38.
    • (1998) Cancer Immunol. Immunother. , vol.47 , pp. 32-38
    • Li, K.1    Adibzadeh, M.2    Halder, T.3    Kalbacher, H.4    Heinzel, S.5    Muller C.zeuthen, J.6    Pawelec, G.7
  • 106
    • 0027462446 scopus 로고
    • Expression of annexins on the surfaces of non-metastatic and metastatic human and rodent tumor cells
    • Yeatman T.J., Updyke T.V., Kaetzel M.A., Dedman J.R., Nicolson G.L. Expression of annexins on the surfaces of non-metastatic and metastatic human and rodent tumor cells. Clin. Exp. Metastasis. 11:1993;37-44.
    • (1993) Clin. Exp. Metastasis , vol.11 , pp. 37-44
    • Yeatman, T.J.1    Updyke, T.V.2    Kaetzel, M.A.3    Dedman, J.R.4    Nicolson, G.L.5
  • 107
    • 0023770128 scopus 로고
    • Cancer metastasis: Tumor cell and host organ properties important in metastasis to specific secondary sites
    • Nicolson G.L. Cancer metastasis: tumor cell and host organ properties important in metastasis to specific secondary sites. Biochim. Biophys. Acta. 948:1988;175-224.
    • (1988) Biochim. Biophys. Acta , vol.948 , pp. 175-224
    • Nicolson, G.L.1
  • 108
    • 0026177265 scopus 로고
    • Tumor and host molecules important in the organ preference of metastsis
    • Nicolson G.L. Tumor and host molecules important in the organ preference of metastsis. Semin. Cancer Biol. 2:1991;143-154.
    • (1991) Semin. Cancer Biol. , vol.2 , pp. 143-154
    • Nicolson, G.L.1
  • 109
    • 0027436971 scopus 로고
    • Extracellular annexin II is associated with divalent cation-dependent tumor cell-endothelial cell adhesion of metastatic RAW117 large-cell lymphoma cells
    • Tressler R.J., Updyke T.V., Yeatman T., Nicolson G.L. Extracellular annexin II is associated with divalent cation-dependent tumor cell-endothelial cell adhesion of metastatic RAW117 large-cell lymphoma cells. J. Cell. Biochem. 53:1993;265-276.
    • (1993) J. Cell. Biochem. , vol.53 , pp. 265-276
    • Tressler, R.J.1    Updyke, T.V.2    Yeatman, T.3    Nicolson, G.L.4
  • 110
    • 0026086635 scopus 로고
    • Release of basic fibroblast growth factor, an angiogenic factor devoid of secretory signal sequence: A trivial phenomenon or a novel secretion mechanism?
    • Mignatti P., Rifkin D.B. Release of basic fibroblast growth factor, an angiogenic factor devoid of secretory signal sequence: a trivial phenomenon or a novel secretion mechanism? J. Cell. Biochem. 47:1991;201-207.
    • (1991) J. Cell. Biochem. , vol.47 , pp. 201-207
    • Mignatti, P.1    Rifkin, D.B.2
  • 113
    • 0024441046 scopus 로고
    • Tenascin: An extracellular matrix protein prominent in specialized embryonic tissues and tumors
    • Erickson H.P., Bourdon M.A. Tenascin: an extracellular matrix protein prominent in specialized embryonic tissues and tumors. Annu. Rev. Cell Biol. 5:1989;71-92.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 71-92
    • Erickson, H.P.1    Bourdon, M.A.2
  • 114
    • 0022972814 scopus 로고
    • Tenascin: An extracellular matrix protein involved in tissue interactions during fetal development and oncogenesis
    • Chiquet-Ehrismann R., Mackie E.J., Pearson C.A., Sakakura T. Tenascin: an extracellular matrix protein involved in tissue interactions during fetal development and oncogenesis. Cell. 47:1986;131-139.
