메뉴 건너뛰기




Volumn 117, Issue 2, 1997, Pages 169-178

Stress response of lysosomal cysteine proteinases in rat C6 glioma cells

Author keywords

Butanol; Cathepsins; Heat shock; Heat shock protein 70; Lysosomal cysteine proteinases; Rat C6 glioma cells

Indexed keywords

ACID PROTEINASE; BUTANOL; CATHEPSIN B; CATHEPSIN L; CYSTEINE PROTEINASE; GELATIN; HEAT SHOCK PROTEIN; TRYPAN BLUE;

EID: 0030787412     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0305-0491(96)00326-4     Document Type: Article
Times cited : (9)

References (32)
  • 1
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H and cathepsin L
    • Barrett, A.J.; Kirschke, H. Cathepsin B, cathepsin H and cathepsin L. Methods Enzymol. 80:535-561;1981.
    • (1981) Methods Enzymol. , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 3
    • 0015984017 scopus 로고
    • Cathepsin B1. A lysosomal enzyme that degrades native collagen
    • Burleigh, M.C.; Barrett, A.J.; Lazarus, G.S. Cathepsin B1. A lysosomal enzyme that degrades native collagen. Biochem. J. 137:387-398;1974.
    • (1974) Biochem. J. , vol.137 , pp. 387-398
    • Burleigh, M.C.1    Barrett, A.J.2    Lazarus, G.S.3
  • 4
    • 0027406136 scopus 로고
    • The ubiquitin-mediated proteolytic pathway
    • Ciechanover, A. The ubiquitin-mediated proteolytic pathway. Brain Pathol. 3:67-75;1993.
    • (1993) Brain Pathol. , vol.3 , pp. 67-75
    • Ciechanover, A.1
  • 6
    • 0024557114 scopus 로고
    • Mechanism for selective secretion of a lysosomal proteinase by transformed mouse fibroblast
    • Dong, J.; Prence, E.M.; Sahagion, G.G. Mechanism for selective secretion of a lysosomal proteinase by transformed mouse fibroblast. J. Biol. Chem. 264:7377-7383;1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7377-7383
    • Dong, J.1    Prence, E.M.2    Sahagion, G.G.3
  • 7
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.J.; Sambrook, J. Protein folding in the cell. Nature 355:33-45;1992.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 8
    • 0026503828 scopus 로고
    • The mechanism and functions of ATP-dependent proteases in bacterial and animal cells
    • Goldberg, A.L. The mechanism and functions of ATP-dependent proteases in bacterial and animal cells. Eur. J. Biochem. 203:9-23;1992.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 9-23
    • Goldberg, A.L.1
  • 9
    • 0018854046 scopus 로고
    • Electrophoretic analysis of plasminogen activator in polyacrylamide gels containing sodium dodecylsulfate and copolymerized substrate
    • Heussen, C.; Dowdle, E.B. Electrophoretic analysis of plasminogen activator in polyacrylamide gels containing sodium dodecylsulfate and copolymerized substrate. Anal. Biochem. 102:196-202;1980.
    • (1980) Anal. Biochem. , vol.102 , pp. 196-202
    • Heussen, C.1    Dowdle, E.B.2
  • 10
    • 0026787869 scopus 로고
    • Stress-induced proteolysis in yeast
    • Hilt, W.; Wolf, D.H. Stress-induced proteolysis in yeast. Mol. Microbiol. 6:2437-2442;1992.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2437-2442
    • Hilt, W.1    Wolf, D.H.2
  • 12
    • 0019724755 scopus 로고
    • On the substrate specificity of cathepsin L
    • Kirschke, H. On the substrate specificity of cathepsin L. Acta Biol. Med. Germ. 40:1427-1431;1981.
    • (1981) Acta Biol. Med. Germ. , vol.40 , pp. 1427-1431
    • Kirschke, H.1
  • 13
    • 0023655791 scopus 로고
    • Purification and characterization of lysosomes from Chinese Hamster ovary cells
    • Madden, E.A.; Wirt, J.B.; Storrie, B. Purification and characterization of lysosomes from Chinese Hamster ovary cells. Arch. Biochem. Biophys. 257:27-38;1987.
