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Volumn 22, Issue 2-3, 2003, Pages 271-286

Pericellular cathepsin B and malignant progression

Author keywords

Cell surface binding proteins; Cysteine proteases; Endosomes; Lysosomes; Secretion

Indexed keywords

CATHEPSIN B; CYSTEINE PROTEINASE; ENZYME PRECURSOR; LIPID; LIPOCORTIN 2; LYSOSOME ENZYME; MATRIX METALLOPROTEINASE; MEMBRANE ENZYME; MESSENGER RNA; SERINE PROTEINASE; SOMATOMEDIN B RECEPTOR; TETRAMER;

EID: 0038215389     PISSN: 01677659     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1023007717757     Document Type: Review
Times cited : (212)

References (130)
  • 2
    • 0023575526 scopus 로고
    • Properties of a plasma membrane-associated cathepsin B-like cysteine proteinase in metastatic B16 melanoma variants
    • Rozhin J, Robinson D, Stevens MA, Lah TT, Honn KV, Ryan RE, Sloane BF: Properties of a plasma membrane-associated cathepsin B-like cysteine proteinase in metastatic B16 melanoma variants. Cancer Res 47(24 Pt 1): 6620-6628, 1987
    • (1987) Cancer Res , vol.47 , Issue.24 PART 1 , 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
  • 4
    • 0026596861 scopus 로고
    • Proteolytic processing and glycosylation of cathepsin B. The role of the primary structure of the latent precursor and of the carbohydrate moiety for cell-type-specific molecular forms of the enzyme
    • Mach L, Stuwe K, Hagen A, Ballaun C, Glossl J: Proteolytic processing and glycosylation of cathepsin B. The role of the primary structure of the latent precursor and of the carbohydrate moiety for cell-type-specific molecular forms of the enzyme. Biochem J 282(Pt 2): 577-582, 1992
    • (1992) Biochem J , vol.282 , Issue.PART 2 , pp. 577-582
    • Mach, L.1    Stuwe, K.2    Hagen, A.3    Ballaun, C.4    Glossl, J.5
  • 6
    • 0034930528 scopus 로고    scopus 로고
    • Towards specific functions of lysosomal cysteine peptidases: Phenotypes of mice deficient for cathepsin B or cathepsin L
    • Reinheckel T, Deussing J, Roth W, Peters C: Towards specific functions of lysosomal cysteine peptidases: Phenotypes of mice deficient for cathepsin B or cathepsin L. Biol Chem 382(5): 735-741, 2001
    • (2001) Biol Chem , vol.382 , Issue.5 , pp. 735-741
    • Reinheckel, T.1    Deussing, J.2    Roth, W.3    Peters, C.4
  • 7
    • 0019765848 scopus 로고
    • Cathepsin B, Cathepsin H, Cathepsin L
    • Barrett AJ, Kirschke H: Cathepsin B, Cathepsin H, Cathepsin L. Methods Enzymol 80(Pt C): 535-561, 1981
    • (1981) Methods Enzymol , vol.80 , Issue.PART C , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 8
    • 0033848451 scopus 로고    scopus 로고
    • The relative importance of cysteine peptidases in osteoarthritis
    • Lang A, Horler D, Baici A: The relative importance of cysteine peptidases in osteoarthritis. J Rheumatol 27(8): 1970-1979, 2000
    • (2000) J Rheumatol , vol.27 , Issue.8 , pp. 1970-1979
    • Lang, A.1    Horler, D.2    Baici, A.3
  • 9
    • 0028273525 scopus 로고
    • Membrane association of cathepsin B can be induced by transfection of human breast epithelial cells with c-Ha-ras oncogene
    • Sloane BF, Moin K, Sameni M, Tait LR, 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(Pt 2): 373-384, 1994
    • (1994) J Cell Sci , vol.107 , Issue.PART 2 , pp. 373-384
    • Sloane, B.F.1    Moin, K.2    Sameni, M.3    Tait, L.R.4    Rozhin, J.5    Ziegler, G.6
  • 10
    • 0003126050 scopus 로고    scopus 로고
    • Molecular regulation, membrane association and secretion of tumor cathepsin B
    • Frosch BA, Berquin I, Emmert-Buck MR, Moin K, Sloane BF: Molecular regulation, membrane association and secretion of tumor cathepsin B. Apmis 107(1): 28-37, 1999
    • (1999) Apmis , vol.107 , Issue.1 , pp. 28-37
    • Frosch, B.A.1    Berquin, I.2    Emmert-Buck, M.R.3    Moin, K.4    Sloane, B.F.5
  • 11
    • 0028901908 scopus 로고
    • Cathepsin B in osteoarthritis: Cytochemical and histochemical analysis of human femoral head cartilage
    • Baici A, Lang A, Horler D, Kissling R, Merlin C: Cathepsin B in osteoarthritis: Cytochemical and histochemical analysis of human femoral head cartilage. Ann Rheum Dis 54(4): 289-297, 1995
    • (1995) Ann Rheum Dis , vol.54 , Issue.4 , pp. 289-297
    • Baici, A.1    Lang, A.2    Horler, D.3    Kissling, R.4    Merlin, C.5
  • 12
    • 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 BF, Emmert-Buck MR: Cathepsin B expression in colorectal carcinomas correlates with tumor progression and shortened patient survival. Am J Pathol 145(2): 301-309, 1994
    • (1994) Am J Pathol , vol.145 , Issue.2 , 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.R.7
  • 13
    • 0036660666 scopus 로고    scopus 로고
    • Determination of cathepsin B expression may offer additional prognostic information for ovarian cancer patients
    • Scorilas A, Fotiou S, Tsiambas E, Yotis J, Kotsiandri F, Sameni M, Sloane BF, Talieri M: Determination of cathepsin B expression may offer additional prognostic information for ovarian cancer patients. Biol Chem 383(7/8): 1297-1303, 2002
    • (2002) Biol Chem , vol.383 , Issue.7-8 , pp. 1297-1303
    • Scorilas, A.1    Fotiou, S.2    Tsiambas, E.3    Yotis, J.4    Kotsiandri, F.5    Sameni, M.6    Sloane, B.F.7    Talieri, M.8
  • 14
    • 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 AA, Gleason DF, Deleon OF, Wilson MJ, Sloane BF: Localization of a biotinylated cathepsin B oligonucleotide probe in human prostate including invasive cells and invasive edges by in situ hybridization. Anat Rec 235(2): 233-240, 1993
    • (1993) Anat Rec , vol.235 , Issue.2 , pp. 233-240
    • Sinha, A.A.1    Gleason, D.F.2    Deleon, O.F.3    Wilson, M.J.4    Sloane, B.F.5
  • 16
    • 0037200058 scopus 로고    scopus 로고
    • Interaction of human breast fibroblasts with collagen I increases secretion of procathepsin B
    • Koblinski JE, Dosescu J, Sameni M, Moin K, Clark K, Sloane BF: Interaction of human breast fibroblasts with collagen I increases secretion of procathepsin B. J Biol Chem 277(35): 32220-32227, 2002
