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Volumn 74, Issue 3, 1997, Pages 294-301

Influence of 12(S)-hydroxyeicosatetraenoic acid (12(S)-HETE) on the localization of cathepsin B and cathepsin L in human lung tumor cells

Author keywords

12(S) HETE; Cathepsin B; Cathepsin L; Localization; Lung cells

Indexed keywords

CATHEPSIN B; CATHEPSIN L; HYDROXYICOSATETRAENOIC ACID; SOMATOMEDIN B RECEPTOR;

EID: 0030667637     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (20)

References (43)
  • 1
    • 0029896938 scopus 로고    scopus 로고
    • Cathepsin b activity in normal human osteoblast-like cells and human osteoblastic osteosarcoma cells (MG-63): Regulation by interleukin-1 beta and parathyroid hormone
    • Aisa, M. C., S. Rahman, U. Senin, D. Maggio, R. G. G. Russell: Cathepsin b activity in normal human osteoblast-like cells and human osteoblastic osteosarcoma cells (MG-63): regulation by interleukin-1 beta and parathyroid hormone. Biochim. Biophys. Acta-Gene Subjects 1290, 29-36 (1996).
    • (1996) Biochim. Biophys. Acta-Gene Subjects , vol.1290 , pp. 29-36
    • Aisa, M.C.1    Rahman, S.2    Senin, U.3    Maggio, D.4    Russell, R.G.G.5
  • 2
    • 0023904014 scopus 로고
    • Characterization of the state of differentiation of six newly established human non-small-cell lung cancer cell lines
    • Bepler, G., A. Koehler, P. Kiefer, K. Havemann, K. Beisenherz, G. Jacques, C. Gropp, M. Haeder: Characterization of the state of differentiation of six newly established human non-small-cell lung cancer cell lines. Differentiation 37, 158-171 (1988).
    • (1988) Differentiation , vol.37 , pp. 158-171
    • Bepler, G.1    Koehler, A.2    Kiefer, P.3    Havemann, K.4    Beisenherz, K.5    Jacques, G.6    Gropp, C.7    Haeder, M.8
  • 4
    • 0029996240 scopus 로고    scopus 로고
    • Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells
    • Brix, K., P. Lemansky, V. Herzog: Evidence for extracellularly acting cathepsins mediating thyroid hormone liberation in thyroid epithelial cells. Endocrinology 137, 1963-1974 (1996).
    • (1996) Endocrinology , vol.137 , pp. 1963-1974
    • Brix, K.1    Lemansky, P.2    Herzog, V.3
  • 5
    • 0023463127 scopus 로고
    • Constitutive and regulated secretion of proteins
    • Burgess, T. L., R. B. Kelly: Constitutive and regulated secretion of proteins. Annu. Rev. Cell Biol. 3, 243-293 (1987).
    • (1987) Annu. Rev. Cell Biol. , vol.3 , pp. 243-293
    • Burgess, T.L.1    Kelly, R.B.2
  • 6
    • 0029010424 scopus 로고
    • Colocalization of hydrolytic enzymes with widely disparate pH optima: Implications for the regulation of lysosomal pH
    • Butor, C., G. Griffiths, N. Aronson, A. Varki: Colocalization of hydrolytic enzymes with widely disparate pH optima: implications for the regulation of lysosomal pH. J. Cell Sci. 108, 2213-2219 (1995).
    • (1995) J. Cell Sci. , vol.108 , pp. 2213-2219
    • Butor, C.1    Griffiths, G.2    Aronson, N.3    Varki, A.4
  • 7
    • 0023907414 scopus 로고
    • Mannose 6-phosphate/insulin-like growth factor II-binding proteins in human serum and urine
    • Causin, C., A. Waheed, T. Braulke, U. Junghans, P. Maly, R. E. Humbel, K. von Figura: Mannose 6-phosphate/insulin-like growth factor II-binding proteins in human serum and urine. Biochem. J. 252, 795-799 (1988).
