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Volumn 29, Issue 10, 1997, Pages 727-734

Ultrastructural localization of cathepsin B in gingival tissue from chronic periodontitis patients

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN B; GOLD DERIVATIVE; POLYCLONAL ANTIBODY;

EID: 0031438087     PISSN: 00182214     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1026465118281     Document Type: Article
Times cited : (13)

References (43)
  • 2
    • 0001310293 scopus 로고
    • Cathepsin B and other thiol proteinases
    • (edited by BARRETT, A.J.). Amsterdam: Elsevier/North Holland Biomedical Press
    • BARRETT, A.J. (1977) Cathepsin B and other thiol proteinases. In Proteinases in Mammalian Cells and Tissues (edited by BARRETT, A.J.). pp. 181-208. Amsterdam: Elsevier/North Holland Biomedical Press.
    • (1977) Proteinases in Mammalian Cells and Tissues , pp. 181-208
    • Barrett, A.J.1
  • 3
    • 0026575258 scopus 로고
    • Degradation of extracellular matrix proteins by human cathepsin B from normal and tumor tissues
    • BUCK, M.R., KARUTIS, D.G., DAY, N.A., HONN, K.V. & SLOANE, B.F. (1992) Degradation of extracellular matrix proteins by human cathepsin B from normal and tumor tissues. Biochem. J. 282, 273-8.
    • (1992) Biochem. J. , vol.282 , pp. 273-278
    • Buck, M.R.1    Karutis, D.G.2    Day, N.A.3    Honn, K.V.4    Sloane, B.F.5
  • 4
    • 0015984017 scopus 로고
    • Cathepsin B1 - A lysosomal enzyme that degrades native collagen
    • BURLEIGH, M.C., BARRETT, A.J. & LAZARUS, G.S. (1974) Cathepsin B1 - a lysosomal enzyme that degrades native collagen. Biochem. J. 137, 387-98.
    • (1974) Biochem. J. , vol.137 , pp. 387-398
    • Burleigh, M.C.1    Barrett, A.J.2    Lazarus, G.S.3
  • 5
    • 0015790915 scopus 로고
    • Fine structural localization of acid and alkaline phosphatase in collagen containing vesicles of fibroblasts
    • DEPORTER, D. & TEN CATE, A. (1973) Fine structural localization of acid and alkaline phosphatase in collagen containing vesicles of fibroblasts. J. Anat. 114, 457-61.
    • (1973) J. Anat. , vol.114 , pp. 457-461
    • Deporter, D.1    Ten Cate, A.2
  • 6
    • 0026211362 scopus 로고
    • Cathepsin B- and L-like activities at local gingival sites of chronic periodontitis patients
    • ELEY, B.M. & COX, S.W. (1991) Cathepsin B- and L-like activities at local gingival sites of chronic periodontitis patients. J. Clin. Periodontol. 18, 499-504.
    • (1991) J. Clin. Periodontol. , vol.18 , pp. 499-504
    • Eley, B.M.1    Cox, S.W.2
  • 7
    • 0030207881 scopus 로고    scopus 로고
    • The relationship between gingival crevicular fluid cathepsin B activity and periodontal attachment loss in chronic periodontitis patients: A 2 year longitudinal study
    • ELEY, B.M. & COX, S.W. (1996) The relationship between gingival crevicular fluid cathepsin B activity and periodontal attachment loss in chronic periodontitis patients: a 2 year longitudinal study. J. Periodont. Res. 31, 381-92.
    • (1996) J. Periodont. Res. , vol.31 , pp. 381-392
    • Eley, B.M.1    Cox, S.W.2
  • 8
    • 0016525355 scopus 로고
    • Intracellular collagen fibrils in the periodontal ligament of man
    • ELEY, B.M. & HARRISON, J.D. (1975) Intracellular collagen fibrils in the periodontal ligament of man. J. Periodont. Res. 10, 168-70.
