- About this Journal ·
- Abstracting and Indexing ·
- Aims and Scope ·
- Article Processing Charges ·
- Articles in Press ·
- Author Guidelines ·
- Bibliographic Information ·
- Citations to this Journal ·
- Contact Information ·
- Editorial Board ·
- Editorial Workflow ·
- Free eTOC Alerts ·
- Publication Ethics ·
- Reviewers Acknowledgment ·
- Submit a Manuscript ·
- Subscription Information ·
- Table of Contents
International Journal of Proteomics
Volume 2010 (2010), Article ID 259163, 11 pages
Heat Shock Protein: Hard Worker or Bad Offender for Gastric Diseases
1Laboratory of Chemoprevention, Lee Gil Ya Cancer and Diabetes Institute, Gachon University of Medicine and Science, Incheon, Republic of Korea
2Laboratory of Translational Medicine, Lee Gil Ya Cancer and Diabetes Institute, Gachon University of Medicine and Science, Incheon, Republic of Korea
3Laboratory of Cell Regulation and Carcinogenesis, Lee Gil Ya Cancer and Diabetes Institute, Gachon University of Medicine and Science, Incheon, Republic of Korea
4Department of Gastroenterology, Gachon Graduate School of Medicine Gil Medical Center, Songdo-dong 7-45, Yeonsu-gu, Incheon, 406-840, Republic of Korea
Received 28 June 2010; Accepted 5 September 2010
Academic Editor: Ho Jeong Kwon
Copyright © 2010 Ho-Jae Lee et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- B. Bukau and A. L. Horwich, “The Hsp70 and Hsp60 chaperone machines,” Cell, vol. 92, no. 3, pp. 351–366, 1998.
- C. Garrido, S. Gurbuxani, L. Ravagnan, and G. Kroemer, “Heat shock proteins: endogenous modulators of apoptotic cell death,” Biochemical and Biophysical Research Communications, vol. 286, no. 3, pp. 433–442, 2001.
- K. C. Kregel, “Invited review: heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance,” Journal of Applied Physiology, vol. 92, no. 5, pp. 2177–2186, 2002.
- H. M. Beere, “‘The stress of dying’: the role of heat shock proteins in the regulation of apoptosis,” Journal of Cell Science, vol. 117, no. 13, pp. 2641–2651, 2004.
- P. Mehlen, C. Kretz-Remy, X. Préville, and A.-P. Arrigo, “Human hsp27, Drosophila hsp27 and human αB-crystallin expression-mediated increase in glutathione is essential for the protective activity of these proteins against TNFα-induced cell death,” EMBO Journal, vol. 15, no. 11, pp. 2695–2706, 1996.
- L. J. Thompson and H. De Reuset, “Genomics of Helicobacter pylori,” Helicobacter, vol. 7, supplement 1, pp. 1–7, 2002.
- K. Herrmann, A. Walch, B. Balluff et al., “Proteomic and metabolic prediction of response to therapy in gastrointestinal cancers,” Nature Clinical Practice Gastroenterology and Hepatology, vol. 6, no. 3, pp. 170–183, 2009.
- L. Laine, K. Takeuchi, and A. Tarnawski, “Gastric mucosal defense and cytoprotection: bench to bedside,” Gastroenterology, vol. 135, no. 1, pp. 41–60, 2008.
- M. P. Mayer and B. Bukau, “Hsp70 chaperones: cellular functions and molecular mechanism,” Cellular and Molecular Life Sciences, vol. 62, no. 6, pp. 670–684, 2005.
- M. Yeo, H.-K. Park, D.-K. Kim et al., “Restoration of heat shock protein70 suppresses gastric mucosal inducible nitric oxide synthase expression induced by Helicobacter pylori,” Proteomics, vol. 4, no. 11, pp. 3335–3342, 2004.
- W. S. Axsen, C. M. Styer, and J. V. Solnick, “Inhibition of heat shock protein expression by Helicobacter pylori,” Microbial Pathogenesis, vol. 47, no. 4, pp. 231–236, 2009.
- P. Pierzchalski, A. Krawiec, A. Ptak-Belowska, A. Barańska, S. J. Konturek, and W. W. Pawlik, “The mechanism of heat-shock protein 70 gene expression abolition in gastric epithelium caused by Helicobacter pylori infection,” Helicobacter, vol. 11, no. 2, pp. 96–104, 2006.
