메뉴 건너뛰기




Volumn 5, Issue , 2015, Pages

Geranylgeranylacetone selectively binds to the HSP70 of Helicobacter pylori and alters its coccoid morphology

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DITERPENE; HEAT SHOCK PROTEIN 70; PROTEIN BINDING; RECOMBINANT PROTEIN; TEPRENONE;

EID: 84941096182     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep13738     Document Type: Article
Times cited : (4)

References (41)
  • 1
    • 0032420217 scopus 로고    scopus 로고
    • Helicobacter pylori infection and the pathogenesis of duodenal ulceration
    • Walker, M. M. & Crabtree, J. E. Helicobacter pylori infection and the pathogenesis of duodenal ulceration. Ann. N. Y. Acad. Sci. 859, 96-111 (1998).
    • (1998) Ann. N. Y. Acad. Sci. , vol.859 , pp. 96-111
    • Walker, M.M.1    Crabtree, J.E.2
  • 2
    • 33644823894 scopus 로고    scopus 로고
    • The role of persistence in Helicobacter pylori pathogenesis
    • Israel, D. A. & Peek, R. M. Jr. The role of persistence in Helicobacter pylori pathogenesis. Curr. Opin. Gastroenterol. 22, 3-7 (2006).
    • (2006) Curr. Opin. Gastroenterol. , vol.22 , pp. 3-7
    • Israel, D.A.1    Peek, R.M.2
  • 3
    • 84872766567 scopus 로고    scopus 로고
    • Role of the Helicobacter pylori-induced inflammatory response in the development of gastric cancer
    • Lamb, A. & Chen, L. F. Role of the Helicobacter pylori-induced inflammatory response in the development of gastric cancer. J. Cell. Biochem. 114, 491-7 (2013).
    • (2013) J. Cell. Biochem. , vol.114 , pp. 491-497
    • Lamb, A.1    Chen, L.F.2
  • 4
    • 84883807676 scopus 로고    scopus 로고
    • Multi-center randomized controlled study to establish the standard third-line regimen for Helicobacter pylori eradication in Japan
    • Murakami, K. et al. Multi-center randomized controlled study to establish the standard third-line regimen for Helicobacter pylori eradication in Japan. J Gastroenterol. 48, 1128-35 (2013).
    • (2013) J Gastroenterol. , vol.48 , pp. 1128-1135
    • Murakami, K.1
  • 5
    • 0028029963 scopus 로고
    • Coccoid forms of Helicobacter pylori in the human stomach
    • Chan, W. Y. et al. Coccoid forms of Helicobacter pylori in the human stomach. Am. J. Clin. Pathol. 102, 503-507 (1994).
    • (1994) Am. J. Clin. Pathol. , vol.102 , pp. 503-507
    • Chan, W.Y.1
  • 6
    • 0028610509 scopus 로고
    • Electron microscopic study of association between Helicobacter pylori and gastric and duodenal mucosa
    • Noach, L. et al. Electron microscopic study of association between Helicobacter pylori and gastric and duodenal mucosa. J. Clin. Pathol. 47, 699-704 (1994).
    • (1994) J. Clin. Pathol. , vol.47 , pp. 699-704
    • Noach, L.1
  • 7
    • 0034530139 scopus 로고    scopus 로고
    • Effect of teprenone on gastric mucosal injury induced by Helicobacter pylori in rats
    • Saita, H. & Murakami, M. Effect of teprenone on gastric mucosal injury induced by Helicobacter pylori in rats. Arzneimittelforschung. 50, 1110-4 (2000).
    • (2000) Arzneimittelforschung , vol.50 , pp. 1110-1114
    • Saita, H.1    Murakami, M.2
  • 8
    • 3342881872 scopus 로고    scopus 로고
    • Geranylgeranylacetone attenuates suppression by Helicobacter pylori extract of human umbilical vein epithelial cell growth
    • Tatsuta, M. et al. Geranylgeranylacetone attenuates suppression by Helicobacter pylori extract of human umbilical vein epithelial cell growth. Hepatogastroenterology. 51, 1558-60 (2004).
    • (2004) Hepatogastroenterology , vol.51 , pp. 1558-1560
    • Tatsuta, M.1
  • 9
    • 11144353819 scopus 로고    scopus 로고
    • Teprenone, but not H2-receptor blocker or sucralfate, suppresses corpus Helicobacter pylori colonization and gastritis in humans: Teprenone inhibition of H. pylori-induced interleukin-8 in MKN28 gastric epithelial cell lines
    • Miyake, K. et al. Teprenone, but not H2-receptor blocker or sucralfate, suppresses corpus Helicobacter pylori colonization and gastritis in humans: teprenone inhibition of H. pylori-induced interleukin-8 in MKN28 gastric epithelial cell lines. Helicobacter. 9, 130-7 (2004).