    • (1975) J. Periodont. Res. , vol.10 , pp. 168-170
    • Eley, B.M.1    Harrison, J.D.2
  • 10
    • 0021929277 scopus 로고
    • The digestion of phagocytosed collagen is inhibited by the proteinase inhibitors leupeptin and E-64
    • EVERTS, V., BEERTSEN, W. & TIGCHELAAR-GUTTER, W. (1985) The digestion of phagocytosed collagen is inhibited by the proteinase inhibitors leupeptin and E-64. Coll. Rel. Res. 5, 315-36.
    • (1985) Coll. Rel. Res. , vol.5 , pp. 315-336
    • Everts, V.1    Beertsen, W.2    Tigchelaar-Gutter, W.3
  • 11
    • 8944249294 scopus 로고    scopus 로고
    • Phagocytosis and intracellular digestion of collagen, its role in turnover and remodelling
    • EVERTS, V., VAN DER ZEE, E., CREEMERS, L. & BEERTSEN, W. (1996) Phagocytosis and intracellular digestion of collagen, its role in turnover and remodelling. Histochem. J. 28, 229-245.
    • (1996) Histochem. J. , vol.28 , pp. 229-245
    • Everts, V.1    Van Der Zee, E.2    Creemers, L.3    Beertsen, W.4
  • 13
    • 0018687057 scopus 로고
    • The fluorescence and bright field demonstration of cathepsin B in human fibroblasts
    • GRAF, M., LEEMANN, U., RUCH, F. & STRÄULI, P. (1979) The fluorescence and bright field demonstration of cathepsin B in human fibroblasts. Histochemistry 64, 319-22.
    • (1979) Histochemistry , vol.64 , pp. 319-322
    • Graf, M.1    Leemann, U.2    Ruch, F.3    Sträuli, P.4
  • 14
    • 0019783571 scopus 로고
    • Histochemical localization of cathepsin B at the invasion front of the rabbit V2 carcinoma
    • GRAF, M., BAICI, A. & STRÄULI, P. (1981) Histochemical localization of cathepsin B at the invasion front of the rabbit V2 carcinoma. Lab. Invest. 45, 587-96.
    • (1981) Lab. Invest. , vol.45 , pp. 587-596
    • Graf, M.1    Baici, A.2    Sträuli, P.3
  • 15
    • 0025423520 scopus 로고
    • 'In vitro' digestion of intact bovine lens capsules by four lysosomal cysteine-proteinases
    • GUINEC, N., PAGANO, M., DALET-FUMERON, V. & ENGLER, R. (1990) 'In vitro' digestion of intact bovine lens capsules by four lysosomal cysteine-proteinases. Biol. Chem. Hoppe Seyler 371 (Suppl.), 239-54.
    • (1990) Biol. Chem. Hoppe Seyler , vol.371 , Issue.SUPPL. , pp. 239-254
    • Guinec, N.1    Pagano, M.2    Dalet-Fumeron, V.3    Engler, R.4
  • 16
    • 0023645465 scopus 로고
    • Biosynthesis of cathepsin B in cultured normal and I-cell fibroblasts
    • HANEWINKEL, H., GLOSSL, J. & KRESSE, H. (1987) Biosynthesis of cathepsin B in cultured normal and I-cell fibroblasts. J. Biol. Chem. 262, 12351-5.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12351-12355
    • Hanewinkel, H.1    Glossl, J.2    Kresse, H.3
  • 17
    • 0028432706 scopus 로고
    • Comparative histochemical, biochemical and immunocytochemical studies of cathepsin B in human gingiva
    • KENNETT, C.N., COX, S.W., & ELEY, B.M. (1994) Comparative histochemical, biochemical and immunocytochemical studies of cathepsin B in human gingiva. J. Periodont. Res. 29, 203-13.
    • (1994) J. Periodont. Res. , vol.29 , pp. 203-213
    • Kennett, C.N.1    Cox, S.W.2    Eley, B.M.3
  • 18
    • 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., GÜNZLER, W.A., JÄNICKE, F. & GRAEFF, H. (1991) 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, 5147-52.