    • (1986) Cell , vol.47 , pp. 131-139
    • Chiquet-Ehrismann, R.1    Mackie, E.J.2    Pearson, C.A.3    Sakakura, T.4
  • 115
    • 0025827485 scopus 로고
    • Tenascin in normal, reactive, hyperplastic, and neoplastic tissues: Biologic and pathologic implications
    • Koukoulis G.K., Gould V.E., Bhattacharyya A., Could J.E., Howeedy A.A., Virtanen I. Tenascin in normal, reactive, hyperplastic, and neoplastic tissues: biologic and pathologic implications. Hum. Pathol. 22:1991;636-643.
    • (1991) Hum. Pathol. , vol.22 , pp. 636-643
    • Koukoulis, G.K.1    Gould, V.E.2    Bhattacharyya, A.3    Could, J.E.4    Howeedy, A.A.5    Virtanen, I.6
  • 116
    • 0025980153 scopus 로고
    • Enhanced expression of neural cell adhesion molecules and tenascin (cytotactin) during wound healing
    • Chuong C.M., Chen H.M. Enhanced expression of neural cell adhesion molecules and tenascin (cytotactin) during wound healing. Am. J. Pathol. 138:1991;427-440.
    • (1991) Am. J. Pathol. , vol.138 , pp. 427-440
    • Chuong, C.M.1    Chen, H.M.2
  • 117
    • 0025098987 scopus 로고
    • Binding of hexabrachion (tenascin) to the extracellular matrix and substratum and its effect on cell adhesion
    • Lightner V.A., Erickson H.P. Binding of hexabrachion (tenascin) to the extracellular matrix and substratum and its effect on cell adhesion. J. Cell Sci. 95:1990;263-277.
    • (1990) J. Cell Sci. , vol.95 , pp. 263-277
    • Lightner, V.A.1    Erickson, H.P.2
  • 118
  • 119
    • 0025847137 scopus 로고
    • The extracellular matrix of lip wounds in fetal, neonatal and adult mice
    • Whitby D.J., Ferguson M.W. The extracellular matrix of lip wounds in fetal, neonatal and adult mice. Development. 112:1991;651-668.
    • (1991) Development , vol.112 , pp. 651-668
    • Whitby, D.J.1    Ferguson, M.W.2
  • 121
    • 0024515867 scopus 로고
    • Fibroblasts that proliferate near denervated synaptic sites in skeletal muscle synthesize the adhesive molecules tenascin (J1), N-CAM, fibronectin, and a heparan sulfate proteoglycan
    • Gatchalian C.L., Schachner M., Sanes J.R. Fibroblasts that proliferate near denervated synaptic sites in skeletal muscle synthesize the adhesive molecules tenascin (J1), N-CAM, fibronectin, and a heparan sulfate proteoglycan. J. Cell Biol. 108:1989;1873-1890.
    • (1989) J. Cell Biol. , vol.108 , pp. 1873-1890
    • Gatchalian, C.L.1    Schachner, M.2    Sanes, J.R.3
  • 122
    • 0030003154 scopus 로고    scopus 로고
    • Mitogenesis, cell migration and loss of focal adhesion induced by tenascin-C interacting with its cell surface receptor, annexin II
    • Chung C.Y., Murphy-Ullrich J.E., Erickson H.P. Mitogenesis, cell migration and loss of focal adhesion induced by tenascin-C interacting with its cell surface receptor, annexin II. Mol. Biol. Cell. 7:1996;883-892.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 883-892
    • Chung, C.Y.1    Murphy-Ullrich, J.E.2    Erickson, H.P.3
  • 123
    • 0024840912 scopus 로고
    • Proteinases and extracellular matrix remodeling
    • Alexander C.M., Werb Z. Proteinases and extracellular matrix remodeling. Curr. Opin. Cell Biol. 1:1989;974-982.