    • (2002) J Biol Chem , vol.277 , Issue.35 , pp. 32220-32227
    • Koblinski, J.E.1    Dosescu, J.2    Sameni, M.3    Moin, K.4    Clark, K.5    Sloane, B.F.6
  • 17
    • 0034008432 scopus 로고    scopus 로고
    • Transcription of human cathepsin B is mediated by Sp1 and Ets family factors in glioma
    • Yan S, Berquin IM, Troen BR, Sloane BF: Transcription of human cathepsin B is mediated by Sp1 and Ets family factors in glioma. DNA Cell Biol 19(2): 79-91, 2000
    • (2000) DNA Cell Biol , vol.19 , Issue.2 , pp. 79-91
    • Yan, S.1    Berquin, I.M.2    Troen, B.R.3    Sloane, B.F.4
  • 18
    • 0036083164 scopus 로고    scopus 로고
    • Ets-1 upregulates matrix metalloproteinase-1 expression through extracellular matrix adhesion in vascular endothelial cells
    • Naito S, Shimizu S, Matsuu M, Nakashima M, Nakayama T, Yamashita S, Sekine I: Ets-1 upregulates matrix metalloproteinase-1 expression through extracellular matrix adhesion in vascular endothelial cells. Biochem Biophys Res Commun 291(1): 130-138, 2002
    • (2002) Biochem Biophys Res Commun , vol.291 , Issue.1 , pp. 130-138
    • Naito, S.1    Shimizu, S.2    Matsuu, M.3    Nakashima, M.4    Nakayama, T.5    Yamashita, S.6    Sekine, I.7
  • 19
    • 0031838477 scopus 로고    scopus 로고
    • The expression of an Ets1 transcription factor lacking its activation domain decreases uPA proteolytic activity and cell motility, and impairs normal tubulogenesis and cancerous scattering in mammary epithelial cells
    • Delannoy-Courdent A, Mattot V, Fafeur V, Fauquette W, Pollet I, Calmels T, Vercamer C, Boilly B, Vandenbunder B, Desbiens X: The expression of an Ets1 transcription factor lacking its activation domain decreases uPA proteolytic activity and cell motility, and impairs normal tubulogenesis and cancerous scattering in mammary epithelial cells. J Cell Sci 111(Pt 11): 1521-1534, 1998
    • (1998) J Cell Sci , vol.111 , Issue.PART 11 , pp. 1521-1534
    • Delannoy-Courdent, A.1    Mattot, V.2    Fafeur, V.3    Fauquette, W.4    Pollet, I.5    Calmels, T.6    Vercamer, C.7    Boilly, B.8    Vandenbunder, B.9    Desbiens, X.10
  • 20
    • 0037041012 scopus 로고    scopus 로고
    • Identification and functional analysis of the rat caspase-3 gene promoter
    • Liu W, Wang G, Yakovlev AG: Identification and functional analysis of the rat caspase-3 gene promoter. J Biol Chem 277(10): 8273-8278, 2002
    • (2002) J Biol Chem , vol.277 , Issue.10 , pp. 8273-8278
    • Liu, W.1    Wang, G.2    Yakovlev, A.G.3
  • 21
    • 0037177886 scopus 로고    scopus 로고
    • Phorbol ester activation of a proteolytic cascade capable of activating latent transforming growth factor-beta. A process initiated by the exocytosis of cathepsin B
    • Guo M, Mathieu PA, Linebaugh B, Sloane BF, Reiners JJ Jr: Phorbol ester activation of a proteolytic cascade capable of activating latent transforming growth factor-beta. A process initiated by the exocytosis of cathepsin B. J Biol Chem 277(17): 14829-14837, 2002
    • (2002) J Biol Chem , vol.277 , Issue.17 , pp. 14829-14837
    • Guo, M.1    Mathieu, P.A.2    Linebaugh, B.3    Sloane, B.F.4    Reiners J.J., Jr.5
  • 23
    • 0024513083 scopus 로고
    • Cathepsin B in human breast tumor tissue and cancer cells
    • Krepela E, Vicar J, Cernoch M: Cathepsin B in human breast tumor tissue and cancer cells. Neoplasma 36(1): 41-52, 1989
    • (1989) Neoplasma , vol.36 , Issue.1 , pp. 41-52
    • Krepela, E.1    Vicar, J.2    Cernoch, M.3
  • 25
    • 0025863290 scopus 로고
    • Stage-specific increases in cathepsin B messenger RNA content in human colorectal carcinoma
    • Murnane MJ, Sheahan K, Ozdemirli M, Shuja S: Stage-specific increases in cathepsin B messenger RNA content in human colorectal carcinoma. Cancer Res 51(4): 1137-1142, 1991
    • (1991) Cancer Res , vol.51 , Issue.4 , pp. 1137-1142
    • Murnane, M.J.1    Sheahan, K.2    Ozdemirli, M.3    Shuja, S.4
  • 27
    • 0024321219 scopus 로고
    • Cysteine protease activities and tumor development in human colorectal carcinoma
    • Sheahan K, Shuja S, Murnane MJ: Cysteine protease activities and tumor development in human colorectal carcinoma. Cancer Res 49(14): 3809-3814, 1989
    • (1989) Cancer Res , vol.49 , Issue.14 , pp. 3809-3814
    • Sheahan, K.1    Shuja, S.2    Murnane, M.J.3
  • 28
    • 0026095328 scopus 로고
    • Cysteine endopeptidase activity levels in normal human tissues, colorectal adenomas and carcinomas
    • Shuja S, Sheahan K, Murnane MJ: Cysteine endopeptidase activity levels in normal human tissues, colorectal adenomas and carcinomas. Int J Cancer 49(3): 341-346, 1991
    • (1991) Int J Cancer , vol.49 , Issue.3 , pp. 341-346
    • Shuja, S.1    Sheahan, K.2    Murnane, M.J.3
  • 31
    • 0005328942 scopus 로고    scopus 로고
    • Cathepsin B on invasion and metastasis of gastric carcinoma
    • Liu Y, Xiao S, Shi Y, Wang L, Ren W, Sloane BF: Cathepsin B on invasion and metastasis of gastric carcinoma. Chin Med J (Engl) 111(9): 784-788, 1998
    • (1998) Chin Med J (Engl) , vol.111 , Issue.9 , pp. 784-788
    • Liu, Y.1    Xiao, S.2    Shi, Y.3    Wang, L.4    Ren, W.5    Sloane, B.F.6
  • 36
    • 0035281687 scopus 로고    scopus 로고
    • Activity, expression, and transcription rate of the cathepsins B, D, H, and L in cutaneous malignant melanoma
    • Frohlich E, Schlagenhauff B, Mohrle M, Weber E, Klessen C, Rassner G: Activity, expression, and transcription rate of the cathepsins B, D, H, and L in cutaneous malignant melanoma. Cancer 91(5): 972-982, 2001
    • (2001) Cancer , vol.91 , Issue.5 , pp. 972-982
    • Frohlich, E.1    Schlagenhauff, B.2    Mohrle, M.3    Weber, E.4    Klessen, C.5    Rassner, G.6
  • 37
    • 0031874052 scopus 로고    scopus 로고
    • Presence of activated ras correlates with increased cysteine proteinase activities in human colorectal carcinomas
    • Kim K, Cai J, Shuja S, Kuo T, Murnane MJ: Presence of activated ras correlates with increased cysteine proteinase activities in human colorectal carcinomas. Int J Cancer 79(4): 324-333, 1998