    • (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    Günzler, W.A.7    Jänicke, F.8    Graeff, H.9
  • 19
    • 0023116652 scopus 로고
    • Cytochemical and biochemical evidence of cathepsin B in malignant, transformed and normal breast epithelial cells
    • KREPELA, E., BARTEK, J., SKALKOVA, D., VICAR, J., RASNICK, D., TAYLOR-PAPADIMITRIOU, J. & HALLOWES, R.C. (1987) Cytochemical and biochemical evidence of cathepsin B in malignant, transformed and normal breast epithelial cells. J. Cell Sci. 87, 145-54.
    • (1987) J. Cell Sci. , vol.87 , pp. 145-154
    • Krepela, E.1    Bartek, J.2    Skalkova, D.3    Vicar, J.4    Rasnick, D.5    Taylor-Papadimitriou, J.6    Hallowes, R.C.7
  • 20
    • 0025061478 scopus 로고
    • Susceptibility of the cartilage collagens types II, IX and XI to degradation by the cysteine proteinases, cathepsins B and L
    • MACIEWICZ, R.A., WOTTON, S.F., ETHERINGTON, D.J. & DUANCE, V.C. (1990) Susceptibility of the cartilage collagens types II, IX and XI to degradation by the cysteine proteinases, cathepsins B and L. FEBS Lett. 269, 189-93.
    • (1990) FEBS Lett. , vol.269 , pp. 189-193
    • Maciewicz, R.A.1    Wotton, S.F.2    Etherington, D.J.3    Duance, V.C.4
  • 21
    • 0021797883 scopus 로고
    • Cathepsin B activity in human blood monocytes during differentiation in vitro
    • MORLAND, B. (1985) Cathepsin B activity in human blood monocytes during differentiation in vitro. Scand. J. Immunol. 22, 9-16.
    • (1985) Scand. J. Immunol. , vol.22 , pp. 9-16
    • Morland, B.1
  • 22
    • 0018639923 scopus 로고
    • Cathepsin B activity in stimulated mouse peritoneal macrophages
    • MORLAND, B. & PEDERSEN, A. (1979) Cathepsin B activity in stimulated mouse peritoneal macrophages. Lab. Invest. 41, 379-84.
    • (1979) Lab. Invest. , vol.41 , pp. 379-384
    • Morland, B.1    Pedersen, A.2
  • 23
    • 0015921502 scopus 로고
    • Cathepsins B1 and D. Action on human cartilage proteoglycans
    • MORRISON, R., BARRETT, A., DINGLE, J. & PRIOR, D. (1973) Cathepsins B1 and D. Action on human cartilage proteoglycans. Biochim. Biophys. Acta 302, 411-19.
    • (1973) Biochim. Biophys. Acta , vol.302 , pp. 411-419
    • Morrison, R.1    Barrett, A.2    Dingle, J.3    Prior, D.4
  • 24
    • 0019497034 scopus 로고
    • Immunofluorescent localization of cathepsins B and D in human fibroblasts
    • MORT, J.S., POOLE, A.R. & DECKER, R.S. (1981) Immunofluorescent localization of cathepsins B and D in human fibroblasts. J. Histochem. Cytochem. 29, 649-57.
    • (1981) J. Histochem. Cytochem. , vol.29 , pp. 649-657
    • Mort, J.S.1    Poole, A.R.2    Decker, R.S.3
  • 25
    • 0021344717 scopus 로고
    • Extracellular presence of the lysosomal proteinase cathepsin B in rheumatoid synovium and its activity at neutral pH
    • MORT, J.S., RECKLIES, A.D. & POOLE, A.R. (1984) Extracellular presence of the lysosomal proteinase cathepsin B in rheumatoid synovium and its activity at neutral pH. Arthr. Rheum. 27, 509-15.
    • (1984) Arthr. Rheum. , vol.27 , pp. 509-515
    • Mort, J.S.1    Recklies, A.D.2    Poole, A.R.3
  • 26
    • 0025811915 scopus 로고
    • The role of inflammatory mediators in the pathogenesis of periodontal disease
    • PAGE, R. (1991) The role of inflammatory mediators in the pathogenesis of periodontal disease. J. Periodont. Res. 26, 230-42.