    • (1988) Biochem. J. , vol.252 , pp. 795-799
    • Causin, C.1    Waheed, A.2    Braulke, T.3    Junghans, U.4    Maly, P.5    Humbel, R.E.6    Von Figura, K.7
  • 8
    • 0025084076 scopus 로고
    • Mannose-6-phosphate receptor dependent secretion of lysosomal enzymes
    • Chao, H. H.-J., A. Waheed, R. Pohlmann, A. Hille, K. von Figura: Mannose-6-phosphate receptor dependent secretion of lysosomal enzymes. EMBO J. 9, 3507-3513 (1990).
    • (1990) EMBO J. , vol.9 , pp. 3507-3513
    • Chao, H.H.-J.1    Waheed, A.2    Pohlmann, R.3    Hille, A.4    Von Figura, K.5
  • 9
    • 0026522287 scopus 로고
    • The role of proteolytic enzymes in cancer invasion and metastasis
    • Duffy, M. J.: The role of proteolytic enzymes in cancer invasion and metastasis. Clin. Exp. Metastasis 10, 145-155 (1992).
    • (1992) Clin. Exp. Metastasis , vol.10 , pp. 145-155
    • Duffy, M.J.1
  • 10
    • 0029126230 scopus 로고
    • Paraformaldehyde fixation of neutrophils for immunolabeling of granule antigens in cryoultrasections
    • Elliot, E., C. Dennison, P. H. Fortgens, J. Travis: Paraformaldehyde fixation of neutrophils for immunolabeling of granule antigens in cryoultrasections. J. Histochem. Cytochem. 43, 1019-1025 (1995).
    • (1995) J. Histochem. Cytochem. , vol.43 , pp. 1019-1025
    • Elliot, E.1    Dennison, C.2    Fortgens, P.H.3    Travis, J.4
  • 12
    • 0027443394 scopus 로고
    • Mannose-6-phosphate-independent targeting of lysosomal enzymes in I-cell disease B lymphoblasts
    • Glickman, J. N., S. Kornfeld: Mannose-6-phosphate-independent targeting of lysosomal enzymes in I-cell disease B lymphoblasts. J. Cell Biol. 123, 99-108 (1993).
    • (1993) J. Cell Biol. , vol.123 , pp. 99-108
    • Glickman, J.N.1    Kornfeld, S.2
  • 16
    • 0027931667 scopus 로고
    • A lipoxygenase metabolite, 12(S)-HETE, stimulates protein kinase C-mediated release of cathepsin B from malignant cells
    • Honn, K. V., J. Timar, R. Bazaz, M. Sameni, G. Ziegler, B. F. Sloane: A lipoxygenase metabolite, 12(S)-HETE, stimulates protein kinase C-mediated release of cathepsin B from malignant cells. Exp. Cell Res. 214, 120-130 (1994).
    • (1994) Exp. Cell Res. , vol.214 , pp. 120-130
    • Honn, K.V.1    Timar, J.2    Bazaz, R.3    Sameni, M.4    Ziegler, G.5    Sloane, B.F.6
  • 17
    • 0027242012 scopus 로고
    • Mouse procathepsin L lacking a functional glycosylation site is properly folded, stable, and secreted by NIH 3T3 cells
    • Kane, S. E., Mouse procathepsin L lacking a functional glycosylation site is properly folded, stable, and secreted by NIH 3T3 cells. J. Biol. Chem. 268, 11456-11462 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 11456-11462
    • Kane, S.E.1
  • 19
  • 20
    • 0025365591 scopus 로고
    • Lysosomal enzyme targeting
    • Kornfeld, S.: Lysosomal enzyme targeting. Biochem. Soc. Trans. 18, 367-374 (1990).
    • (1990) Biochem. Soc. Trans. , vol.18 , pp. 367-374
    • Kornfeld, S.1
  • 22
    • 0028241106 scopus 로고
    • Distinct molecular mechanisms for protein sorting within immature secretory granules of pancreatic beta-cells
    • Kuliawat, R., P. Arvan: Distinct molecular mechanisms for protein sorting within immature secretory granules of pancreatic beta-cells. J. Cell Biol. 126, 77-86 (1994).