    • (1998) Int J Cancer , vol.79 , Issue.4 , pp. 324-333
    • Kim, K.1    Cai, J.2    Shuja, S.3    Kuo, T.4    Murnane, M.J.5
  • 39
    • 0029048724 scopus 로고
    • Identification of two new exons and multiple transcription start points in the 5′-untranslated region of the human cathepsin-B-encoding gene
    • Berquin IM, Cao L, Fong D, Sloane BF: Identification of two new exons and multiple transcription start points in the 5′-untranslated region of the human cathepsin-B-encoding gene. Gene 159(2): 143-149, 1995
    • (1995) Gene , vol.159 , Issue.2 , pp. 143-149
    • Berquin, I.M.1    Cao, L.2    Fong, D.3    Sloane, B.F.4
  • 40
    • 0026925864 scopus 로고
    • Oncogenic conversion alters the transcriptional properties of ets
    • Wasylyk C, Wasylyk B: Oncogenic conversion alters the transcriptional properties of ets. Cell Growth Differ 3(9): 617-625, 1992
    • (1992) Cell Growth Differ , vol.3 , Issue.9 , pp. 617-625
    • Wasylyk, C.1    Wasylyk, B.2
  • 41
    • 0030971757 scopus 로고    scopus 로고
    • The ETS1 transcription factor is expressed during epithelial-mesenchymal transitions in the chick embryo and is activated in scatter factor-stimulated MDCK epithelial cells
    • Fafeur V, Tulasne D, Queva C, Vercamer C, Dimster V, Mattot V, Stehelin D, Desbiens X, Vandenbunder B: The ETS1 transcription factor is expressed during epithelial-mesenchymal transitions in the chick embryo and is activated in scatter factor-stimulated MDCK epithelial cells. Cell Growth Differ 8(6): 655-665, 1997
    • (1997) Cell Growth Differ , vol.8 , Issue.6 , pp. 655-665
    • Fafeur, V.1    Tulasne, D.2    Queva, C.3    Vercamer, C.4    Dimster, V.5    Mattot, V.6    Stehelin, D.7    Desbiens, X.8    Vandenbunder, B.9
  • 42
    • 0032557529 scopus 로고    scopus 로고
    • In vivo expression of an alternatively spliced human tumor message that encodes a truncated form of cathepsin B. Subcellular distribution of the truncated enzyme in COS cells
    • Mehtani S, Gong Q, Panella J, Subbiah S, Peffley DM, Frankfater A: In vivo expression of an alternatively spliced human tumor message that encodes a truncated form of cathepsin B. Subcellular distribution of the truncated enzyme in COS cells. J Biol Chem 273(21): 13236-13244, 1998
    • (1998) J Biol Chem , vol.273 , Issue.21 , pp. 13236-13244
    • Mehtani, S.1    Gong, Q.2    Panella, J.3    Subbiah, S.4    Peffley, D.M.5    Frankfater, A.6
  • 43
    • 0034890869 scopus 로고    scopus 로고
    • Alternative messenger RNA splicing and enzyme forms of cathepsin B in human osteoarthritic cartilage and cultured chondrocytes
    • Berardi S, Lang A, Kostoulas G, Horler D, Vilei EM, Baici A: Alternative messenger RNA splicing and enzyme forms of cathepsin B in human osteoarthritic cartilage and cultured chondrocytes. Arthritis Rheum 44(8): 1819-1831, 2001
    • (2001) Arthritis Rheum , vol.44 , Issue.8 , pp. 1819-1831
    • Berardi, S.1    Lang, A.2    Kostoulas, G.3    Horler, D.4    Vilei, E.M.5    Baici, A.6
  • 44
  • 45
    • 0030736630 scopus 로고    scopus 로고
    • Oncogenic c-Ki-ras but not oncogenic c-Ha-ras up-regulates CEA expression and disrupts basolateral polarity in colon epithelial cells
    • Yan Z, Deng X, Chen M, Xu Y, Ahram M, Sloane BF, Friedman E: Oncogenic c-Ki-ras but not oncogenic c-Ha-ras up-regulates CEA expression and disrupts basolateral polarity in colon epithelial cells. J Biol Chem 272(44): 27902-27907, 1997
    • (1997) J Biol Chem , vol.272 , Issue.44 , pp. 27902-27907
    • Yan, Z.1    Deng, X.2    Chen, M.3    Xu, Y.4    Ahram, M.5    Sloane, B.F.6    Friedman, E.7
  • 46
    • 0028618307 scopus 로고
    • Pericellular pH affects distribution and secretion of cathepsin B in malignant cells
    • Rozhin J, Sameni M, Ziegler G, Sloane BF: Pericellular pH affects distribution and secretion of cathepsin B in malignant cells. Cancer Res 54(24): 6517-6525, 1994
    • (1994) Cancer Res , vol.54 , Issue.24 , pp. 6517-6525
    • Rozhin, J.1    Sameni, M.2    Ziegler, G.3    Sloane, B.F.4
  • 47
    • 0025312728 scopus 로고
    • A genetic model for colorectal tumorigenesis
    • Fearon ER, Vogelstein B: A genetic model for colorectal tumorigenesis. Cell 61(5): 759-767, 1990
    • (1990) Cell , vol.61 , Issue.5 , pp. 759-767
    • Fearon, E.R.1    Vogelstein, B.2
  • 49
    • 0031080747 scopus 로고    scopus 로고
    • Functional defects in lysosomal enzymes in autosomal dominant polycystic kidney disease (ADPKD): Abnormalities in synthesis, molecular processing, polarity, and secretion
    • Hartz PA, Wilson PD: Functional defects in lysosomal enzymes in autosomal dominant polycystic kidney disease (ADPKD): Abnormalities in synthesis, molecular processing, polarity, and secretion. Biochem Mol Med 60(1): 8-26, 1997
    • (1997) Biochem Mol Med , vol.60 , Issue.1 , pp. 8-26
    • Hartz, P.A.1    Wilson, P.D.2
  • 50
    • 0027221060 scopus 로고
    • Autocrine, endocrine and paracrine regulation of growth abnormalities in autosomal dominant polycystic kidney disease
    • Wilson PD, Du J, Norman JT: Autocrine, endocrine and paracrine regulation of growth abnormalities in autosomal dominant polycystic kidney disease. Eur J Cell Biol 61(1): 131-138, 1993
    • (1993) Eur J Cell Biol , vol.61 , Issue.1 , pp. 131-138
    • Wilson, P.D.1    Du, J.2    Norman, J.T.3
  • 51
    • 0029082997 scopus 로고
    • Abnormal polarization of EGF receptors and autocrine stimulation of cyst epithelial growth in human ADPKD
    • Du J, Wilson PD: Abnormal polarization of EGF receptors and autocrine stimulation of cyst epithelial growth in human ADPKD. Am J Physiol 269(2 Pt 1): C487-C495, 1995
    • (1995) Am J Physiol , vol.269 , Issue.2 PART 1
    • Du, J.1    Wilson, P.D.2
  • 52
    • 0026436985 scopus 로고
    • Autosomal dominant polycystic kidney disease: Cellular and molecular mechanisms of cyst formation
    • Wilson PD, Burrow CR: Autosomal dominant polycystic kidney disease: Cellular and molecular mechanisms of cyst formation. Adv Nephrol Necker Hosp 21: 125-142, 1992
    • (1992) Adv Nephrol Necker Hosp , vol.21 , pp. 125-142