- S. R. Choi, S. A. Lee, Y. J. Kim, C. Y. Ok, H. J. Lee, and K. B. Hahm, “Role of heat shock proteins in gastric inflammation and ulcer healing,” Journal of Physiology and Pharmacology, vol. 60, supplement 7, pp. 5–17, 2009.
- T. Y. Oh, M. Yeo, S. U. Han, et al., “Synergism of Helicobacter pylori infection and stress on the augmentation of gastric mucosal damage and its prevention with α-tocopherol,” Free Radical Biology and Medicine, vol. 38, no. 11, pp. 1447–1457, 2005.
- M. Yeo, H.-K. Park, K.-M. Lee et al., “Blockage of HSP 90 modulates Helicobacter pylori-induced IL-8 productions through the inactivation of transcriptional factors of AP-1 and NF-κB,” Biochemical and Biophysical Research Communications, vol. 320, no. 3, pp. 816–824, 2004.
- D. E. Taylor, R. N. Fedorak, and R. Sherburne, “Antigenic mimicry between Helicobacter pylori and gastric mucosa: failure to implicate heat-shock protein Hsp60 using immunoelectron microscopy,” Helicobacter, vol. 4, no. 3, pp. 148–153, 1999.
- S. K. Calderwood, M. A. Khaleque, D. B. Sawyer, and D. R. Ciocca, “Heat shock proteins in cancer: chaperones of tumorigenesis,” Trends in Biochemical Sciences, vol. 31, no. 3, pp. 164–172, 2006.
- D. R. Ciocca and S. K. Calderwood, “Heat shock proteins in cancer: diagnostic, prognostic, predictive, and treatment implications,” Cell Stress and Chaperones, vol. 10, no. 2, pp. 86–103, 2005.
- M. Sherman and G. Multhoff, “Heat shock proteins in cancer,” Annals of the New York Academy of Sciences, vol. 1113, pp. 192–201, 2007.
- T. Rogalla, M. Ehrnsperger, X. Preville et al., “Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor by phosphorylation,” Journal of Biological Chemistry, vol. 274, no. 27, pp. 18947–18956, 1999.
- D. N. Dhanasekaran and G. L. Johnson, “MAPKs: function, regulation, role in cancer and therapeutic targeting,” Oncogene, vol. 26, no. 22, pp. 3097–3099, 2007.
- Y. Kawahara, K. Yokota, M. Mizuno et al., “Antibodies to human gastric epithelial cells and heat shock protein 60 in Helicobacter pylori positive mucosa associated lymphoid tissue lymphoma,” Gut, vol. 45, no. 1, pp. 20–23, 1999.
- J. G. Fox and T. C. Wang, “Helicobacter pylori infection: pathogenesis,” Current Opinion in Gastroenterology, vol. 18, no. 1, pp. 15–25, 2002.
- L. Neckers, “Heat shock protein 90: the cancer chaperone,” Journal of Biosciences, vol. 32, no. 3, pp. 517–530, 2007.
- M. J. Blaser, G. I. Perez-Perez, H. Kleanthous et al., “Infection with Helicobacter pylori strains possessing cagA is associated with an increased risk of developing adenocarcinoma of the stomach,” Cancer Research, vol. 55, no. 10, pp. 2111–2115, 1995.
- S. Jang, K. R. Jones, C. H. Olsen et al., “Epidemiological link between gastric disease and polymorphisms in vacA and cagA,” Journal of Clinical Microbiology, vol. 48, no. 2, pp. 559–567, 2010.
- C. S. Lin, P. J. He, N. M. Tsai, et al., “A potential role for Helicobacter pylori heat shock protein 60 in gastric tumorigenesis,” Biochemical and Biophysical Research Communications, vol. 392, no. 2, pp. 183–189, 2010.
- A. Tarnawski, J. Stachura, D. Hollander, I. J. Sarfeh, and J. Bogdal, “Cellular aspects of alcohol-induced injury and prostaglandin protection of the human gastric mucosa: focus on the mucosal microvessels,” Journal of Clinical Gastroenterology, vol. 10, supplement 1, pp. S35–S45, 1988.
- A. Robert, J. E. Nezamis, C. Lancaster, and A. J. Hanchar, “Cytoprotection by prostaglandins in rats. Prevention of gastric necrosis produced by alcohol, HCl, NaOH, hypertonic NaCl, and thermal injury,” Gastroenterology, vol. 77, no. 3, pp. 433–443, 1979.