    • (1994) J. Cell Biol. , vol.126 , pp. 77-86
    • Kuliawat, R.1    Arvan, P.2
  • 23
    • 0027535914 scopus 로고
    • Biology and biochemistry of proteinases in tumor invasion
    • Mignatti, P., D. B. Rifkin: Biology and biochemistry of proteinases in tumor invasion. Physiol. Rev. 73, 161-195 (1993).
    • (1993) Physiol. Rev. , vol.73 , pp. 161-195
    • Mignatti, P.1    Rifkin, D.B.2
  • 24
    • 0019497034 scopus 로고
    • Immunofluorescent localization of cathepsins B and D in human fibroblasts
    • Mort, J. S., A. R. Poole, R. S. Decker: Immunofluorescent localization of cathepsins B and D in human fibroblasts. J. Histochem. Cytochem. 29, 649-657 (1981).
    • (1981) J. Histochem. Cytochem. , vol.29 , pp. 649-657
    • Mort, J.S.1    Poole, A.R.2    Decker, R.S.3
  • 25
    • 0029883537 scopus 로고    scopus 로고
    • Cathepsin b is a prorenin processing enzyme
    • Neves, F. A. R., K. G. Duncan, J. D. Baxter: Cathepsin b is a prorenin processing enzyme. Hypertension 27, 514-517 (1996).
    • (1996) Hypertension , vol.27 , pp. 514-517
    • Neves, F.A.R.1    Duncan, K.G.2    Baxter, J.D.3
  • 26
    • 0023890834 scopus 로고
    • Biosynthesis of lysosomal cathepsin B and H in cultured rat hepatocytes
    • Nishimura, Y., J. Amano, H. Sato, H. Tsuji, K. Kato: Biosynthesis of lysosomal cathepsin B and H in cultured rat hepatocytes. Arch. Biochem. Biophys. 262, 159-170 (1988).
    • (1988) Arch. Biochem. Biophys. , vol.262 , pp. 159-170
    • Nishimura, Y.1    Amano, J.2    Sato, H.3    Tsuji, H.4    Kato, K.5
  • 27
    • 0029443042 scopus 로고
    • Neutrophil proteinases and matrix degradation. The cell biology of pericellular proteolysis
    • Owen, C. A., E. J. Campbell: Neutrophil proteinases and matrix degradation. The cell biology of pericellular proteolysis. Semin. Cell Biol. 6, 367-376 (1995).
    • (1995) Semin. Cell Biol. , vol.6 , pp. 367-376
    • Owen, C.A.1    Campbell, E.J.2
  • 28
    • 0026334198 scopus 로고
    • Mannose 6-phosphate-independent targeting of cathepsin D to lysosomes in HepG2 cells
    • Rijnboutt, S., A. J. Kal, H. J. Geuze, H. Aerts, G. J. Strous: Mannose 6-phosphate-independent targeting of cathepsin D to lysosomes in HepG2 cells. J. Biol. Chem. 266, 23586-23592 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 23586-23592
    • Rijnboutt, S.1    Kal, A.J.2    Geuze, H.J.3    Aerts, H.4    Strous, G.J.5
  • 29
    • 0028618307 scopus 로고
    • Pericellular pH affects distribution and secretion of cathepsin B in malignant cells
    • Rozhin, J., M. Sameni, G. Ziegler, B. F. Sloane: Pericellular pH affects distribution and secretion of cathepsin B in malignant cells. Cancer Res. 54, 6517-6525 (1994).
    • (1994) Cancer Res. , vol.54 , pp. 6517-6525
    • Rozhin, J.1    Sameni, M.2    Ziegler, G.3    Sloane, B.F.4
  • 30
    • 0025413394 scopus 로고
    • Cathepsin B and cystatins: Evidence for a role in cancer progression
    • Sloane, B. F. Cathepsin B and cystatins: evidence for a role in cancer progression. Semin. Cancer Biol. 1, 137-152 (1990).