    • Wilson, P.D.1    Burrow, C.R.2
  • 53
    • 0024402455 scopus 로고
    • Cyst-derived cells do not exhibit accelerated growth or features of transformed cells in vitro
    • Carone FA, Nakamura S, Schumacher BS, Punyarit P, Bauer KD: Cyst-derived cells do not exhibit accelerated growth or features of transformed cells in vitro. Kidney Int 35(6): 1351-1357, 1989
    • (1989) Kidney Int , vol.35 , Issue.6 , pp. 1351-1357
    • Carone, F.A.1    Nakamura, S.2    Schumacher, B.S.3    Punyarit, P.4    Bauer, K.D.5
  • 54
    • 0024321224 scopus 로고
    • Increased secretion, altered processing, and glycosylation of pro-cathepsin D in human mammary cancer cells
    • Capony F, Rougeot C, Montcourrier P, Cavailles V, Salazar G, Rochefort H: Increased secretion, altered processing, and glycosylation of pro-cathepsin D in human mammary cancer cells. Cancer Res 49(14): 3904-3909, 1989
    • (1989) Cancer Res , vol.49 , Issue.14 , pp. 3904-3909
    • Capony, F.1    Rougeot, C.2    Montcourrier, P.3    Cavailles, V.4    Salazar, G.5    Rochefort, H.6
  • 55
    • 0023576902 scopus 로고
    • Translocation and clustering of endosomes and lysosomes depends on microtubules
    • Matteoni R, Kreis TE: Translocation and clustering of endosomes and lysosomes depends on microtubules. J Cell Biol 105(3): 1253-1265, 1987
    • (1987) J Cell Biol , vol.105 , Issue.3 , pp. 1253-1265
    • Matteoni, R.1    Kreis, T.E.2
  • 56
    • 0032468335 scopus 로고    scopus 로고
    • Malignant transformation alters intracellular trafficking of lysosomal cathepsin D in human breast epithelial cells
    • Nishimura Y, Sameni M, Sloane BF: Malignant transformation alters intracellular trafficking of lysosomal cathepsin D in human breast epithelial cells. Pathol Oncol Res 4(4): 283-296, 1998
    • (1998) Pathol Oncol Res , vol.4 , Issue.4 , pp. 283-296
    • Nishimura, Y.1    Sameni, M.2    Sloane, B.F.3
  • 57
    • 0031965953 scopus 로고    scopus 로고
    • Dynein and dynein-related genes
    • Milisav I: Dynein and dynein-related genes. Cell Motil Cytoskeleton 39(4): 261-272, 1998
    • (1998) Cell Motil Cytoskeleton , vol.39 , Issue.4 , pp. 261-272
    • Milisav, I.1
  • 58
    • 0032489870 scopus 로고    scopus 로고
    • Golgi vesiculation and lysosome dispersion in cells lacking cytoplasmic dynein
    • Harada A, Takei Y, Kanai Y, Tanaka Y, Nonaka S, Hirokawa N: Golgi vesiculation and lysosome dispersion in cells lacking cytoplasmic dynein. J Cell Biol 141(1): 51-59, 1998
    • (1998) J Cell Biol , vol.141 , Issue.1 , pp. 51-59
    • Harada, A.1    Takei, Y.2    Kanai, Y.3    Tanaka, Y.4    Nonaka, S.5    Hirokawa, N.6
  • 60
    • 0030984076 scopus 로고    scopus 로고
    • Kinesin- and myosin-driven steps of vesicle recruitment for Ca2+-regulated exocytosis
    • Bi GQ, Morris RL, Liao G, Alderton JM, Scholey JM, Steinhardt RA: Kinesin- and myosin-driven steps of vesicle recruitment for Ca2+-regulated exocytosis. J Cell Biol 138(5): 999-1008, 1997
    • (1997) J Cell Biol , vol.138 , Issue.5 , pp. 999-1008
    • Bi, G.Q.1    Morris, R.L.2    Liao, G.3    Alderton, J.M.4    Scholey, J.M.5    Steinhardt, R.A.6
  • 61
    • 0036468983 scopus 로고    scopus 로고
    • Principles of cargo attachment to cytoplasmic motor proteins
    • Kamal A, Goldstein LS: Principles of cargo attachment to cytoplasmic motor proteins. Curr Opin Cell Biol 14(1): 63-68, 2002
    • (2002) Curr Opin Cell Biol , vol.14 , Issue.1 , pp. 63-68
    • Kamal, A.1    Goldstein, L.S.2
  • 62
    • 0028871742 scopus 로고
    • Point mutation of adenosine triphosphate-binding motif generated rigor kinesin that selectively blocks anterograde lysosome membrane transport
    • Nakata T, Hirokawa N: Point mutation of adenosine triphosphate-binding motif generated rigor kinesin that selectively blocks anterograde lysosome membrane transport. J Cell Biol 131(4): 1039-1053, 1995
    • (1995) J Cell Biol , vol.131 , Issue.4 , pp. 1039-1053
    • Nakata, T.1    Hirokawa, N.2
  • 63
    • 0026345106 scopus 로고
    • Regulation of kinesin expression and type IV collagenase secretion in invasive human prostate PC-3 tumor sublines
    • Stearns ME, Wang M: Regulation of kinesin expression and type IV collagenase secretion in invasive human prostate PC-3 tumor sublines. Cancer Res 51(21): 5866-5875, 1991
    • (1991) Cancer Res , vol.51 , Issue.21 , pp. 5866-5875
    • Stearns, M.E.1    Wang, M.2
  • 64
    • 0032531562 scopus 로고    scopus 로고
    • KIF2beta, a new kinesin super-family protein in non-neuronal cells, is associated with lysosomes and may be implicated in their centrifugal translocation
    • Santama N, Krijnse-Locker J, Griffiths G, Noda Y, Hirokawa N, Dotti CG: KIF2beta, a new kinesin super-family protein in non-neuronal cells, is associated with lysosomes and may be implicated in their centrifugal translocation. Embo J 17(20): 5855-5867, 1998
    • (1998) Embo J , vol.17 , Issue.20 , pp. 5855-5867
    • Santama, N.1    Krijnse-Locker, J.2    Griffiths, G.3    Noda, Y.4    Hirokawa, N.5    Dotti, C.G.6
  • 65
    • 0025147271 scopus 로고
    • Cathepsin D in breast cancer cells can digest extracellular matrix in large acidic vesicles
    • Montcourrier P, Mangeat PH, Salazar G, Morisset M, Sahuquet A, Rochefort H: Cathepsin D in breast cancer cells can digest extracellular matrix in large acidic vesicles. Cancer Res 50(18): 6045-6054, 1990
    • (1990) Cancer Res , vol.50 , Issue.18 , pp. 6045-6054
    • Montcourrier, P.1    Mangeat, P.H.2    Salazar, G.3    Morisset, M.4    Sahuquet, A.5    Rochefort, H.6
  • 66
    • 0027379702 scopus 로고
    • Targeted disruption of the mouse cation-dependent mannose 6-phosphate receptor results in partial missorting of multiple lysosomal enzymes
    • Ludwig T, Ovitt CE, Bauer U, Hollinshead M, Remmler J, Lobel P, Ruther U, Hoflack B: Targeted disruption of the mouse cation-dependent mannose 6-phosphate receptor results in partial missorting of multiple lysosomal enzymes. Embo J 12(13): 5225-5235, 1993
    • (1993) Embo J , vol.12 , Issue.13 , pp. 5225-5235