    • (1989) Curr. Opin. Cell Biol. , vol.1 , pp. 974-982
    • Alexander, C.M.1    Werb, Z.2
  • 124
    • 0026341460 scopus 로고
    • In vivo paracrine interaction between urokinase and its receptor: Effect on tumor cell invasion
    • Ossowski L., Clunie G., Masucci M.T., Blasi F. In vivo paracrine interaction between urokinase and its receptor: effect on tumor cell invasion. J. Cell Biol. 115:1991;1107-1112.
    • (1991) J. Cell Biol. , vol.115 , pp. 1107-1112
    • Ossowski, L.1    Clunie, G.2    Masucci, M.T.3    Blasi, F.4
  • 125
    • 0033548069 scopus 로고    scopus 로고
    • Identification of the tissue inhibitor of metalloproteinases-2 (TIMP-2) binding site on the hemopexin carboxyl domain of human gelatinase A by site-directed mutagenesis. The hierarchical role in binding timp-2 of the unique cationic clusters of hemopexin modules iii and iv
    • Overall C.M., King A.E., Sam D.K., Ong A.D., Lau T.T.Y., Wallon U.M., DeClerck Y.A., Atherstone J. Identification of the tissue inhibitor of metalloproteinases-2 (TIMP-2) binding site on the hemopexin carboxyl domain of human gelatinase A by site-directed mutagenesis. The hierarchical role in binding timp-2 of the unique cationic clusters of hemopexin modules iii and iv. J. Biol. Chem. 274:1999;4421-4429.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4421-4429
    • Overall, C.M.1    King, A.E.2    Sam, D.K.3    Ong, A.D.4    Lau, T.T.Y.5    Wallon, U.M.6    Declerck, Y.A.7    Atherstone, J.8
  • 126
    • 0033556368 scopus 로고    scopus 로고
    • Enhanced production and activation of progelatinase A mediated by membrane-type 1 matrix metalloproteinase in human papillary thyroid carcinomas
    • Nakamura H., Ueno H., Yamashita K., Shimada T., Yamamoto E., Noguchi M., Fujimoto N., Sato H., Seiki M., Okada Y. Enhanced production and activation of progelatinase A mediated by membrane-type 1 matrix metalloproteinase in human papillary thyroid carcinomas. Cancer Res. 59:1999;467-473.
    • (1999) Cancer Res. , vol.59 , pp. 467-473
    • Nakamura, H.1    Ueno, H.2    Yamashita, K.3    Shimada, T.4    Yamamoto, E.5    Noguchi, M.6    Fujimoto, N.7    Sato, H.8    Seiki, M.9    Okada, Y.10
  • 127
    • 0025880945 scopus 로고
    • The endothelial cell tissue plasminogen activator receptor. Specific interaction with plasminogen
    • Hajjar K.A. The endothelial cell tissue plasminogen activator receptor. Specific interaction with plasminogen. J. Biol. Chem. 266:1991;21962-21970.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21962-21970
    • Hajjar, K.A.1
  • 128
    • 0025363927 scopus 로고
    • Identification and characterization of human endothelial cell membrane binding sites for tissue plasminogen activator and urokinase
    • Hajjar K.A., Hamel N.M. Identification and characterization of human endothelial cell membrane binding sites for tissue plasminogen activator and urokinase. J. Biol. Chem. 265:1990;2908-2916.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2908-2916
    • Hajjar, K.A.1    Hamel, N.M.2
  • 130
    • 0032374094 scopus 로고    scopus 로고
    • The p11 subunit of the annexin II tetramer plays a key role in the stimulation of t-PA-dependent plasminogen activation
    • Kassam G., Le B.H., Choi K.S., Kang H.M., Fitzpatrick S.L., Louie P., Waisman D.M. The p11 subunit of the annexin II tetramer plays a key role in the stimulation of t-PA-dependent plasminogen activation. Biochemistry. 37:1998;16958-16966.