    • (2004) Helicobacter , vol.9 , pp. 130-137
    • Miyake, K.1
  • 10
    • 0036918371 scopus 로고    scopus 로고
    • Suppression of Helicobacter pylori-induced interleukin-8 production in gastric cancer cell lines by an anti-ulcer drug, geranylgeranylacetone
    • Yoshimura, N. et al. Suppression of Helicobacter pylori-induced interleukin-8 production in gastric cancer cell lines by an anti-ulcer drug, geranylgeranylacetone. J. Gastroenterol. Hepatol. 17, 1153-60 (2002).
    • (2002) J. Gastroenterol. Hepatol. , vol.17 , pp. 1153-1160
    • Yoshimura, N.1
  • 11
    • 0030038266 scopus 로고    scopus 로고
    • Geranylgeranylacetone induces heat shock proteins in cultured guinea pig gastric mucosal cells and rat gastric mucosa
    • Hirakawa, T. et al. Geranylgeranylacetone induces heat shock proteins in cultured guinea pig gastric mucosal cells and rat gastric mucosa. Gastroenterology. 11, 345-57 (1996).
    • (1996) Gastroenterology , vol.11 , pp. 345-357
    • Hirakawa, T.1
  • 12
    • 28844469267 scopus 로고    scopus 로고
    • Geranylgeranylacetone, a heat shock protein inducer, prevents acoustic injury in the guinea pig
    • Mikuriya, T. et al. Geranylgeranylacetone, a heat shock protein inducer, prevents acoustic injury in the guinea pig. Brain Res. 1065, 107-14 (2005).
    • (2005) Brain Res. , vol.1065 , pp. 107-114
    • Mikuriya, T.1
  • 13
    • 0035834026 scopus 로고    scopus 로고
    • Single oral of geranylgeranylacetone induces heat shock protein 72 and renders protection against ischemia/reperfusion injury in rat heart
    • Ooie, T. et al. Single oral of geranylgeranylacetone induces heat shock protein 72 and renders protection against ischemia/reperfusion injury in rat heart. Circulation. 104, 1837-43 (2001).
    • (2001) Circulation , vol.104 , pp. 1837-1843
    • Ooie, T.1
  • 14
    • 15944387661 scopus 로고    scopus 로고
    • Geranylgeranylacetone suppresses inflammatory responses and improves survival after massive hepatectomy in rats
    • Oda, H. et al. Geranylgeranylacetone suppresses inflammatory responses and improves survival after massive hepatectomy in rats. J. Gastrointest. Surg. 6, 464-72 (2002).
    • (2002) J. Gastrointest. Surg. , vol.6 , pp. 464-472
    • Oda, H.1
  • 15
    • 33644668963 scopus 로고    scopus 로고
    • Geranylgeranylacetone, a noninvasive heat shock protein inducer, induces protein kinase C and leads to neuroprotection against cerebral infarction in rats
    • Uchida, S. et al. Geranylgeranylacetone, a noninvasive heat shock protein inducer, induces protein kinase C and leads to neuroprotection against cerebral infarction in rats. Neurosci. Lett. 396, 220-4 (2006).
    • (2006) Neurosci. Lett. , vol.396 , pp. 220-224
    • Uchida, S.1
  • 16
    • 33644854119 scopus 로고    scopus 로고
    • Protective effect of geranylgeranylacetone on trinitrobenzene sulfonic acid-induced colitis in mice
    • Ohkawara, T. et al. Protective effect of geranylgeranylacetone on trinitrobenzene sulfonic acid-induced colitis in mice. Int. J. Mol. Med. 17, 229-34 (2006).
    • (2006) Int. J. Mol. Med. , vol.17 , pp. 229-234
    • Ohkawara, T.1
  • 17
    • 0029887140 scopus 로고    scopus 로고
    • The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding
    • Freeman, B. C. & Morimoto R. I. The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. EMBO J. 15, 2969-79 (1996).
    • (1996) EMBO J. , vol.15 , pp. 2969-2979
    • Freeman, B.C.1    Morimoto, R.I.2
  • 18
    • 0023131188 scopus 로고
    • The ATPase core of a clathrin uncoating protein
    • Chappell, T. G. et al. The ATPase core of a clathrin uncoating protein. J. Biol. Chem. 262, 746-51 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 746-751
    • Chappell, T.G.1
  • 19
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • Flaherty, K. M. et al. Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature. 346, 623-8 (1990).