    • Ludwig, T.1    Ovitt, C.E.2    Bauer, U.3    Hollinshead, M.4    Remmler, J.5    Lobel, P.6    Ruther, U.7    Hoflack, B.8
  • 67
    • 0026730683 scopus 로고
    • Biosynthesis and endocytosis of lysosomal enzymes in human colon carcinoma SW 1116 cells: Impaired internalization of plasma membrane-associated cation-independent mannose 6-phosphate receptor
    • Braulke T, Mach L, Hoflack B, Glossl J: Biosynthesis and endocytosis of lysosomal enzymes in human colon carcinoma SW 1116 cells: Impaired internalization of plasma membrane-associated cation-independent mannose 6-phosphate receptor. Arch Biochem Biophys 298(1): 176-181, 1992
    • (1992) Arch Biochem Biophys , vol.298 , Issue.1 , pp. 176-181
    • Braulke, T.1    Mach, L.2    Hoflack, B.3    Glossl, J.4
  • 68
    • 0030943904 scopus 로고    scopus 로고
    • Differential sorting of lysosomal enzymes out of the regulated secretory pathway in pancreatic beta-cells
    • Kuliawat R, Klumperman J, Ludwig T, Arvan P: Differential sorting of lysosomal enzymes out of the regulated secretory pathway in pancreatic beta-cells. J Cell Biol 137(3): 595-608, 1997
    • (1997) J Cell Biol , vol.137 , Issue.3 , pp. 595-608
    • Kuliawat, R.1    Klumperman, J.2    Ludwig, T.3    Arvan, P.4
  • 69
    • 0033869531 scopus 로고    scopus 로고
    • Invasive properties of murine squamous carcinoma cells: Secretion of matrix-degrading cathepsins is attributable to a deficiency in the mannose 6-phosphate/insulin-like growth factor II receptor
    • Lorenzo K, Ton P, Clark JL, Coulibaly S, Mach L: Invasive properties of murine squamous carcinoma cells: secretion of matrix-degrading cathepsins is attributable to a deficiency in the mannose 6-phosphate/insulin-like growth factor II receptor. Cancer Res 60(15): 4070-4076, 2000
    • (2000) Cancer Res , vol.60 , Issue.15 , pp. 4070-4076
    • Lorenzo, K.1    Ton, P.2    Clark, J.L.3    Coulibaly, S.4    Mach, L.5
  • 70
    • 0028241106 scopus 로고
    • Distinct molecular mechanisms for protein sorting within immature secretory granules of pancreatic beta-cells
    • Kuliawat R, Arvan P: Distinct molecular mechanisms for protein sorting within immature secretory granules of pancreatic beta-cells. J Cell Biol 126(1): 77-86, 1994
    • (1994) J Cell Biol , vol.126 , Issue.1 , pp. 77-86
    • Kuliawat, R.1    Arvan, P.2
  • 71
    • 0030949251 scopus 로고    scopus 로고
    • Differentiation-induced changes in the content, secretion, and subcellular distribution of lysosomal cathepsins in the human colon cancer HT-29 cell line
    • De Stefanis D, Demoz M, Dragonetti A, Houri JJ, Ogier-Denis E, Codogno P, Baccino FM, Isidoro C: Differentiation-induced changes in the content, secretion, and subcellular distribution of lysosomal cathepsins in the human colon cancer HT-29 cell line. Cell Tissue Res 289(1): 109-117, 1997
    • (1997) Cell Tissue Res , vol.289 , Issue.1 , pp. 109-117
    • De Stefanis, D.1    Demoz, M.2    Dragonetti, A.3    Houri, J.J.4    Ogier-Denis, E.5    Codogno, P.6    Baccino, F.M.7    Isidoro, C.8
  • 72
    • 0031709904 scopus 로고    scopus 로고
    • Endocytosis of pro-cathepsin D into breast cancer cells is mostly independent of mannose-6-phosphate receptors
    • Laurent-Matha V, Farnoud MR, Lucas A, Rougeot C, Garcia M, Rochefort H: Endocytosis of pro-cathepsin D into breast cancer cells is mostly independent of mannose-6-phosphate receptors. J Cell Sci 111(Pt 17): 2539-2549, 1998
    • (1998) J Cell Sci , vol.111 , Issue.PART 17 , pp. 2539-2549
    • Laurent-Matha, V.1    Farnoud, M.R.2    Lucas, A.3    Rougeot, C.4    Garcia, M.5    Rochefort, H.6
  • 73
    • 0025743395 scopus 로고
    • Procathepsins L and D are membrane-bound in acidic microsomal vesicles
    • McIntyre GF, Erickson AH: Procathepsins L and D are membrane-bound in acidic microsomal vesicles. J Biol Chem 266(23): 15438-15445, 1991
    • (1991) J Biol Chem , vol.266 , Issue.23 , pp. 15438-15445
    • McIntyre, G.F.1    Erickson, A.H.2
  • 74
    • 0027491305 scopus 로고
    • The lysosomal proenzyme receptor that binds procathepsin L to microsomal membranes at pH 5 is a 43-kDa integral membrane protein
    • McIntyre GF, Erickson AH: The lysosomal proenzyme receptor that binds procathepsin L to microsomal membranes at pH 5 is a 43-kDa integral membrane protein. Proc Natl Acad Sci USA 90(22): 10588-10592, 1993
    • (1993) Proc Natl Acad Sci USA , vol.90 , Issue.22 , pp. 10588-10592
    • McIntyre, G.F.1    Erickson, A.H.2
  • 75
    • 0028125767 scopus 로고
    • The pH-dependent membrane association of procathepsin L is mediated by a 9-residue sequence within the propeptide
    • McIntyre GF, Godbold GD, Erickson AH: The pH-dependent membrane association of procathepsin L is mediated by a 9-residue sequence within the propeptide. J Biol Chem 269(1): 567-572, 1994
    • (1994) J Biol Chem , vol.269 , Issue.1 , pp. 567-572
    • McIntyre, G.F.1    Godbold, G.D.2    Erickson, A.H.3
  • 77
    • 0033567263 scopus 로고    scopus 로고
    • Exocytosis of active cathepsin B enzyme activity at pH 7.0, inhibition and molecular mass
    • Linebaugh BE, Sameni M, Day NA, Sloane BF, Keppler D: Exocytosis of active cathepsin B enzyme activity at pH 7.0, inhibition and molecular mass. Eur J Biochem 264(1): 100-109, 1999
    • (1999) Eur J Biochem , vol.264 , Issue.1 , pp. 100-109
    • Linebaugh, B.E.1    Sameni, M.2    Day, N.A.3    Sloane, B.F.4    Keppler, D.5
  • 78
    • 0034640306 scopus 로고    scopus 로고
    • Protein traffic from the secretory pathway to the endosomal system in pancreatic beta-cells
    • Turner MD, Arvan P: Protein traffic from the secretory pathway to the endosomal system in pancreatic beta-cells. J Biol Chem 275(19): 14025-14030, 2000
    • (2000) J Biol Chem , vol.275 , Issue.19 , pp. 14025-14030
    • Turner, M.D.1    Arvan, P.2
  • 79
    • 0024523485 scopus 로고
    • Changes in lysosome shape and distribution correlated with changes in cytoplasmic pH
    • Heuser J: Changes in lysosome shape and distribution correlated with changes in cytoplasmic pH. J Cell Biol 108(3): 855-864, 1989