    • (1990) Semin. Cancer Biol. , vol.1 , pp. 137-152
    • Sloane, B.F.1
  • 31
    • 0013610638 scopus 로고
    • Alterations in processing and trafficking of cathepsin B during malignant progression
    • N. Katunuma, K. Suzuki, J. Travis, H. Fritz (eds.): Japan Scientific Societies Press/Karger. Tokyo, Basel
    • Sloane, B. F., M. Sameni, L. Cao, I. Berquin, J. Rozhin, G. Ziegler, K. Moin, N. Day: Alterations in processing and trafficking of cathepsin B during malignant progression. In: N. Katunuma, K. Suzuki, J. Travis, H. Fritz (eds.): Biological Functions of Proteases and Inhibitors. pp. 131-147. Japan Scientific Societies Press/Karger. Tokyo, Basel 1994.
    • (1994) Biological Functions of Proteases and Inhibitors , pp. 131-147
    • Sloane, B.F.1    Sameni, M.2    Cao, L.3    Berquin, I.4    Rozhin, J.5    Ziegler, G.6    Moin, K.7    Day, N.8
  • 32
    • 0025761381 scopus 로고
    • Immunolocalization of the insulin regulatable glucose transporter in brown adipose tissue of the rat
    • Slot, J. W., H. J. Geuze, S. Gigengack, G. E. Lienhard, D. E. James: Immunolocalization of the insulin regulatable glucose transporter in brown adipose tissue of the rat. J. Cell Biol. 113, 123-135 (1991).
    • (1991) J. Cell Biol. , vol.113 , pp. 123-135
    • Slot, J.W.1    Geuze, H.J.2    Gigengack, S.3    Lienhard, G.E.4    James, D.E.5
  • 33
    • 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, A. Brüning, S. Gack, B. Ulbricht, H. Spring, G. Trefz, W. Ebert: Cathepsin B activity in human lung tumor cell lines: Ultrastructural localization, pH sensitivity, and inhibitor status at the cellular level. J. Histochem. Cytochem. 42, 917-929 (1994).
    • (1994) J. Histochem. Cytochem. , vol.42 , pp. 917-929
    • Spiess, E.1    Brüning, A.2    Gack, S.3    Ulbricht, B.4    Spring, H.5    Trefz, G.6    Ebert, W.7
  • 34
    • 0016314296 scopus 로고
    • Immunofluorescence studies on the occurence of cathepsin B1 at tumor cell surfaces
    • Sylven, B., O. Snellman, P. Sträuli: Immunofluorescence studies on the occurence of cathepsin B1 at tumor cell surfaces. Virchows Arch. B 17, 97-110 (1974).
    • (1974) Virchows Arch. B , vol.17 , pp. 97-110
    • Sylven, B.1    Snellman, O.2    Sträuli, P.3
  • 35
    • 0027457336 scopus 로고
    • Cysteine proteinases in rat dorsal root ganglion and spinal cord, with special reference to the colocalization of these enzymes with calcitinin gene-related peptide in lysosomes
    • Taniguchi, K., M. Tomita, E. Kominami, Y. Uchiyama: Cysteine proteinases in rat dorsal root ganglion and spinal cord, with special reference to the colocalization of these enzymes with calcitinin gene-related peptide in lysosomes. Brain Res. 601, 143-153 (1993).
    • (1993) Brain Res. , vol.601 , pp. 143-153
    • Taniguchi, K.1    Tomita, M.2    Kominami, E.3    Uchiyama, Y.4
  • 36
    • 0021849003 scopus 로고
    • Coexistence of renin and cathepsin B in epitheloid cell secretory granules
    • Taugner, R., C. P. Bührle, R. Nobiling, H. Kirschke: Coexistence of renin and cathepsin B in epitheloid cell secretory granules. Histochemistry 83, 103-108 (1985).
    • (1985) Histochemistry , vol.83 , pp. 103-108
    • Taugner, R.1    Bührle, C.P.2    Nobiling, R.3    Kirschke, H.4
  • 37
    • 0026316169 scopus 로고
    • Regulated secretion of mature cathepsin B from rat exocrine pancreatic cells
    • Tooze, J., M. Hollinshead, G. Hensel, H. F. Kern, B. Hoflack: Regulated secretion of mature cathepsin B from rat exocrine pancreatic cells. Eur. J. Cell Biol. 56, 187-200 (1991).
