메뉴 건너뛰기




Volumn 72, Issue 7, 2004, Pages 3863-3868

Cleavage of host keratin 8 by a chlamydia-secreted protease

Author keywords

[No Author keywords available]

Indexed keywords

CHLAMYDIAL PROTEASE PROTEASOME LIKE ACTIVITY FACTOR; KERATIN; KERATIN 8; PROTEINASE; UNCLASSIFIED DRUG;

EID: 3042546262     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.72.7.3863-3868.2004     Document Type: Article
Times cited : (79)

References (33)
  • 1
    • 0032938889 scopus 로고    scopus 로고
    • Persistent "silent" Chlamydia trachomatis female genital tract infections
    • Askienazy-Elbhar, M., and J. H. Suchet. 1999. Persistent "silent" Chlamydia trachomatis female genital tract infections. Infect. Dis. Obstet. Gynecol. 7:31-34.
    • (1999) Infect. Dis. Obstet. Gynecol. , vol.7 , pp. 31-34
    • Askienazy-Elbhar, M.1    Suchet, J.H.2
  • 2
    • 0027946866 scopus 로고
    • Persistent chlamydiae: From cell culture to a paradigm for chlamydial pathogenesis
    • Beatty, W. L., R. P. Morrison, and G. I. Byrne. 1994. Persistent chlamydiae: from cell culture to a paradigm for chlamydial pathogenesis. Microbiol. Rev. 58:686-699.
    • (1994) Microbiol. Rev. , vol.58 , pp. 686-699
    • Beatty, W.L.1    Morrison, R.P.2    Byrne, G.I.3
  • 3
    • 0028957558 scopus 로고
    • Tissue-specific and efficient expression of the human simple epithelial keratin 8 gene in transgenic mice
    • Casanova, L., A. Bravo, F. Were, A. Ramirez, J. J. Jorcano, and M. Vidal. 1995. Tissue-specific and efficient expression of the human simple epithelial keratin 8 gene in transgenic mice J. Cell Sci. 108:811-820.
    • (1995) J. Cell Sci. , vol.108 , pp. 811-820
    • Casanova, L.1    Bravo, A.2    Were, F.3    Ramirez, A.4    Jorcano, J.J.5    Vidal, M.6
  • 4
    • 0027167564 scopus 로고
    • The adenovirus L3 23-kilodalton proteinase cleaves the amino-terminal head domain from cytokeratin 18 and disrupts the cytokeratin network of HeLa cells
    • Chen, P. H., D. A. Ornelles, and T. Shenk. 1993. The adenovirus L3 23-kilodalton proteinase cleaves the amino-terminal head domain from cytokeratin 18 and disrupts the cytokeratin network of HeLa cells. J. Virol. 67:3507-3514.
    • (1993) J. Virol. , vol.67 , pp. 3507-3514
    • Chen, P.H.1    Ornelles, D.A.2    Shenk, T.3
  • 5
    • 0037077252 scopus 로고    scopus 로고
    • Cancer-associated cleavage of cytokeratin 8/18 heterotypic complexes exposes a neoepitope in human adenocarcinomas
    • Ditzel, H. J., M. C. Strik, M. K. Larsen, A. C. Willis, A. Waseem, K. Kejling, and J. C. Jensenius. 2002. Cancer-associated cleavage of cytokeratin 8/18 heterotypic complexes exposes a neoepitope in human adenocarcinomas. J. Biol. Chem. 277:21712-21722.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21712-21722
    • Ditzel, H.J.1    Strik, M.C.2    Larsen, M.K.3    Willis, A.C.4    Waseem, A.5    Kejling, K.6    Jensenius, J.C.7
  • 6
    • 0032536526 scopus 로고    scopus 로고
    • Inhibition of apoptosis in chlamydia-infected cells: Blockade of mitochondrial cytochrome c release and caspase activation
    • Fan, T., H. Lu, H. Hu, L. Shi, G. A. McClarty, D. M. Nance, A. H. Greenberg, and G. Zhong. 1998. Inhibition of apoptosis in chlamydia-infected cells: blockade of mitochondrial cytochrome c release and caspase activation. J. Exp. Med. 187:487-496.
    • (1998) J. Exp. Med. , vol.187 , pp. 487-496
    • Fan, T.1    Lu, H.2    Hu, H.3    Shi, L.4    McClarty, G.A.5    Nance, D.M.6    Greenberg, A.H.7    Zhong, G.8
  • 7
    • 0031987892 scopus 로고    scopus 로고
    • The diverse habitats of obligate intracellular parasites
    • Hackstadt, T. 1998. The diverse habitats of obligate intracellular parasites. Curr. Opin. Microbiol. 1:82-87.
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 82-87
    • Hackstadt, T.1
  • 8
    • 0029838076 scopus 로고    scopus 로고
    • Cytokeratin 8 released by breast carcinoma cells in vitro binds plasminogen and tissue-type plasminogen activator and promotes plasminogen activation