    • (1998) Biochemistry , vol.37 , pp. 16958-16966
    • Kassam, G.1    Le, B.H.2    Choi, K.S.3    Kang, H.M.4    Fitzpatrick, S.L.5    Louie, P.6    Waisman, D.M.7
  • 131
    • 0032485048 scopus 로고    scopus 로고
    • The plasminogen activator system in pancreas cancer: Role of t-PA in the invasive potential in vitro
    • Paciucci R., Tora M., Diaz V.M., Real F.X. The plasminogen activator system in pancreas cancer: role of t-PA in the invasive potential in vitro. Oncogene. 16:1998;625-633.
    • (1998) Oncogene , vol.16 , pp. 625-633
    • Paciucci, R.1    Tora, M.2    Diaz, V.M.3    Real, F.X.4
  • 132
    • 0025417934 scopus 로고
    • Stromelysin/transin and tumor progression
    • Matrisian L.M., Bowden G.T. Stromelysin/transin and tumor progression. Semin. Cancer Biol. 1:1990;107-115.
    • (1990) Semin. Cancer Biol. , vol.1 , pp. 107-115
    • Matrisian, L.M.1    Bowden, G.T.2
  • 133
    • 0030588948 scopus 로고    scopus 로고
    • Competition between plasminogen and procathepsin B as a probe to demonstrate the in vitro activation of procathepsin B by the tissue plasminogen activator
    • Dalet-Fumeron V., Boudjennah L., Pagano M. Competition between plasminogen and procathepsin B as a probe to demonstrate the in vitro activation of procathepsin B by the tissue plasminogen activator. Arch. Biochem. Biophys. 335:1996;351-357.
    • (1996) Arch. Biochem. Biophys. , vol.335 , pp. 351-357
    • Dalet-Fumeron, V.1    Boudjennah, L.2    Pagano, M.3
  • 134
    • 0027650966 scopus 로고
    • Proteases of cell adhesion proteins in cancer
    • Monsky W.L., Chen W.T. Proteases of cell adhesion proteins in cancer. Semin. Cancer Biol. 4:1993;251-258.
    • (1993) Semin. Cancer Biol. , vol.4 , pp. 251-258
    • Monsky, W.L.1    Chen, W.T.2
  • 136
    • 0028152543 scopus 로고
    • A potential marker protease of invasiveness, seprase, is localized on invadopodia of human malignant melanoma cells
    • Monsky W.L., Lin C.Y., Aoyama A., Kelly T., Akiyama S.K., Mueller S.C., Chen W.T. A potential marker protease of invasiveness, seprase, is localized on invadopodia of human malignant melanoma cells. Cancer Res. 54:1994;5702-5710.
    • (1994) Cancer Res. , vol.54 , pp. 5702-5710
    • Monsky, W.L.1    Lin, C.Y.2    Aoyama, A.3    Kelly, T.4    Akiyama, S.K.5    Mueller, S.C.6    Chen, W.T.7
  • 137
    • 0025853849 scopus 로고
    • Cellular invasion into matrix beads: Localization of beta 1 integrins and fibronectin to the invadopodia
    • Mueller S.C., Chen W.T. Cellular invasion into matrix beads: localization of beta 1 integrins and fibronectin to the invadopodia. J. Cell Sci. 2:1991;213-225.
    • (1991) J. Cell Sci. , vol.2 , pp. 213-225
    • Mueller, S.C.1    Chen, W.T.2
  • 138
    • 0025029188 scopus 로고
    • A 170-kDa membrane-bound protease is associated with the expression of invasiveness by human malignant melanoma cells
    • Aoyama A., 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. 87:1990;8296-8300.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8296-8300
    • Aoyama, A.1    Chen, W.T.2
  • 140
    • 0031583964 scopus 로고    scopus 로고
    • The intact urokinase receptor is required for efficient vitronectin binding: Receptor cleavage prevents ligand interaction
    • Hoyer-Hansen G., Behrendt N., Ploug M., Dano K., Preissner K.T. The intact urokinase receptor is required for efficient vitronectin binding: receptor cleavage prevents ligand interaction. FEBS Lett. 420:1997;79-85.
