- About this Journal
- Abstracting and Indexing
- Aims and Scope
- Annual Issues
- 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
Journal of Biomedicine and Biotechnology
Volume 2011 (2011), Article ID 193052, 8 pages
Separation and Identification of HSP-Associated Protein Complexes from Pancreatic Cancer Cell Lines Using 2D CN/SDS-PAGE Coupled with Mass Spectrometry
Department of Biophysics and Structural Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences and School of Basic Medicine, Peking Union Medical College, Beijing 100005, China
Received 16 May 2011; Revised 12 August 2011; Accepted 17 August 2011
Academic Editor: Kapil Mehta
Copyright © 2011 Zhiyun Zhao 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.
- M. Abu-Farha, F. Elisma, and D. Figeys, “Identification of protein-protein interactions by mass spectrometry coupled techniques,” Advances in Biochemical Engineering/Biotechnology, vol. 110, pp. 67–80, 2008.
- F. Krause, “Detection and analysis of protein-protein interactions in organellar and prokaryotic proteomes by native gel electrophoresis: (Membrane) protein complexes and supercomplexes,” Electrophoresis, vol. 27, no. 13, pp. 2759–2781, 2006.
- A. J. Link, T. C. Fleischer, C. M. Weaver, V. R. Gerbasi, and J. L. Jennings, “Purifying protein complexes for mass spectrometry: applications to protein translation,” Methods, vol. 35, no. 3, pp. 274–290, 2005.
- R. P. Bahadur and M. Zacharias, “The interface of protein-protein complexes: analysis of contacts and prediction of interactions,” Cellular and Molecular Life Sciences, vol. 65, no. 7-8, pp. 1059–1072, 2008.
- X. Xu, Y. Song, Y. Li, J. Chang, H. Zhang, and L. An, “The tandem affinity purification method: an efficient system for protein complex purification and protein interaction identification,” Protein Expression and Purification, vol. 72, no. 2, pp. 149–156, 2010.
- E. A. Elion, “Detection of protein-protein interactions by coprecipitation,” Current Protocols in Neuroscience, 2006, chapter 5, Unit 5.25.
- B. Suter, S. Kittanakom, and I. Stagljar, “Two-hybrid technologies in proteomics research,” Current Opinion in Biotechnology, vol. 19, no. 4, pp. 316–323, 2008.
- I. Wittig and H. Schägger, “Native electrophoretic techniques to identify protein-protein interactions,” Proteomics, vol. 9, no. 23, pp. 5214–5223, 2009.
- X. Wang, G. Chen, H. Liu, Z. Zhao, and Z. Li, “Four-dimensional orthogonal electrophoresis system for screening protein complexes and protein-protein interactions combined with mass spectrometry,” Journal of Proteome Research, vol. 9, no. 10, pp. 5325–5334, 2010.
- I. Wittig and H. Schägger, “Advantages and limitations of clear-native PAGE,” Proteomics, vol. 5, no. 17, pp. 4338–4346, 2005.
- I. Wittig and H. Schägger, “Features and applications of blue-native and clear-native electrophoresis,” Proteomics, vol. 8, no. 19, pp. 3974–3990, 2008.
- F. Krause and H. Seelert, “Detection and analysis of protein-protein interactions of organellar and prokaryotic proteomes by blue native and colorless native gel electrophoresis,” Current Protocols in Protein Science, 2008, chapter 14, unit 14.11.
- V. Reisinger and L. A. Eichacker, “Analysis of membrane protein complexes by blue native PAGE,” Proteomics, vol. 1, supplement 2, pp. 6–15, 2006.
- M. Kügler, L. Jänsch, V. Kruft, U. K. Schmitz, and H. P. Braun, “Analysis of the chloroplast protein complexes by blue-native polyacrylamide gel electrophoresis (BN-PAGE),” Photosynthesis Research, vol. 53, no. 1, pp. 35–44, 1997.
- L. G. J. Nijtmans, N. S. Henderson, and I. J. Holt, “Blue Native electrophoresis to study mitochondrial and other protein complexes,” Methods, vol. 26, no. 4, pp. 327–334, 2002.
- P. S. Brookes, A. Pinner, A. Ramachandran et al., “High throughput two-dimensional blue-native electrophoresis: a tool for functional proteomics of mitochondria and signaling complexes,” Proteomics, vol. 2, no. 8, pp. 969–977, 2002.
- T. Manabe and Y. Jin, “Noncovalent interactions in human plasma proteins analyzed by the comparison of nondenaturing and denaturing micro-2-D gel electrophoresis patterns after polypeptide assignment using matrix-assisted laser desorption/ionization-mass spectrometry and peptide mass fingerprinting,” Electrophoresis, vol. 29, no. 12, pp. 2672–2688, 2008.
- S. Sunderhaus, H. Eubel, and H. P. Braun, “Two-dimensional blue native/blue native polyacrylamide gel electrophoresis for the characterization of mitochondrial protein complexes and supercomplexes,” Methods in Molecular Biology, vol. 372, pp. 315–324, 2007.