    • Hembrough, T. A., K. R. Kralovich, L. Li, and S. L. Gonias. 1996. Cytokeratin 8 released by breast carcinoma cells in vitro binds plasminogen and tissue-type plasminogen activator and promotes plasminogen activation. Biochem. J. 317:763-769.
    • (1996) Biochem. J. , vol.317 , pp. 763-769
    • Hembrough, T.A.1    Kralovich, K.R.2    Li, L.3    Gonias, S.L.4
  • 9
    • 0029795405 scopus 로고    scopus 로고
    • Cell-surface cytokeratin 8 is the major plasminogen receptor on breast cancer cells and is required for the accelerated activation of cell-associated plasminogen by tissue-type plasminogen activator
    • Hembrough, T. A., L. Li, and S. L. Gonias. 1996. Cell-surface cytokeratin 8 is the major plasminogen receptor on breast cancer cells and is required for the accelerated activation of cell-associated plasminogen by tissue-type plasminogen activator. J. Biol. Chem. 271:25684-25691.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25684-25691
    • Hembrough, T.A.1    Li, L.2    Gonias, S.L.3
  • 10
    • 0028901093 scopus 로고
    • A cytokeratin 8-like protein with plasminogen-binding activity is present on the external surfaces of hepatocytes, HepG2 cells and breast carcinoma cell lines
    • Hembrough, T. A., J. Vasudevan, M. M. Allietta, W. F. Glass II, and S. L. Gonias. 1995. A cytokeratin 8-like protein with plasminogen-binding activity is present on the external surfaces of hepatocytes, HepG2 cells and breast carcinoma cell lines. J. Cell Sci. 108:1071-1082.
    • (1995) J. Cell Sci. , vol.108 , pp. 1071-1082
    • Hembrough, T.A.1    Vasudevan, J.2    Allietta, M.M.3    Glass II, W.F.4    Gonias, S.L.5
  • 12
    • 0033960790 scopus 로고    scopus 로고
    • Intermediate filaments and their associates: Multi-talented structural elements specifying cytoarchitecture and cytodynamics
    • Herrmann, H., and U. Aebi. 2000. Intermediate filaments and their associates: multi-talented structural elements specifying cytoarchitecture and cytodynamics. Curr. Opin. Cell Biol. 12:79-90.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 79-90
    • Herrmann, H.1    Aebi, U.2
  • 13
    • 0030596170 scopus 로고    scopus 로고
    • Structure and assembly properties of the intermediate filament protein vimentin: The role of its head, rod and tail domains
    • Herrmann, H., M. Haner, M. Brettel, S. A. Muller, K. N. Goldie, B. Fedtke, A. Lustig, W. W. Franke, and U. Aebi. 1996. Structure and assembly properties of the intermediate filament protein vimentin: the role of its head, rod and tail domains. J. Mol. Biol. 264:933-953.
    • (1996) J. Mol. Biol. , vol.264 , pp. 933-953
    • Herrmann, H.1    Haner, M.2    Brettel, M.3    Muller, S.A.4    Goldie, K.N.5    Fedtke, B.6    Lustig, A.7    Franke, W.W.8    Aebi, U.9
  • 15
    • 0022339650 scopus 로고
    • Intermediate filament forming ability of desmin derivatives lacking either the amino-terminal 67 or the carboxy-terminal 27 residues
    • Kaufmann, E., K. Weber, and N. Geisler. 1985. Intermediate filament forming ability of desmin derivatives lacking either the amino-terminal 67 or the carboxy-terminal 27 residues. J. Mol. Biol. 185:733-742.
    • (1985) J. Mol. Biol. , vol.185 , pp. 733-742
    • Kaufmann, E.1    Weber, K.2    Geisler, N.3
  • 16
    • 0030474513 scopus 로고    scopus 로고
    • Implications of intermediate filament protein phosphorylation
    • Ku, N. O., J. Liao, C. F. Chou, and M. B. Omary. 1996. Implications of intermediate filament protein phosphorylation. Cancer Metastasis Rev. 15: 429-444.
    • (1996) Cancer Metastasis Rev. , vol.15 , pp. 429-444
    • Ku, N.O.1    Liao, J.2    Chou, C.F.3    Omary, M.B.4
  • 17
    • 0037125190 scopus 로고    scopus 로고
    • A thermosensitive mutant of HRV2 2A proteinase: Evidence for direct cleavage of eIF4GI and eIF4GII
    • Liebig, H. D., J. Seipelt, E. Vassilieva, A. Gradi, and E. Kuechler. 2002. A thermosensitive mutant of HRV2 2A proteinase: evidence for direct cleavage of eIF4GI and eIF4GII. FEBS Lett. 523:53-57.