- M. Saika, T. Ueyama, and E. Senba, “Expression of immediate early genes, HSP70, and COX-2 mRNAS in rat stomach following ethanol ingestion,” Digestive Diseases and Sciences, vol. 45, no. 12, pp. 2455–2462, 2000.
- J. M. Jimenez-Lopez and A. I. Cederbaum, “Green tea polyphenol epigallocatechin-3-gallate protects HepG2 cells against CYP2E1-dependent toxicity,” Free Radical Biology and Medicine, vol. 36, no. 3, pp. 359–370, 2004.
- J.-S. Lee, T.-Y. Oh, Y.-K. Kim et al., “Protective effects of green tea polyphenol extracts against ethanol-induced gastric mucosal damages in rats: stress-responsive transcription factors and MAP kinases as potential targets,” Mutation Research, vol. 579, no. 1-2, pp. 214–224, 2005.
- A. S. Lee, “The glucose-regulated proteins: stress induction and clinical applications,” Trends in Biochemical Sciences, vol. 26, no. 8, pp. 504–510, 2001.
- S. Kai, M. Ohta, M. Tominaga, T. Matsumoto, T. Bandoh, and S. Kitano, “Reduction of ethanol-induced injury in portal hypertensive gastric mucosa of rats by induction of heat shock protein 72 by geranylgeranylacetone,” Wound Repair and Regeneration, vol. 15, no. 6, pp. 875–880, 2007.
- M. Tominaga, M. Ohta, S. Kai, K. Iwaki, K. Shibata, and S. Kitano, “Increased heat-shock protein 90 expression contributes to impaired adaptive cytoprotection in the gastric mucosa of portal hypertensive rats,” Journal of Gastroenterology and Hepatology, vol. 24, no. 6, pp. 1136–1141, 2009.
- M. Knuesel, Y. Wan, Z. Xiao et al., “Identification of novel protein-protein interactions using a versatile mammalian tandem affinity purification expression system,” Molecular & Cellular Proteomics, vol. 2, no. 11, pp. 1225–1233, 2003.
- S. K. Wandinger, K. Richter, and J. Buchner, “The Hsp90 chaperone machinery,” Journal of Biological Chemistry, vol. 283, no. 27, pp. 18473–18477, 2008.
- H. Xin, X. Xu, L. Li et al., “CHIP controls the sensitivity of transforming growth factor-β signaling by modulating the basal level of Smad3 through ubiquitin-mediated degradation,” Journal of Biological Chemistry, vol. 280, no. 21, pp. 20842–20850, 2005.
- H. McDonough and C. Patterson, “CHIP: a link between the chaperone and proteasome systems,” Cell Stress and Chaperones, vol. 8, no. 4, pp. 303–308, 2003.
- Q. Luo, E. Nieves, J. Kzhyshkowska, and R. H. Angeletti, “Endogenous transforming growth factor-β receptor-mediated Smad signaling complexes analyzed by mass spectrometry,” Molecular and Cellular Proteomics, vol. 5, no. 7, pp. 1245–1260, 2006.
- K. H. Wrighton, X. Lin, and X.-H. Feng, “Critical regulation of TGFβ signaling by Hsp90,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 27, pp. 9244–9249, 2008.
- W. B. Pratt and D. O. Toft, “Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery,” Experimental Biology and Medicine, vol. 228, no. 2, pp. 111–133, 2003.
- C. H. Yun, S. Y. Yoon, T. T. Nguyen, et al., “Geldanamycin inhibits TGF-beta signaling through induction of Hsp70,” Archives of Biochemistry and Biophysics, vol. 495, no. 1, pp. 8–13, 2010.
- C. Díez-Fernández, D. Andrés, and M. Cascales, “Attenuating effects of heat shock against TGF-β1-induced apoptosis in cultured rat hepatocytes,” Free Radical Biology and Medicine, vol. 33, no. 6, pp. 835–846, 2002.
- H. Mao, Z. Li, Y. Zhou et al., “HSP72 attenuates renal tubular cell apoptosis and interstitial fibrosis in obstructive nephropathy,” American Journal of Physiology, vol. 295, no. 1, pp. F202–F214, 2008.
- Y. Zhou, H. Mao, S. Li et al., “HSP72 inhibits smad3 activation and nuclear translocation in renal epithelial-to-mesenchymal transition,” Journal of the American Society of Nephrology, vol. 21, no. 4, pp. 598–609, 2010.