    • (1989) J Cell Biol , vol.108 , Issue.3 , pp. 855-864
    • Heuser, J.1
  • 80
    • 0030008358 scopus 로고    scopus 로고
    • Host cell invasion by trypanosomes requires lysosomes and microtubule/kinesin-mediated transport
    • Rodriguez A, Samoff E, Rioult MG, Chung A, Andrews NW: Host cell invasion by trypanosomes requires lysosomes and microtubule/kinesin-mediated transport. J Cell Biol 134(2): 349-362, 1996
    • (1996) J Cell Biol , vol.134 , Issue.2 , pp. 349-362
    • Rodriguez, A.1    Samoff, E.2    Rioult, M.G.3    Chung, A.4    Andrews, N.W.5
  • 81
    • 0027049531 scopus 로고
    • Lysosome recruitment and fusion are early events required for trypanosome invasion of mammalian cells
    • Tardieux I, Webster P, Ravesloot J, Boron W, Lunn JA, Heuser JE, Andrews NW: Lysosome recruitment and fusion are early events required for trypanosome invasion of mammalian cells. Cell 71(7): 1117-1130, 1992
    • (1992) Cell , vol.71 , Issue.7 , pp. 1117-1130
    • Tardieux, I.1    Webster, P.2    Ravesloot, J.3    Boron, W.4    Lunn, J.A.5    Heuser, J.E.6    Andrews, N.W.7
  • 82
  • 83
    • 0030667637 scopus 로고    scopus 로고
    • Influence of 12(S)-hydroxyeicosatetraenoic acid (12(S)-HETE) on the localization of cathepsin B and cathepsin L in human lung tumor cells
    • Ulbricht B, Henny H, Horstmann H, Spring H, Faigle W, Spiess E: Influence of 12(S)-hydroxyeicosatetraenoic acid (12(S)-HETE) on the localization of cathepsin B and cathepsin L in human lung tumor cells. Eur J Cell Biol 74(3): 294-301, 1997
    • (1997) Eur J Cell Biol , vol.74 , Issue.3 , pp. 294-301
    • Ulbricht, B.1    Henny, H.2    Horstmann, H.3    Spring, H.4    Faigle, W.5    Spiess, E.6
  • 84
    • 0030837038 scopus 로고    scopus 로고
    • Selective induction of the secretion of cathepsins B and L by cytokines in synovial fibroblast-like cells
    • Lemaire R, Huet G, Zerimech F, Grard G, Fontaine C, Duquesnoy B, Flipo RM: Selective induction of the secretion of cathepsins B and L by cytokines in synovial fibroblast-like cells. Br J Rheumatol 36(7): 735-743, 1997
    • (1997) Br J Rheumatol , vol.36 , Issue.7 , pp. 735-743
    • Lemaire, R.1    Huet, G.2    Zerimech, F.3    Grard, G.4    Fontaine, C.5    Duquesnoy, B.6    Flipo, R.M.7
  • 85
    • 0037136311 scopus 로고    scopus 로고
    • Surface cathepsin B protects cytotoxic lymphocytes from self-destruction after degranulation
    • Balaji KN, Schaschke N, Machleidt W, Catalfamo M, Henkart PA: Surface cathepsin B protects cytotoxic lymphocytes from self-destruction after degranulation. J Exp Med 196(4): 493-503, 2002
    • (2002) J Exp Med , vol.196 , Issue.4 , pp. 493-503
    • Balaji, K.N.1    Schaschke, N.2    Machleidt, W.3    Catalfamo, M.4    Henkart, P.A.5
  • 86
    • 0029996240 scopus 로고    scopus 로고
    • Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells
    • Brix K, Lemansky P, Herzog V: Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells. Endocrinology 137(5): 1963-1974, 1996
    • (1996) Endocrinology , vol.137 , Issue.5 , pp. 1963-1974
    • Brix, K.1    Lemansky, P.2    Herzog, V.3
  • 87
    • 0035985060 scopus 로고    scopus 로고
    • Thyroid stimulating hormone upregulates secretion of cathepsin B from thyroid epithelial cells
    • Linke M, Jordans S, Mach L, Herzog V, Brix K: Thyroid stimulating hormone upregulates secretion of cathepsin B from thyroid epithelial cells. Biol Chem 383(5): 773-784, 2002
    • (2002) Biol Chem , vol.383 , Issue.5 , pp. 773-784
    • Linke, M.1    Jordans, S.2    Mach, L.3    Herzog, V.4    Brix, K.5
  • 89
    • 0030917299 scopus 로고    scopus 로고
    • Cathepsin B-like activity as a serum tumor marker in ovarian carcinoma
    • Warwas M, Haczynska H, Gerber J, Nowak M: Cathepsin B-like activity as a serum tumor marker in ovarian carcinoma. Eur J Clin Chem Clin Biochem 35(4): 301-304, 1997
    • (1997) Eur J Clin Chem Clin Biochem , vol.35 , Issue.4 , pp. 301-304
    • Warwas, M.1    Haczynska, H.2    Gerber, J.3    Nowak, M.4
  • 90
    • 0035156738 scopus 로고    scopus 로고
    • Plasma membrane association of cathepsin B in human prostate cancer: Biochemical and immunogold electron microscopic analysis
    • Sinha AA, Jamuar MP, Wilson MJ, Rozhin J, Sloane BF: Plasma membrane association of cathepsin B in human prostate cancer: Biochemical and immunogold electron microscopic analysis. Prostate 49(3): 172-184, 2001
    • (2001) Prostate , vol.49 , Issue.3 , pp. 172-184
    • Sinha, A.A.1    Jamuar, M.P.2    Wilson, M.J.3    Rozhin, J.4    Sloane, B.F.5
  • 91
    • 0028297896 scopus 로고
    • Human gastric adenocarcinoma cathepsin B: Isolation and sequencing of full-length cDNAs and polymorphisms of the gene
    • Cao L, Taggart RT, Berquin IM, Moin K, Fong D, Sloane BF: Human gastric adenocarcinoma cathepsin B: Isolation and sequencing of full-length cDNAs and polymorphisms of the gene. Gene 139(2): 163-169, 1994
    • (1994) Gene , vol.139 , Issue.2 , pp. 163-169
    • Cao, L.1    Taggart, R.T.2    Berquin, I.M.3    Moin, K.4    Fong, D.5    Sloane, B.F.6
  • 92
    • 0026729645 scopus 로고
    • Human tumor cathepsin B. Comparison with normal liver cathepsin B
    • Moin K, Day NA, Sameni M, Hasnain S, Hirama T, Sloane BF: Human tumor cathepsin B. Comparison with normal liver cathepsin B. Biochem J 285(Pt 2): 427-434, 1992
    • (1992) Biochem J , vol.285 , Issue.PART 2 , pp. 427-434
    • Moin, K.1    Day, N.A.2    Sameni, M.3    Hasnain, S.4    Hirama, T.5    Sloane, B.F.6
  • 95
    • 0029950355 scopus 로고    scopus 로고
    • Expression, subcellular distribution and plasma membrane binding of cathepsin B and gelatinases in bone metastatic tissue
    • Arkona C, Wiederanders B: Expression, subcellular distribution and plasma membrane binding of cathepsin B and gelatinases in bone metastatic tissue. Biol Chem 377(11): 695-702, 1996
    • (1996) Biol Chem , vol.377 , Issue.11 , pp. 695-702
    • Arkona, C.1    Wiederanders, B.2
  • 96
    • 0034725119 scopus 로고    scopus 로고
    • Human procathepsin B interacts with the annexin II tetramer on the surface of tumor cells