    • (2002) FEBS Lett. , vol.523 , pp. 53-57
    • Liebig, H.D.1    Seipelt, J.2    Vassilieva, E.3    Gradi, A.4    Kuechler, E.5
  • 18
    • 0036155312 scopus 로고    scopus 로고
    • Biomarkers predictive of lymph node metastases in oral squamous cell carcinoma
    • Discussion, 60:147-148
    • Lopes, M. A., N. G. Nikitakis, M. A. Reynolds, R. A. Ord, and J. Sauk, Jr. 2002. Biomarkers predictive of lymph node metastases in oral squamous cell carcinoma. J. Oral Maxillofac. Surg. 60:142-147. (Discussion, 60:147-148.)
    • (2002) J. Oral Maxillofac. Surg. , vol.60 , pp. 142-147
    • Lopes, M.A.1    Nikitakis, N.G.2    Reynolds, M.A.3    Ord, R.A.4    Sauk Jr., J.5
  • 19
    • 0030473762 scopus 로고    scopus 로고
    • Oncogenic regulation and function of keratins 8 and 18
    • Oshima, R. G., H. Baribault, and C. Caulin. 1996. Oncogenic regulation and function of keratins 8 and 18. Cancer Metastasis Rev. 15:445-471.
    • (1996) Cancer Metastasis Rev. , vol.15 , pp. 445-471
    • Oshima, R.G.1    Baribault, H.2    Caulin, C.3
  • 20
    • 0021739972 scopus 로고
    • Reconstitution of cytokeratin filaments in vitro: Further evidence for the role of nonhelical peptides in filament assembly
    • Sauk, J. J., M. Krumweide, D. Cocking-Johnson, and J. G. White. 1984. Reconstitution of cytokeratin filaments in vitro: further evidence for the role of nonhelical peptides in filament assembly. J. Cell Biol. 99:1590-1597.
    • (1984) J. Cell Biol. , vol.99 , pp. 1590-1597
    • Sauk, J.J.1    Krumweide, M.2    Cocking-Johnson, D.3    White, J.G.4
  • 21
    • 0025115234 scopus 로고
    • Distribution of cytokeratin polypeptides in human transitional cell carcinomas, with special emphasis on changing expression patterns during tumor progression
    • Schaafsma, H. E., F. C. Ramaekers, G. N. van Muijen, E. B. Lane, I. M. Leigh, H. Robben, A. Huijsmans, E. C. Ooms, and D. J. Ruiter. 1990. Distribution of cytokeratin polypeptides in human transitional cell carcinomas, with special emphasis on changing expression patterns during tumor progression. Am. J. Pathol. 136:329-343.
    • (1990) Am. J. Pathol. , vol.136 , pp. 329-343
    • Schaafsma, H.E.1    Ramaekers, F.C.2    Van Muijen, G.N.3    Lane, E.B.4    Leigh, I.M.5    Robben, H.6    Huijsmans, A.7    Ooms, E.C.8    Ruiter, D.J.9
  • 22
    • 0017513929 scopus 로고
    • The expanding clinical spectrum of infections with Chlamydia trachomatis
    • Schacter, J. 1977. The expanding clinical spectrum of infections with Chlamydia trachomatis. Sex. Transm. Dis. 4:116-118.
    • (1977) Sex. Transm. Dis. , vol.4 , pp. 116-118
    • Schacter, J.1
  • 23
    • 0034733665 scopus 로고    scopus 로고
    • 2A proteinase of human rhinovirus cleaves cytokeratin 8 in infected HeLa cells
    • Seipelt, J., H. D. Liebig, W. Sommergruber, C. Gerner, and E. Kuechler. 2000. 2A proteinase of human rhinovirus cleaves cytokeratin 8 in infected HeLa cells. J. Biol. Chem. 275:20084-20089.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20084-20089
    • Seipelt, J.1    Liebig, H.D.2    Sommergruber, W.3    Gerner, C.4    Kuechler, E.5
  • 25
    • 0037086445 scopus 로고    scopus 로고
    • Conserved segments 1A and 2B of the intermediate filament dimer: Their atomic structures and role in filament assembly
    • Strelkov, S. V., H. Herrmann, N. Geisler, T. Wedig, R. Zimbelmann, U. Aebi, and P. Burkhard. 2002. Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly. EMBO J. 21:1255-1266.
    • (2002) EMBO J. , vol.21 , pp. 1255-1266
    • Strelkov, S.V.1    Herrmann, H.2    Geisler, N.3    Wedig, T.4    Zimbelmann, R.5    Aebi, U.6    Burkhard, P.7
  • 26
    • 0033865327 scopus 로고    scopus 로고
    • Intracellular survival by chlamydia
    • Wyrick, P. B. 2000. Intracellular survival by chlamydia. Cell Microbiol. 2:275-282.
    • (2000) Cell Microbiol. , vol.2 , pp. 275-282
    • Wyrick, P.B.1
  • 27
    • 0028196637 scopus 로고