    • (1991) J. Periodont. Res. , vol.26 , pp. 230-242
    • Page, R.1
  • 27
    • 0025051964 scopus 로고
    • Modulation of the transport of a lysosomal enzyme by PDGF
    • PRENCE, E.M., DONG, J. & SAHAGIAN, G.G. (1990) Modulation of the transport of a lysosomal enzyme by PDGF. J. Cell Biol. 100, 319-26.
    • (1990) J. Cell Biol. , vol.100 , pp. 319-326
    • Prence, E.M.1    Dong, J.2    Sahagian, G.G.3
  • 28
    • 0029007093 scopus 로고
    • Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages
    • REDDY, V.Y., ZHANG, Q.-Y. & WEISS, S.J. (1995) Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages. Proc. Natl. Acad. Sci. USA 92, 3849-53.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3849-3853
    • Reddy, V.Y.1    Zhang, Q.-Y.2    Weiss, S.J.3
  • 29
    • 52649114611 scopus 로고
    • The use of lead citrate at high pH as an electron opaque stain in electron microscopy
    • REYNOLDS, E.S. (1963) The use of lead citrate at high pH as an electron opaque stain in electron microscopy. J. Cell Biol. 17, 208-12.
    • (1963) J. Cell Biol. , vol.17 , pp. 208-212
    • Reynolds, E.S.1
  • 30
    • 0026728142 scopus 로고
    • An appraisal of low-temperature embedding by progressive lowering of temperature into Lowicryl HM20 for immunocytochemical studies
    • ROBERTSON, D., MONAGHAN, P., CLARKE, C. & ATHERTON, A.J. (1992) An appraisal of low-temperature embedding by progressive lowering of temperature into Lowicryl HM20 for immunocytochemical studies. J. Microscopy 168, 85-100.
    • (1992) J. Microscopy , vol.168 , pp. 85-100
    • Robertson, D.1    Monaghan, P.2    Clarke, C.3    Atherton, A.J.4
  • 31
    • 0022596874 scopus 로고
    • Proteases and their inhibitors in chronic inflammatory periodontal disease
    • SANDHOLM, L. (1986) Proteases and their inhibitors in chronic inflammatory periodontal disease. J. Clin. Periodontol. 13, 19-26.
    • (1986) J. Clin. Periodontol. , vol.13 , pp. 19-26
    • Sandholm, L.1
  • 32
    • 0027340176 scopus 로고
    • Cystein-proteinase localization in osteoclasts: An immunocytochemical study
    • SASAKI, T. & UENO-MATSUDA, E. (1993) Cystein-proteinase localization in osteoclasts: an immunocytochemical study. Cell Tissue Res. 271, 177-9.
    • (1993) Cell Tissue Res. , vol.271 , pp. 177-179
    • Sasaki, T.1    Ueno-Matsuda, E.2
  • 33
    • 0023882543 scopus 로고
    • Microelectrode studies on the acid environment beneath adherent macrophages and osteoclasts
    • SILVER, I.A., MURRILLS, R.J. & ETHERINGTON, D.J. (1988) Microelectrode studies on the acid environment beneath adherent macrophages and osteoclasts. Exp. Cell Res. 175, 266-75.
    • (1988) Exp. Cell Res. , vol.175 , pp. 266-275
    • Silver, I.A.1    Murrills, R.J.2    Etherington, D.J.3
  • 34
    • 84939684025 scopus 로고
    • Plasma membrane-associated cysteine proteinases in human and animal tumors
    • SLOANE, B.F., ROZHIN, J., HATFIELD, J.S., CRISSMAN, J.D. & HONN, K.V. (1987) Plasma membrane-associated cysteine proteinases in human and animal tumors. Exp. Cell Biol. 55, 209-24.