    • Mai J, Finley RL Jr, Waisman DM, Sloane BF: Human procathepsin B interacts with the annexin II tetramer on the surface of tumor cells. J Biol Chem 275(17): 12806-12812, 2000
    • (2000) J Biol Chem , vol.275 , Issue.17 , pp. 12806-12812
    • Mai, J.1    Finley R.L., Jr.2    Waisman, D.M.3    Sloane, B.F.4
  • 97
    • 0029669991 scopus 로고    scopus 로고
    • The S100 family of EF-hand calcium-binding proteins: Functions and pathology
    • Schafer BW, Heizmann CW: The S100 family of EF-hand calcium-binding proteins: Functions and pathology. Trends Biochem Sci 21(4): 134-140, 1996
    • (1996) Trends Biochem Sci , vol.21 , Issue.4 , pp. 134-140
    • Schafer, B.W.1    Heizmann, C.W.2
  • 98
    • 0027094236 scopus 로고
    • The tight association of the tyrosine kinase substrate annexin II with the submembranous cytoskeleton depends on intact p11- and Ca(2+)-binding sites
    • Thiel C, Osborn M, Gerke V: The tight association of the tyrosine kinase substrate annexin II with the submembranous cytoskeleton depends on intact p11- and Ca(2+)-binding sites. J Cell Sci 103(Pt 3): 733-742, 1992
    • (1992) J Cell Sci , vol.103 , Issue.PART 3 , pp. 733-742
    • Thiel, C.1    Osborn, M.2    Gerke, V.3
  • 99
    • 0027140743 scopus 로고
    • Enhanced expression of annexin II in human pancreatic carcinoma cells and primary pancreatic cancers
    • Vishwanatha JK, Chiang Y, Kumble KD, Hollingsworth MA, Pour PM: Enhanced expression of annexin II in human pancreatic carcinoma cells and primary pancreatic cancers. Carcinogenesis 14(12): 2575-2579, 1993
    • (1993) Carcinogenesis , vol.14 , Issue.12 , pp. 2575-2579
    • Vishwanatha, J.K.1    Chiang, Y.2    Kumble, K.D.3    Hollingsworth, M.A.4    Pour, P.M.5
  • 100
    • 0026587708 scopus 로고
    • Enhanced levels of annexins in pancreatic carcinoma cells of Syrian hamsters and their intrapancreatic allografts
    • Kumble KD, Hirota M, Pour PM, Vishwanatha JK: Enhanced levels of annexins in pancreatic carcinoma cells of Syrian hamsters and their intrapancreatic allografts. Cancer Res 52(1): 163-167, 1992
    • (1992) Cancer Res , vol.52 , Issue.1 , pp. 163-167
    • Kumble, K.D.1    Hirota, M.2    Pour, P.M.3    Vishwanatha, J.K.4
  • 101
    • 0026513632 scopus 로고
    • Elevated expression of annexin II (lipocortin II, p36) in a multidrug resistant small cell lung cancer cell line
    • Cole SP, Pinkoski MJ, Bhardwaj G, Deeley RG: Elevated expression of annexin II (lipocortin II, p36) in a multidrug resistant small cell lung cancer cell line. Br J Cancer 65(4): 498-502, 1992
    • (1992) Br J Cancer , vol.65 , Issue.4 , pp. 498-502
    • Cole, S.P.1    Pinkoski, M.J.2    Bhardwaj, G.3    Deeley, R.G.4
  • 102
    • 0027092615 scopus 로고
    • Developmental regulation of annexin II (Lipocortin 2) in human brain and expression in high grade glioma
    • Reeves SA, Chavez-Kappel C, Davis R, Rosenblum M, Israel MA: Developmental regulation of annexin II (Lipocortin 2) in human brain and expression in high grade glioma. Cancer Res 52(24): 6871-6876, 1992
    • (1992) Cancer Res , vol.52 , Issue.24 , pp. 6871-6876
    • Reeves, S.A.1    Chavez-Kappel, C.2    Davis, R.3    Rosenblum, M.4    Israel, M.A.5
  • 103
    • 0028633553 scopus 로고
    • Annexin II marks astrocytic brain tumors of high histologic grade
    • Roseman BJ, Bollen A, Hsu J, Lamborn K, Israel MA: Annexin II marks astrocytic brain tumors of high histologic grade. Oncol Res 6(12): 561-567, 1994
    • (1994) Oncol Res , vol.6 , Issue.12 , pp. 561-567
    • Roseman, B.J.1    Bollen, A.2    Hsu, J.3    Lamborn, K.4    Israel, M.A.5
  • 104
    • 0030580097 scopus 로고    scopus 로고
    • Altered expression of annexin II in human B-cell lymphoma cell lines
    • Chiang Y, Davis RG, Vishwanatha JK: Altered expression of annexin II in human B-cell lymphoma cell lines. Biochim Biophys Acta 1313(3): 295-301, 1996
    • (1996) Biochim Biophys Acta , vol.1313 , Issue.3 , pp. 295-301
    • Chiang, Y.1    Davis, R.G.2    Vishwanatha, J.K.3
  • 105
    • 0027462446 scopus 로고
    • Expression of annexins on the surfaces of non-metastatic and metastatic human and rodent tumor cells
    • Yeatman TJ, Updyke TV, Kaetzel MA, Dedman JR, Nicolson GL: Expression of annexins on the surfaces of non-metastatic and metastatic human and rodent tumor cells. Clin Exp Metastasis 11(1): 37-44, 1993
    • (1993) Clin Exp Metastasis , vol.11 , Issue.1 , pp. 37-44
    • Yeatman, T.J.1    Updyke, T.V.2    Kaetzel, M.A.3    Dedman, J.R.4    Nicolson, G.L.5
  • 106
  • 107
    • 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(3): 511-522, 1990
    • (1990) J Cell Physiol , vol.144 , Issue.3 , pp. 511-522
    • Wirl, G.1    Schwartz-Albiez, R.2
  • 108
    • 0028305739 scopus 로고
    • Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C
    • Chung CY, Erickson HP: Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C. J Cell Biol 126(2): 539-548, 1994
    • (1994) J Cell Biol , vol.126 , Issue.2 , pp. 539-548
    • Chung, C.Y.1    Erickson, H.P.2
  • 110
    • 0028023538 scopus 로고
    • An endothelial cell receptor for plasminogen/tissue plasminogen activator. I. Identity with annexin 11
    • Hajjar KA, Jacovina AT, Chacko J: An endothelial cell receptor for plasminogen/tissue plasminogen activator. I. Identity with annexin 11. J Biol Chem 269(33): 21191-21197, 1994
    • (1994) J Biol Chem , vol.269 , Issue.33 , pp. 21191-21197
    • Hajjar, K.A.1    Jacovina, A.T.2    Chacko, J.3
  • 111
    • 0027275642 scopus 로고
    • Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells
    • Sargiacomo M, Sudol M, Tang Z, Lisanti MP: Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells. J Cell Biol 122(4): 789-807, 1993
    • (1993) J Cell Biol , vol.122 , Issue.4 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.3    Lisanti, M.P.4
  • 112
    • 0028060685 scopus 로고
    • The annexin 112p11(2) complex is the major protein component of the triton X-100-insoluble low-density fraction prepared from MDCK cells in the presence of Ca2+