    • (1997) FEBS Lett. , vol.420 , pp. 79-85
    • Hoyer-Hansen, G.1    Behrendt, N.2    Ploug, M.3    Dano, K.4    Preissner, K.T.5
  • 141
    • 0344507516 scopus 로고    scopus 로고
    • A role for caveolin and the urokinase receptor in integrin-mediated adhesion and signaling
    • Wei Y., Yang X., Liu Q., Wilkins J.A., Chapman H.A. A role for caveolin and the urokinase receptor in integrin-mediated adhesion and signaling. J. Cell Biol. 144:1999;1285-1294.
    • (1999) J. Cell Biol. , vol.144 , pp. 1285-1294
    • Wei, Y.1    Yang, X.2    Liu, Q.3    Wilkins, J.A.4    Chapman, H.A.5
  • 142
    • 0028944244 scopus 로고
    • The urokinase-type plasminogen activator receptor, a GPI-linked protein, is localized in caveolae
    • Stahl A., Mueller B.M. The urokinase-type plasminogen activator receptor, a GPI-linked protein, is localized in caveolae. J. Cell Biol. 129:1995;335-344.
    • (1995) J. Cell Biol. , vol.129 , pp. 335-344
    • Stahl, A.1    Mueller, B.M.2
  • 143
    • 0029014820 scopus 로고
    • Endothelial caveolae have the molecular transport machinery for vesicle budding, docking, and fusion including VAMP, NSF, SNAP, annexins, and GTPases
    • Schnitzer J.E., Liu J., Oh P. Endothelial caveolae have the molecular transport machinery for vesicle budding, docking, and fusion including VAMP, NSF, SNAP, annexins, and GTPases. J. Biol. Chem. 270:1995;14399-14404.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14399-14404
    • Schnitzer, J.E.1    Liu, J.2    Oh, P.3
  • 144
    • 0027231101 scopus 로고
    • Stress-relaxation of fibroblasts in collagen matrices triggers ectocytosis of plasma membrane vesicles containing actin, annexins II and VI, and beta 1 integrin receptors
    • Lee T.L., Lin Y.C., Mochitate K., Grinnell F. Stress-relaxation of fibroblasts in collagen matrices triggers ectocytosis of plasma membrane vesicles containing actin, annexins II and VI, and beta 1 integrin receptors. J. Cell. Sci. 105:1993;167-177.
    • (1993) J. Cell. Sci. , vol.105 , pp. 167-177
    • Lee, T.L.1    Lin, Y.C.2    Mochitate, K.3    Grinnell, F.4
  • 145
    • 0029965589 scopus 로고    scopus 로고
    • A mechanism for regulation of melanoma invasion. Ligation of alpha6beta1 integrin by laminin G peptides
    • Nakahara H., Nomizu M., Akiyama S.K., Yamada Y., Yeh Y., Chen W.T. A mechanism for regulation of melanoma invasion. Ligation of alpha6beta1 integrin by laminin G peptides. J. Biol. Chem. 271:1996;27221-27224.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27221-27224
    • Nakahara, H.1    Nomizu, M.2    Akiyama, S.K.3    Yamada, Y.4    Yeh, Y.5    Chen, W.T.6
  • 146
    • 0032484149 scopus 로고    scopus 로고
    • Up-regulation of caveolae and caveolar constituents in multidrug-resistant cancer cells
    • Lavie Y., Fiucci G., Liscovitch M. Up-regulation of caveolae and caveolar constituents in multidrug-resistant cancer cells. J. Biol. Chem. 273:1998;32380-32383.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32380-32383
    • Lavie, Y.1    Fiucci, G.2    Liscovitch, M.3


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