    • (1991) Eur. J. Cell Biol. , vol.56 , pp. 187-200
    • Tooze, J.1    Hollinshead, M.2    Hensel, G.3    Kern, H.F.4    Hoflack, B.5
  • 38
    • 0030218021 scopus 로고    scopus 로고
    • Differential secretion of cathepsins B and L from normal and tumor human lung cells stimulated by 12(S)-hydroxy-eicosatetraenoic acid (12(S)-HETE)
    • Ulbricht, B., W. Hagmann, W. Ebert, E. Spiess: Differential secretion of cathepsins B and L from normal and tumor human lung cells stimulated by 12(S)-hydroxy-eicosatetraenoic acid (12(S)-HETE). Exp. Cell Res. 226, 255-263 (1996).
    • (1996) Exp. Cell Res. , vol.226 , pp. 255-263
    • Ulbricht, B.1    Hagmann, W.2    Ebert, W.3    Spiess, E.4
  • 39
    • 0028990820 scopus 로고
    • Cysteine proteinases in GH4C1 cells, a rat pituitary tumor cell line, are secreted by the constitutive and regulated secretory pathways
    • Waguri, S., N. Sato, T. Watanabe, K. Ishidoh, E. Kominami, K. Sato, Y. Uchiyama: Cysteine proteinases in GH4C1 cells, a rat pituitary tumor cell line, are secreted by the constitutive and regulated secretory pathways. Eur. J. Cell Biol. 67, 308-318 (1995).
    • (1995) Eur. J. Cell Biol. , vol.67 , pp. 308-318
    • Waguri, S.1    Sato, N.2    Watanabe, T.3    Ishidoh, K.4    Kominami, E.5    Sato, K.6    Uchiyama, Y.7
  • 40
    • 0025782824 scopus 로고
    • Quantitation of Mr 46000 and Mr 300 000 mannose 6-phosphate receptors in human cells and tissues
    • Wenk, J., A. Hille, K. von Figura: Quantitation of Mr 46000 and Mr 300 000 mannose 6-phosphate receptors in human cells and tissues. Biochem. Int. 23, 723-732 (1991).
    • (1991) Biochem. Int. , vol.23 , pp. 723-732
    • Wenk, J.1    Hille, A.2    Von Figura, K.3
  • 41
    • 0028048344 scopus 로고
    • Cathepsin B in tumors, normal tissue and isolated cells from the human lung
    • Werle, B., W. Ebert, W. Klein, E. Spiess: Cathepsin B in tumors, normal tissue and isolated cells from the human lung. Anticancer Res. 14, 1169-1176 (1994).
    • (1994) Anticancer Res. , vol.14 , pp. 1169-1176
    • Werle, B.1    Ebert, W.2    Klein, W.3    Spiess, E.4
  • 42
    • 0029257305 scopus 로고
    • Assessment of cathepsin L activity by use of the inhibitor CA-074 compared to cathepsin B activity in human lung tumor tissue
    • Werle, B., W. Ebert, W. Klein, E. Spiess: Assessment of cathepsin L activity by use of the inhibitor CA-074 compared to cathepsin B activity in human lung tumor tissue. Biol. Chem. Hoppe-Seyler 276, 157-164 (1995).
    • (1995) Biol. Chem. Hoppe-Seyler , vol.276 , pp. 157-164
    • Werle, B.1    Ebert, W.2    Klein, W.3    Spiess, E.4
  • 43
    • 0023475205 scopus 로고
    • Immunocytochemical localization of cathepsins B and H in rat liver
    • Yokota, S., K. Kato: Immunocytochemical localization of cathepsins B and H in rat liver. Histochemistry 88, 97-103 (1987).
    • (1987) Histochemistry , vol.88 , pp. 97-103
    • Yokota, S.1    Kato, K.2


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