    • Harder T, Gerke V: The annexin 112p11(2) complex is the major protein component of the triton X-100-insoluble low-density fraction prepared from MDCK cells in the presence of Ca2+. Biochim Biophys Acta 1223(3): 375-382, 1994
    • (1994) Biochim Biophys Acta , vol.1223 , Issue.3 , pp. 375-382
    • Harder, T.1    Gerke, V.2
  • 113
    • 0032498628 scopus 로고    scopus 로고
    • Caveolin transfection results in caveolae formation but not apical sorting of glycosylphosphatidylinositol (GPI)-anchored proteins in epithelial cells
    • Lipardi C, Mora R, Colomer V, Paladino S, Nitsch L, Rodriguez-Boulan E, Zurzolo C: Caveolin transfection results in caveolae formation but not apical sorting of glycosylphosphatidylinositol (GPI)-anchored proteins in epithelial cells. J Cell Biol 140(3): 617-626, 1998
    • (1998) J Cell Biol , vol.140 , Issue.3 , pp. 617-626
    • Lipardi, C.1    Mora, R.2    Colomer, V.3    Paladino, S.4    Nitsch, L.5    Rodriguez-Boulan, E.6    Zurzolo, C.7
  • 116
    • 0035153475 scopus 로고    scopus 로고
    • Elevated expression of caveolin-1 in adenocarcinoma of the colon
    • Fine SW, Lisanti MP, Galbiati F, Li M: Elevated expression of caveolin-1 in adenocarcinoma of the colon. Am J Clin Patho1 115(5): 719-724, 2001
    • (2001) Am J Clin Patho1 , vol.115 , Issue.5 , pp. 719-724
    • Fine, S.W.1    Lisanti, M.P.2    Galbiati, F.3    Li, M.4
  • 117
    • 0033571471 scopus 로고    scopus 로고
    • Caveolin-1 expression in clinically confined human prostate cancer: A novel prognostic marker
    • Yang G, Truong LD, Wheeler TM, Thompson TC: Caveolin-1 expression in clinically confined human prostate cancer: A novel prognostic marker. Cancer Res 59(22): 5719-5723, 1999
    • (1999) Cancer Res , vol.59 , Issue.22 , pp. 5719-5723
    • Yang, G.1    Truong, L.D.2    Wheeler, T.M.3    Thompson, T.C.4
  • 118
    • 0028944244 scopus 로고
    • The urokinase-type plasminogen activator receptor, a GPI-linked protein, is localized in caveolae
    • Stahl A, Mueller BM: The urokinase-type plasminogen activator receptor, a GPI-linked protein, is localized in caveolae. J Cell Biol 129(2): 335-344, 1995
    • (1995) J Cell Biol , vol.129 , Issue.2 , pp. 335-344
    • Stahl, A.1    Mueller, B.M.2
  • 119
    • 0035252979 scopus 로고    scopus 로고
    • Localization of membrane-type 1 matrix metalloproteinase in caveolae membrane domains
    • Annabi B, Lachambre M, Bousquet-Gagnon N, Page M, Gingras D, Beliveau R: Localization of membrane-type 1 matrix metalloproteinase in caveolae membrane domains. Biochem J 353(Pt 3): 547-553, 2001
    • (2001) Biochem J , vol.353 , Issue.PART 3 , pp. 547-553
    • Annabi, B.1    Lachambre, M.2    Bousquet-Gagnon, N.3    Page, M.4    Gingras, D.5    Beliveau, R.6
  • 120
  • 121
    • 0026575258 scopus 로고
    • Degradation of extracellular-matrix proteins by human cathepsin B from normal and tumor tissues
    • Buck MR, Karustis DG, Day NA, Honn KV, Sloane BF: Degradation of extracellular-matrix proteins by human cathepsin B from normal and tumor tissues. Biochem J 282(Pt 1): 273-278, 1992
    • (1992) Biochem J , vol.282 , Issue.PART 1 , pp. 273-278
    • Buck, M.R.1    Karustis, D.G.2    Day, N.A.3    Honn, K.V.4    Sloane, B.F.5
  • 123
    • 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 SP, Malhothra R, Banner BF: Cathepsin B expression and its correlation with tumor-associated laminin and tumor progression in gastric cancer. Arch Pathol Lab Med 122(2): 172-177, 1998
    • (1998) Arch Pathol Lab Med , vol.122 , Issue.2 , pp. 172-177
    • Khan, A.1    Krishna, M.2    Baker, S.P.3    Malhothra, R.4    Banner, B.F.5
  • 124
    • 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(1): 46-51, 1994
    • (1994) Cancer , vol.74 , Issue.1 , pp. 46-51
    • Sukoh, N.1    Abe, S.2    Ogura, S.3    Isobe, H.4    Takekawa, H.5    Inoue, K.6    Kawakami, Y.7
  • 125
    • 0027463459 scopus 로고
    • Cathepsin B expression in tumor cells and laminin distribution in pulmonary adenocarcinoma
    • Higashiyama M, Doi O, Kodama K, Yokouchi H, Tateishi R: Cathepsin B expression in tumor cells and laminin distribution in pulmonary adenocarcinoma. J Clin Pathol 46(1): 18-22, 1993
    • (1993) J Clin Pathol , vol.46 , Issue.1 , pp. 18-22
    • Higashiyama, M.1    Doi, O.2    Kodama, K.3    Yokouchi, H.4    Tateishi, R.5
  • 126
    • 0034930565 scopus 로고    scopus 로고
    • Imaging proteolysis by living human glioma cells
    • Sameni M, Dosescu J, Sloane BF: Imaging proteolysis by living human glioma cells. Biol Chem 382(5): 785-788, 2001
    • (2001) Biol Chem , vol.382 , Issue.5 , pp. 785-788
    • Sameni, M.1    Dosescu, J.2    Sloane, B.F.3
  • 127
    • 0034486945 scopus 로고    scopus 로고
    • Imaging proteolysis by living human breast cancer cells
    • Sameni M, Moin K, Sloane BF: Imaging proteolysis by living human breast cancer cells. Neoplasia 2(6): 496-504, 2000
    • (2000) Neoplasia , vol.2 , Issue.6 , pp. 496-504
    • Sameni, M.1    Moin, K.2    Sloane, B.F.3
  • 128
    • 0034615565 scopus 로고    scopus 로고
    • Cell surface complex of cathepsin B/annexin II tetramer in malignant progression
    • Mai J, Waisman DM, Sloane BF: Cell surface complex of cathepsin B/annexin II tetramer in malignant progression. Biochim Biophys Acta 1477(1-2): 215-230, 2000
    • (2000) Biochim Biophys Acta , vol.1477 , Issue.1-2 , pp. 215-230
    • Mai, J.1    Waisman, D.M.2    Sloane, B.F.3
  • 129
    • 0027319177 scopus 로고
    • Characterization of the cathepsin B gene and multiple mRNAs in human tissues: Evidence for alternative splicing of cathepsin B pre-mRNA
    • Gong Q, Chan SJ, Bajkowski AS, Steiner DF, Frankfater A: Characterization of the cathepsin B gene and multiple mRNAs in human tissues: evidence for alternative splicing of cathepsin B pre-mRNA. DNA Cell Biol 12(4): 299-309, 1993
    • (1993) DNA Cell Biol , vol.12 , Issue.4 , pp. 299-309
    • Gong, Q.1    Chan, S.J.2    Bajkowski, A.S.3    Steiner, D.F.4    Frankfater, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.