- K. Liu, L. Qian, J. Wang et al., “Two-dimensional blue native/SDS-PAGE analysis reveals heat shock protein chaperone machinery involved in hepatitis B virus production in HepG2.2.15 cells,” Molecular and Cellular Proteomics, vol. 8, no. 3, pp. 495–505, 2009.
- M. M. Camacho-Carvcajal, B. Wollscheid, R. Aebersold, V. Steimle, and W. W. A. Schamel, “Two-dimensional Blue Native/SDS gel electrophoresiss of multi-protein complexes from whole cellular lysates: a proteomics approach,” Molecular and Cellular Proteomics, vol. 3, no. 2, pp. 176–182, 2004.
- A. Jemal, R. Siegel, E. Ward et al., “Cancer statistics, 2006,” CA-A Cancer Journal for Clinicians, vol. 56, no. 2, pp. 106–130, 2006.
- P. Ghaneh, E. Costello, and J. P. Neoptolemos, “Biology and management of pancreatic cancer,” Postgraduate Medical Journal, vol. 84, no. 995, pp. 478–497, 2008.
- V. Dudeja, S. M. Vickers, and A. K. Saluja, “The role of heat shock proteins in gastrointestinal diseases,” Gut, vol. 58, no. 7, pp. 1000–1009, 2009.
- L. Tutar and Y. Tutar, “Heat shock proteins; An overview,” Current Pharmaceutical Biotechnology, vol. 11, no. 2, pp. 216–222, 2010.
- A. L. Joly, G. Wettstein, G. Mignot, F. Ghiringhelli, and C. Garrido, “Dual role of heat shock proteins as regulators of apoptosis and innate immunity,” Journal of Innate Immunity, vol. 2, no. 3, pp. 238–247, 2010.
- V. V. Malaitsev, I. M. Bogdanova, and O. V. Makarova, “Heat shock proteins and their role in the development of pathological processes,” Arkhiv Patologii, vol. 70, no. 6, pp. 31–38, 2008.
- A. Di Pietro, G. Tosti, P. F. Ferrucci, and A. Testori, “Heat shock protein peptide complex 96-based vaccines in melanoma: how far we are, how far we can get,” Human Vaccines, vol. 5, no. 11, pp. 727–737, 2009.
- Y. Oki and A. Younes, “Heat shock protein-based cancer vaccines,” Expert Review of Vaccines, vol. 3, no. 4, pp. 403–411, 2004.
- A. Saluja and V. Dudeja, “Heat shock proteins in pancreatic diseases,” Journal of Gastroenterology and Hepatology, vol. 23, supplement 1, pp. S42–S45, 2008.
- T. M. Gress, F. Müller-Pillasch, C. Weber et al., “Differential expression of heat shock proteins in pancreatic carcinoma,” Cancer Research, vol. 54, no. 2, pp. 547–551, 1994.
- S. Elsasser, M. Schmidt, and D. Finley, “Characterization of the proteasome using native gel electrophoresis,” Methods in Enzymology, vol. 398, pp. 353–363, 2005.
- G. Chen, Y. Luo, X. Wang et al., “A relatively simple and economical protocol for proteomic analyses of human 20S proteasome: compatible with both scaled-up and scaled-down purifications,” Electrophoresis, vol. 30, no. 14, pp. 2422–2430, 2009.
- N. H. Reifschneider, S. Goto, H. Nakamoto et al., “Defining the mitochondrial proteomes from five rat organs in a physiologically significant context using 2D blue-native/SDS-PAGE,” Journal of Proteome Research, vol. 5, no. 5, pp. 1117–1132, 2006.
- J. C. Christianson, T. A. Shaler, R. E. Tyler, and R. R. Kopito, “OS-9 and GRP94 deliver mutant α1-antitrypsin to the Hrd1?SEL1L ubiquitin ligase complex for ERAD,” Nature Cell Biology, vol. 10, no. 3, pp. 272–282, 2008.
- X. Chen, D. Eastonb, H.-J. Oh, D.-S. Lee-Yoon, X. Liu, and J. Subjeck, “The 170 kDa glucose regulated stress protein is a large HSP70-, HSP110-like protein of the endoplasmic reticulum,” FEBS Letters, vol. 380, no. 1-2, pp. 68–72, 1996.
- H. Coe and M. Michalak, “ERp57, a multifunctional endoplasmic reticulum resident oxidoreductase,” International Journal of Biochemistry and Cell Biology, vol. 42, no. 6, pp. 796–799, 2010.
- J. Trepel, M. Mollapour, G. Giaccone, and L. Neckers, “Targeting the dynamic HSP90 complex in cancer,” Nature Reviews Cancer, vol. 10, no. 8, pp. 537–549, 2010.
- H. Hao, Y. Naomoto, X. Bao et al., “HSP90 and its inhibitors,” Oncology Reports, vol. 23, no. 6, pp. 1483–1492, 2010.
- C. E. Jessop, R. H. Watkins, J. J. Simmons, M. Tasab, and N. J. Bulleid, “Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins,” Journal of Cell Science, vol. 122, no. 23, pp. 4287–4295, 2009.