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1
  • 20
    • 0027433805 scopus 로고
    • Identification of the peptide binding domain of hsc70. 18-Kilodalton fragment located immediately after ATPase domain is sufficient for high affinity binding
    • Wang, T.-F. et al. Identification of the peptide binding domain of hsc70. 18-Kilodalton fragment located immediately after ATPase domain is sufficient for high affinity binding. J. Biol. Chem. 268, 26049-26051 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 26049-26051
    • Wang, T.-F.1
  • 21
    • 0029038683 scopus 로고
    • The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology
    • Morghauser, R. C. et al. The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology Biochemistry 34, 6261-6266 (1995).
    • (1995) Biochemistry , vol.34 , pp. 6261-6266
    • Morghauser, R.C.1
  • 22
    • 0028268243 scopus 로고
    • Kinetics of molecular chaperone action
    • Schmid, D. et al. Kinetics of molecular chaperone action. Science 263, 971-973 (1994).
    • (1994) Science , vol.263 , pp. 971-973
    • Schmid, D.1
  • 23
    • 0028850872 scopus 로고
    • Effect of nucleotide on the binding of peptides to 70-kDa heat shock protein
    • Greene, L. E. et al. Effect of nucleotide on the binding of peptides to 70-kDa heat shock protein J. Biol. Chem. 270, 2967-2973 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 2967-2973
    • Greene, L.E.1
  • 24
    • 33845755480 scopus 로고    scopus 로고
    • The induction mechanism of the molecular chaperone HSP70 in the gastric mucosa by Geranylgeranylacetone (HSP-inducer)
    • Otaka, M. et al. The induction mechanism of the molecular chaperone HSP70 in the gastric mucosa by Geranylgeranylacetone (HSP-inducer). Biochem. Biophys. Res. Commun. 353, 399-404 (2007).
    • (2007) Biochem. Biophys. Res. Commun. , vol.353 , pp. 399-404
    • Otaka, M.1
  • 25
    • 0027652761 scopus 로고
    • Antibacterial activity of teprenone, a non water-soluble antiulcer agent, against Helicobacter pylori
    • Ishii, E. Antibacterial activity of teprenone, a non water-soluble antiulcer agent, against Helicobacter pylori. Zentralbl. Bakteriol. 280, 239-43 (1993).
    • (1993) Zentralbl. Bakteriol. , vol.280 , pp. 239-243
    • Ishii, E.1
  • 26
    • 84889589086 scopus 로고    scopus 로고
    • Helicobacter pylori and interleukin-8 in gastric cancer
    • Lee, K. E. et al. Helicobacter pylori and interleukin-8 in gastric cancer. World J Gastroenterol. 19, 8192-202 (2013).
    • (2013) World J Gastroenterol. , vol.19 , pp. 8192-8202
    • Lee, K.E.1
  • 27
    • 34548297296 scopus 로고    scopus 로고
    • Geranylgeranylacetone protects the human gastric mucosa from diclofenac-induced injury via induction of heat shock protein 70
    • Yanaka, A. et al. Geranylgeranylacetone protects the human gastric mucosa from diclofenac-induced injury via induction of heat shock protein 70. Digestion 75, 148-155 (2007).
    • (2007) Digestion , vol.75 , pp. 148-155
    • Yanaka, A.1
  • 28
    • 0032706190 scopus 로고    scopus 로고
    • Competition of various β-lactam antibiotics for the major penicillin-binding proteins of Helicobacter pylori: Antibacterial activity and effects on bacterial morphology
    • DeLoney, C. R. & Schiller, N. L. Competition of various β-lactam antibiotics for the major penicillin-binding proteins of Helicobacter pylori: antibacterial activity and effects on bacterial morphology. Antimicrob. Agents. Chemother. 43, 2702-9 (1999).
    • (1999) Antimicrob. Agents. Chemother. , vol.43 , pp. 2702-2709
    • DeLoney, C.R.1    Schiller, N.L.2
  • 29
    • 0029156456 scopus 로고
    • Bactericidal and morphological effects of amoxicillin on Helicobacter pylori
    • Berry, V. et al. Bactericidal and morphological effects of amoxicillin on Helicobacter pylori. Antimicrob. Agents. Chemother. 39, 1859-61 (1995).
    • (1995) Antimicrob. Agents. Chemother. , vol.39 , pp. 1859-1861
    • Berry, V.1
  • 30
    • 0345020432 scopus 로고    scopus 로고
    • Risk of development of in vitro resistance to amoxicillin, clarithromycin, and metronidazole in Helicobacter pylori
    • Sorberg, M. et al. Risk of development of in vitro resistance to amoxicillin, clarithromycin, and metronidazole in Helicobacter pylori. Antimicrob. Agents. Chemother. 42, 1222-8 (1998).
    • (1998) Antimicrob. Agents. Chemother. , vol.42 , pp. 1222-1228
    • Sorberg, M.1
  • 31
    • 84864543674 scopus 로고    scopus 로고
    • Factors modulating the outcome of treatment for the eradication of Helicobacter pylori infection
    • Figura, N. et al. Factors modulating the outcome of treatment for the eradication of Helicobacter pylori infection. New Microbiol. 35, 335-40 (2012).