    • (1987) Arch. Biochem. Biophys. , vol.257 , pp. 27-38
    • Madden, E.A.1    Wirt, J.B.2    Storrie, B.3
  • 15
    • 0028862911 scopus 로고
    • Purification and characterization of procathepsin L, a self processing zymogen of guinea pig spermatozoa that acts on a cathepsin D assay substrate
    • McDonald, J.K.; Emerick, J.M.C. Purification and characterization of procathepsin L, a self processing zymogen of guinea pig spermatozoa that acts on a cathepsin D assay substrate. Arch. Biochem. Biophys. 323:409-422;1995.
    • (1995) Arch. Biochem. Biophys. , vol.323 , pp. 409-422
    • McDonald, J.K.1    Emerick, J.M.C.2
  • 16
    • 0028143975 scopus 로고
    • Heat shock inhibits and activates different protein degradation pathways and proteinase activities in Neurospora crassa
    • Mohsenzadeh, S.; Xu, C.; Fracella, F.; Rensing, L. Heat shock inhibits and activates different protein degradation pathways and proteinase activities in Neurospora crassa. FEMS Microbiol. Lett. 124:215-224;1995.
    • (1995) FEMS Microbiol. Lett. , vol.124 , pp. 215-224
    • Mohsenzadeh, S.1    Xu, C.2    Fracella, F.3    Rensing, L.4
  • 17
    • 0001913819 scopus 로고
    • Mechanism and regulation of induced and basal protein degradation in liver
    • Glaumann, H.; Ballard, F.J. (eds). New York: Academic Press
    • Mortimore, G.E. Mechanism and regulation of induced and basal protein degradation in liver. In: Glaumann, H.; Ballard, F.J. (eds). Lysosomes: Their Role in Protein Breakdown. New York: Academic Press; 1987:413-444.
    • (1987) Lysosomes: Their Role in Protein Breakdown , pp. 413-444
    • Mortimore, G.E.1
  • 18
    • 0027955199 scopus 로고
    • Heat shock response and cytotoxicity in C6 rat glioma cells: Structure-activity relationship of different alcohols
    • Neuhaus-Steinmetz, U.; Xu, C.; Fracella, F.; Oberheitmann, B.; Richter-Landsberg, C.; Rensing, L. Heat shock response and cytotoxicity in C6 rat glioma cells: Structure-activity relationship of different alcohols. Mol. Pharm. 45:36-41;1994.
    • (1994) Mol. Pharm. , vol.45 , pp. 36-41
    • Neuhaus-Steinmetz, U.1    Xu, C.2    Fracella, F.3    Oberheitmann, B.4    Richter-Landsberg, C.5    Rensing, L.6
  • 19
    • 0018609721 scopus 로고
    • A simple, versatile, sensitive and volume-independent method for quantitative protein determination which is independent of other external influences
    • Neuhoff, V.; Philipp, K.; Zimmer, H.G.; Mesecke, S. A simple, versatile, sensitive and volume-independent method for quantitative protein determination which is independent of other external influences. Hoppe Seyler's Z. Physiol. Chem. 360: 1657-1670;1979.
    • (1979) Hoppe Seyler's Z. Physiol. Chem. , vol.360 , pp. 1657-1670
    • Neuhoff, V.1    Philipp, K.2    Zimmer, H.G.3    Mesecke, S.4
  • 21
    • 0029098591 scopus 로고
    • Microglial cathepsin B: An immunological examination of cellular and secreted species
    • Ryan, R.E.; Sloane, B.F.; Sameni, M.; Wood, P.L. Microglial cathepsin B: An immunological examination of cellular and secreted species. J. Neurochem. 65:1035-1045;1995.
    • (1995) J. Neurochem. , vol.65 , pp. 1035-1045
    • Ryan, R.E.1    Sloane, B.F.2    Sameni, M.3    Wood, P.L.4
  • 22
    • 0026575964 scopus 로고
    • Ubiquitin, a central component of selective cytoplasmic proteolysis is linked to proteins residing at the locus of non-selective proteolysis, the vaculoe