    • (1987) Exp. Cell Biol. , vol.55 , pp. 209-224
    • Sloane, B.F.1    Rozhin, J.2    Hatfield, J.S.3    Crissman, J.D.4    Honn, K.V.5
  • 35
    • 0025676568 scopus 로고
    • Cathepsin B and its endogenous inhibitors: The role in tumor malignancy
    • SLOANE, B.F., MOIN, K., KREPELA, E. & ROZHIN, J. (1990) Cathepsin B and its endogenous inhibitors: the role in tumor malignancy. Cancer Metastasis Rev. 9, 333-52.
    • (1990) Cancer Metastasis Rev. , vol.9 , pp. 333-352
    • Sloane, B.F.1    Moin, K.2    Krepela, E.3    Rozhin, J.4
  • 36
    • 0028273525 scopus 로고
    • Membrane association of cathepsin B can be induced by transinfection of human breast epithelial cells with c-Ha-ras oncogene
    • SLOANE, B.F., MOIN, K., SAMENI, M., TAIT, L.R., ROZHIN, J. & ZIEGLER, G. (1994) Membrane association of cathepsin B can be induced by transinfection of human breast epithelial cells with c-Ha-ras oncogene. J. Cell Sci. 107, 373-84.
    • (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
  • 37
    • 0028341492 scopus 로고
    • Cathepsin B activity in human lung tumor cell lines: Ultrastructural localization, pH sensitivity, and inhibitor status at the cellular level
    • SPIESS, E., BRUNlNG, A., GACK, S., ULBRICHT, B., SPRING, H., TREFZ, G. & EBERT, W. (1994) Cathepsin B activity in human lung tumor cell lines: ultrastructural localization, pH sensitivity, and inhibitor status at the cellular level. J. Histochem. Cytochem. 42, 917-29.
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 917-929
    • Spiess, E.1    Brunlng, A.2    Gack, S.3    Ulbricht, B.4    Spring, H.5    Trefz, G.6    Ebert, W.7
  • 38
    • 0022407152 scopus 로고
    • The subcellular localization of soluble and membrane bound lysosomal enzymes in I-cell fibroblasts: A comparative immunocytochemical study
    • VAN DONGEN, J.M., WILLENSEN, R., GINNS, E.I., SIPS, H.J., TAGER, J.M., BARRANGER, J.A. & REUSER, A.J.J. (1985) The subcellular localization of soluble and membrane bound lysosomal enzymes in I-cell fibroblasts: a comparative immunocytochemical study. Eur. J. Cell Biol. 39, 179-89.
    • (1985) Eur. J. Cell Biol. , vol.39 , pp. 179-189
    • Van Dongen, J.M.1    Willensen, R.2    Ginns, E.I.3    Sips, H.J.4    Tager, J.M.5    Barranger, J.A.6    Reuser, A.J.J.7
  • 40
    • 0023510163 scopus 로고
    • Localization of cathepsin B activity in fibroblasts and chondrocytes by continuous monitoring of the formation of a final fluorescent reaction product using 5-nitrosalicylaldehyde
    • VAN NOORDEN, C.J.F., VOGELS, I.M.C., EVERTS, V. & BEERTSEN, W. (1987) Localization of cathepsin B activity in fibroblasts and chondrocytes by continuous monitoring of the formation of a final fluorescent reaction product using 5-nitrosalicylaldehyde. Histochem. J. 19, 483-7.
    • (1987) Histochem. J. , vol.19 , pp. 483-487
    • Van Noorden, C.J.F.1    Vogels, I.M.C.2    Everts, V.3    Beertsen, W.4
  • 43
    • 0019862162 scopus 로고
    • Demonstration of membrane-bound proteolytic activity on the surface of mononuclear leukocytes
    • ZUCKER-FRANKLIN, D., LAVIE, G. & FRANKLIN, E.C. (1981) Demonstration of membrane-bound proteolytic activity on the surface of mononuclear leukocytes. J. Histochem. Cytochem. 29, 451-6.
    • (1981) J. Histochem. Cytochem. , vol.29 , pp. 451-456
    • Zucker-Franklin, D.1    Lavie, G.2    Franklin, E.C.3


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