    • (2012) New Microbiol. , vol.35 , pp. 335-340
    • Figura, N.1
  • 32
    • 0033984890 scopus 로고    scopus 로고
    • Helicobacter pylori: Cultivability and antibiotic susceptibility of coccoid forms
    • Brenciaglia, M. I. et al. Helicobacter pylori: cultivability and antibiotic susceptibility of coccoid forms. Int. J. Antimicrob. Agents. 13, 237-41 (2000).
    • (2000) Int. J. Antimicrob. Agents. , vol.13 , pp. 237-241
    • Brenciaglia, M.I.1
  • 33
    • 0030088822 scopus 로고    scopus 로고
    • Susceptibility of Helicobacter pylori to the bactericidal activity of human serum
    • Gonzalez-Valencia, G. et al. Susceptibility of Helicobacter pylori to the bactericidal activity of human serum. Helicobacter. 1, 28-33 (1996).
    • (1996) Helicobacter , vol.1 , pp. 28-33
    • Gonzalez-Valencia, G.1
  • 34
    • 0035977010 scopus 로고    scopus 로고
    • Distinct mechanism of Helicobacter pylori-mediated NF-κB activation between gastric cancer cells and monocytic cells
    • Maeda, S. et al. Distinct mechanism of Helicobacter pylori-mediated NF-κB activation between gastric cancer cells and monocytic cells. J. Biol. Chem. 276, 44856-64 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 44856-44864
    • Maeda, S.1
  • 35
    • 30644474993 scopus 로고    scopus 로고
    • NF-κB and ERK-signaling pathways contribute to the gene expression induced by cag PAI-positive-Helicobacter pylori infection
    • Shibata, W. et al. NF-κB and ERK-signaling pathways contribute to the gene expression induced by cag PAI-positive-Helicobacter pylori infection. World J Gastroenterol. 11, 6134-43 (2005).
    • (2005) World J Gastroenterol. , vol.11 , pp. 6134-6143
    • Shibata, W.1
  • 36
    • 79953702794 scopus 로고    scopus 로고
    • Role of the cag-pathogenicity island encoded type IV secretion system in Helicobacter pylori pathogenesis
    • Review
    • Tegtmeyer, N. et al. Role of the cag-pathogenicity island encoded type IV secretion system in Helicobacter pylori pathogenesis. FEBS J. 278, 1190-202 (2011). Review.
    • (2011) FEBS J. , vol.278 , pp. 1190-1202
    • Tegtmeyer, N.1
  • 37
    • 79953707331 scopus 로고    scopus 로고
    • Structural and functional aspects of unique type IV secretory components in the Helicobacter pylori cag-pathogenicity island
    • Cendron, L. & Zanotti, G. Structural and functional aspects of unique type IV secretory components in the Helicobacter pylori cag-pathogenicity island. FEBS J. 278, 1223-31 (2011).
    • (2011) FEBS J. , vol.278 , pp. 1223-1231
    • Cendron, L.1    Zanotti, G.2
  • 38
    • 84878379759 scopus 로고    scopus 로고
    • Assessment of cagE and babA mRNA expression during morphological conversion of Helicobacter pylori from spiral to coccoid
    • Poursina, F. et al. Assessment of cagE and babA mRNA expression during morphological conversion of Helicobacter pylori from spiral to coccoid. Curr. Microbiol. 66, 406-13 (2012).
    • (2012) Curr. Microbiol. , vol.66 , pp. 406-413
    • Poursina, F.1
  • 39
    • 0033520946 scopus 로고    scopus 로고
    • Mammalian HSP60 is a major target for an immunosuppressant mizoribine
    • Itoh, H. et al. Mammalian HSP60 is a major target for an immunosuppressant mizoribine. J. Biol. Chem. 274, 35147-35151 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 35147-35151
    • Itoh, H.1
  • 40
    • 2342430914 scopus 로고    scopus 로고
    • 73-kDa molecular chaperone HSP73 is a direct target of antibiotic gentamicin
    • Miyazaki, T. et al. 73-kDa molecular chaperone HSP73 is a direct target of antibiotic gentamicin. J. Biol. Chem. 279, 17295-17300 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 17295-17300
    • Miyazaki, T.1
  • 41
    • 0032987678 scopus 로고    scopus 로고
    • Colony formation by Helicobacter pylori after long-term incubation under anaerobic conditions
    • Yamaguchi, H. Colony formation by Helicobacter pylori after long-term incubation under anaerobic conditions. FEMS Microbiol. Lett. 175, 107-111 (1999).
    • (1999) FEMS Microbiol. Lett. , vol.175 , pp. 107-111
    • Yamaguchi, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.