    • Adenovirus inhibition of cell translation facilitates release of virus particles and enhances degradation of the cytokeratin network
    • Zhang, Y., and R. J. Schneider. 1994. Adenovirus inhibition of cell translation facilitates release of virus particles and enhances degradation of the cytokeratin network. J. Virol. 68:2544-2555.
    • (1994) J. Virol. , vol.68 , pp. 2544-2555
    • Zhang, Y.1    Schneider, R.J.2
  • 28
    • 0029845011 scopus 로고    scopus 로고
    • Evidence that binding site occupancy is necessary and sufficient for effective major histocompatibility complex (MHC) class II transport through the secretory pathway redefines the primary function of class II-associated invariant chain peptides (CLIP)
    • Zhong, G., F. Castellino, P. Romagnoli, and R. N. Germain. 1996. Evidence that binding site occupancy is necessary and sufficient for effective major histocompatibility complex (MHC) class II transport through the secretory pathway redefines the primary function of class II-associated invariant chain peptides (CLIP). J. Exp. Med. 184:2061-2066.
    • (1996) J. Exp. Med. , vol.184 , pp. 2061-2066
    • Zhong, G.1    Castellino, F.2    Romagnoli, P.3    Germain, R.N.4
  • 29
    • 0035896736 scopus 로고    scopus 로고
    • Identification of a chlamydial protease-like activity factor responsible for the degradation of host transcription factors
    • Zhong, G., P. Fan, H. Ji, F. Dong, and Y. Huang. 2001. Identification of a chlamydial protease-like activity factor responsible for the degradation of host transcription factors. J. Exp. Med. 193:935-942.
    • (2001) J. Exp. Med. , vol.193 , pp. 935-942
    • Zhong, G.1    Fan, P.2    Ji, H.3    Dong, F.4    Huang, Y.5
  • 30
    • 0033591635 scopus 로고    scopus 로고
    • Chlamydia inhibits interferon gamma-inducible major histocompatibility complex class II expression by degradation of upstream stimulatory factor 1
    • Zhong, G., T. Fan, and L. Liu. 1999. Chlamydia inhibits interferon gamma-inducible major histocompatibility complex class II expression by degradation of upstream stimulatory factor 1. J. Exp. Med. 189:1931-1938.
    • (1999) J. Exp. Med. , vol.189 , pp. 1931-1938
    • Zhong, G.1    Fan, T.2    Liu, L.3
  • 31
    • 0034193165 scopus 로고    scopus 로고
    • Degradation of transcription factor RFX5 during the inhibition of both constitutive and interferon gamma-inducible major histocompatibility complex class I expression in chlamydia-infected cells
    • Zhong, G., L. Liu, T. Fan, P. Fan, and H. Ji. 2000. Degradation of transcription factor RFX5 during the inhibition of both constitutive and interferon gamma-inducible major histocompatibility complex class I expression in chlamydia-infected cells. J. Exp. Med. 191:1525-1534.
    • (2000) J. Exp. Med. , vol.191 , pp. 1525-1534
    • Zhong, G.1    Liu, L.2    Fan, T.3    Fan, P.4    Ji, H.5
  • 32
    • 13144265793 scopus 로고    scopus 로고
    • Production, specificity, and functionality of monoclonal antibodies to specific peptide-major histocompatibility complex class II complexes formed by processing of exogenous protein
    • Zhong, G., C. Reis e Sousa, and R. N. Germain. 1997. Production, specificity, and functionality of monoclonal antibodies to specific peptide-major histocompatibility complex class II complexes formed by processing of exogenous protein. Proc. Natl. Acad. Sci. USA 94:13856-13861.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13856-13861
    • Zhong, G.1    Reis E Sousa, C.2    Germain, R.N.3
  • 33
    • 0023931006 scopus 로고
    • Recombinant murine gamma interferon inhibits Chlamydia trachomatis serovar L1 in vivo
    • Zhong, G. M., E. M. Peterson, C. W. Czarniecki, and L. M. de la Maza. 1988. Recombinant murine gamma interferon inhibits Chlamydia trachomatis serovar L1 in vivo. Infect. Immun. 56:283-286.
    • (1988) Infect. Immun. , vol.56 , pp. 283-286
    • Zhong, G.M.1    Peterson, E.M.2    Czarniecki, C.W.3    De La Maza, L.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.