    • Simeon, A.; van der Klei, J.J.; Venhuis, M.; Wolf, D.H. Ubiquitin, a central component of selective cytoplasmic proteolysis is linked to proteins residing at the locus of non-selective proteolysis, the vaculoe. FEBS Lett. 301:231-235;1992.
    • (1992) FEBS Lett. , vol.301 , pp. 231-235
    • Simeon, A.1    Van Der Klei, J.J.2    Venhuis, M.3    Wolf, D.H.4
  • 23
    • 0019757154 scopus 로고
    • Cathepsin D from porcine and bovine spleen
    • Takahashi, T.; Tang, J. Cathepsin D from porcine and bovine spleen. Methods Enzymol. 80:565-581;1981.
    • (1981) Methods Enzymol. , vol.80 , pp. 565-581
    • Takahashi, T.1    Tang, J.2
  • 24
    • 0026808914 scopus 로고
    • Protein and peptide binding and stimulation of in vitro lysosomal proteolysis by the 73-kDa heat shock cognate protein
    • Terlecky, S.R.; Chiang, H.L.; Olson, T.S.; Dice. J.F. Protein and peptide binding and stimulation of in vitro lysosomal proteolysis by the 73-kDa heat shock cognate protein. J. Biol. Chem. 264:9202-9209;1992.
    • (1992) J. Biol. Chem. , vol.264 , pp. 9202-9209
    • Terlecky, S.R.1    Chiang, H.L.2    Olson, T.S.3    Dice, J.F.4
  • 26
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some application
    • Towbin, H.; Staehelin, T.; Gordon, J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some application. Proc. Natl. Acad. Sci. USA 76:4350-4354;1979.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 27
    • 0028936570 scopus 로고
    • Identification of bovine stefin A, a novel protein inhibitor of cysteine proteinases
    • Turk, B.; Ritonja, A.; Björk, J.; Stoka, V.; Dolenc, J.; Turk, V. Identification of bovine stefin A, a novel protein inhibitor of cysteine proteinases. FEBS Lett. 360:101-106;1995.
    • (1995) FEBS Lett. , vol.360 , pp. 101-106
    • Turk, B.1    Ritonja, A.2    Björk, J.3    Stoka, V.4    Dolenc, J.5    Turk, V.6
  • 28
    • 0027205018 scopus 로고
    • CaBP2 is a rat homolog of ERP72 with proteindisulfide isomerase activity
    • Van, P.N.; Rupp, K.; Lampen, A.; Söling, H.D. CaBP2 is a rat homolog of ERP72 with proteindisulfide isomerase activity. Eur. J. Biochem. 213:789-795;1994.
    • (1994) Eur. J. Biochem. , vol.213 , pp. 789-795
    • Van, P.N.1    Rupp, K.2    Lampen, A.3    Söling, H.D.4
  • 29
    • 0022555844 scopus 로고
    • Lysosomal enzymes and their receptors
    • Von Figura, K.; Hasilik, A. Lysosomal enzymes and their receptors. Annu. Rev. Biochem. 55:167-193;1986.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 167-193
    • Von Figura, K.1    Hasilik, A.2
  • 31
    • 0001860842 scopus 로고
    • The mammalian stress response: Cell physiology and biochemistry of stress proteins
    • Morimoto, R.J.; Tissières, A.; Georgopoulos, C. (eds). New York: Cold Spring Harbor Laboratory Press;
    • Welch, W.J. The mammalian stress response: cell physiology and biochemistry of stress proteins. In: Morimoto, R.J.; Tissières, A.; Georgopoulos, C. (eds). Stress Proteins in Biology and Medicine. New York: Cold Spring Harbor Laboratory Press; 1990;223-278.
    • (1990) Stress Proteins in Biology and Medicine , pp. 223-278
    • Welch, W.J.1
  • 32
    • 0027939865 scopus 로고
    • A proteolytic activity enhanced by arsenite in Chinese hamster ovary cells: Possible involvement in arsenite-induced cell killing
    • Yih, L.H.; Lee, T.C. A proteolytic activity enhanced by arsenite in Chinese hamster ovary cells: Possible involvement in arsenite-induced cell killing. Biochem. Biophys. Res. Commun. 202:1015-1022;1994.
    • (1994) Biochem. Biophys. Res. Commun. , vol.202 , pp. 1015-1022
    • Yih, L.H.1    Lee, T.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.