- Z. Yang, C. W. Lanks, and L. Tong, “Molecular mechanism for the regulation of human mitochondrial NAD(P)+-Dependent malic enzyme by ATP and umarate,” Structure, vol. 10, no. 7, pp. 951–960, 2002.
- K. Honda, T. Yamada, R. Endo et al., “Actinin-4, a novel actin-bundling protein associated with cell motility and cancer invasion,” Journal of Cell Biology, vol. 140, no. 6, pp. 1383–1393, 1998.
- X. Yang, Y. Hu, D. H. Yin et al., “Catalytic strategy of S-Adenosyl-L-homocysteine hydrolase: transition-state stabilization and the avoidance of abortive reactions,” Biochemistry, vol. 42, no. 7, pp. 1900–1909, 2003.
- F. Cappello, E. C. de Macario, L. Marasà, G. Zummo, and A. J. Macario, “Hsp60 expression, new locations, functions and perspectives for cancer diagnosis and therapy,” Cancer Biology & Therapy, vol. 7, no. 6, pp. 801–809, 2008.
- D. Tondeleir, D. Vandamme, J. Vandekerckhove, C. Ampe, and A. Lambrechts, “Actin isoform expression patterns during mammalian development and in pathology: insights from mouse models,” Cell Motility and the Cytoskeleton, vol. 66, no. 10, pp. 798–815, 2009.
- F. Ren, H. Wu, Y. Lei et al., “Quantitative proteomics identification of phosphoglycerate mutase 1 as a novel therapeutic target in hepatocellular carcinoma,” Molecular Cancer, vol. 9, article 81, 2010.
- M. Nakamura, H. Morisawa, S. Imajoh-Ohmi, C. Takamura, H. Fukuda, and T. Toda, “Proteomic analysis of protein complexes in human SH-SY5Y neuroblastoma cells by using blue-native gel electrophoresis: an increase in lamin A/C associated with heat shock protein 90 in response to 6-hydroxydopamine-induced oxidative stress,” Experimental Gerontology, vol. 44, no. 6-7, pp. 375–382, 2009.
- H. P. Kim, D. Morse, and A. M. K. Choi, “Heat-shock proteins: new keys to the development of cytoprotective therapies,” Expert Opinion on Therapeutic Targets, vol. 10, no. 5, pp. 759–769, 2006.
- E. M. Karapanagiotou, K. Syrigos, and M. W. Saif, “Heat shock protein inhibitors and vaccines as new agents in cancer treatment,” Expert Opinion on Investigational Drugs, vol. 18, no. 2, pp. 161–174, 2009.
- A. P. Kyriazis, W. B. McCombs, and A. A. Sandberg, “Establishment and characterization of human pancreatic adenocarcinoma cell line SW-1990 in tissue culture and the nude mouse,” Cancer Research, vol. 43, no. 9, pp. 4393–4401, 1983.
- M. E. Madden and M. P. Sarras, “Morphological and biochemical characterization of a human pancreatic ductal cell line (PANC-1),” Pancreas, vol. 3, no. 5, pp. 512–528, 1988.
- S. Ishigaki, N. Hishikawa, J. I. Niwa et al., “Physical and functional interaction between dorfin and valosin-containing protein that are colocalized in ubiquitylated inclusions in neurodegenerative disorders,” The Journal of Biological Chemistry, vol. 279, no. 49, pp. 51376–51385, 2004.
- K. E. Hung, V. Faca, K. Song et al., “Comprehensive proteome analysis of an Apc mouse model uncovers proteins associated with intestinal tumorigenesis,” Cancer Prevention Research, vol. 2, no. 3, pp. 224–233, 2009.
- J. C. Ghosh, T. Dohi, H. K. Byoung, and D. C. Altieri, “Hsp60 regulation of tumor cell apoptosis,” The Journal of Biological Chemistry, vol. 283, no. 8, pp. 5188–5194, 2008.
- T. Qi, J. Han, Y. Cui, M. Zong, X. Liu, and B. Zhu, “Comparative proteomic analysis for the detection of biomarkers in pancreatic ductal adenocarcinomas,” Journal of Clinical Pathology, vol. 61, no. 1, pp. 49–58, 2008.
- K. Mehta, “Biological and therapeutic significance of tissue transglutaminase in pancreatic cancer,” Amino Acids, vol. 36, no. 4, pp. 709–716, 2009.
- G. Di Giacomo, A. Lentini, S. Beninati, M. Piacentini, and C. Rodolfo, “In vivo evaluation of type 2 transglutaminase contribution to the metastasis formation in melanoma,” Amino Acids, vol. 36, no. 4, pp. 717–724, 2009.
- N. Chen, W. Sun, X. Deng et al., “Quantitative proteome analysis of HCC cell lines with different metastatic potentials by SILAC,” Proteomics, vol. 8, no. 23-24, pp. 5108–5118, 2008.
- T. Grewal, M. Koese, C. Rentero, and C. Enrich, “Annexin A6-regulator of the EGFR/Ras signalling pathway and cholesterol homeostasis,” International Journal of Biochemistry and Cell Biology, vol. 42, no. 5, pp. 580–584, 2010.