Proteomic analysis of human osteoarthritic chondrocytes reveals protein changes in stress and glycolysis

Proteomics

Volumn 8, Issue 3, 2008, Pages 495-507

  Ruiz Romero, Cristina ^a   Carreira, Vanessa ^a   Rego, Ignacio ^a   Remeseiro, Silvia ^a   López Armada, María J ^a   Blanco, Francisco J ^a  

^a HOSPITAL JUAN CANALEJO   (Spain)

Author keywords

Apoptosis; Chondrocytes; GRP78; HSP90; Nitric oxide; Osteoarthritis

Indexed keywords

ENOLASE; FRUCTOSE BISPHOSPHATE ALDOLASE; GLUCOSE REGULATED PROTEIN 78; GLUTATHIONE TRANSFERASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HEAT SHOCK PROTEIN 90; PROTEIN;

ARTICLE; CARTILAGE CELL; CARTILAGE DEGENERATION; CELL ISOLATION; CELLULAR STRESS RESPONSE; CONTROLLED STUDY; GLYCOLYSIS; HUMAN; HUMAN CELL; IMMUNOHISTOCHEMISTRY; JOINT PROSTHESIS; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NUCLEOTIDE SEQUENCE; OSTEOARTHRITIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN METABOLISM; PROTEIN STRUCTURE; PROTEIN TARGETING; PROTEOMICS; STAINING; TWO DIMENSIONAL GEL ELECTROPHORESIS; WESTERN BLOTTING;

CARTILAGE, ARTICULAR; CELLS, CULTURED; CHONDROCYTES; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; GLYCOLYSIS; HUMANS; ORGANOMETALLIC COMPOUNDS; OSTEOARTHRITIS, KNEE; PROTEOME; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 39149086750     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200700249     Document Type: Article

References (38)

1. Pritzker, K. P. H., in: Brandt, K. D., Doherty, M., Lohmander, L. S. (Eds.),Osteoarthritis, Oxford University Press, NY 1998, pp. 50-61.
2. López-Armada, M. J., Carames, B., Cillero-Pastor, B., Blanco, F. J., Fisiopatología de la Artrosis ¿cuál es la actualidad? Rev. Esp. Reum. 2004, 31, 379-393.
3. Heinegard, D., Bayliss, M., Lorenzo, P., in: Brandt, K. D., Doherty, M., Lohmander, L. S. (Eds.), Osteoarthritis, Oxford University Press, NY 1998, pp. 74-84.
4. Lotz, M., Blanco, F. J., von Kempis, J., Dudler, J. et al., Cytokine regulation of chondrocyte functions. J. Rheumatol. 1995, 43, 104-108.
5. Görg, A., Weiss, W., Dunn, M. J., Current two-dimensional electrophoresis technology for proteomics. Proteomics 2004, 4, 3665-3685.
6. Ruiz-Romero, C., Lopez-Armada, M. J., Blanco, F. J., Proteomic characterization of human normal articular chondrocytes: A novel tool for the study of osteoarthritis and other rheumatic diseases. Proteomics 2005, 5, 3048-3059.
7. De Ceuninck, F., Marcheteau, E., Berger, S., Caliez, A. et al., Assessment of some tools for the characterization of human osteoarthritic cartilage proteome. J. Biomol. Technol. 2005, 16, 256-265.
8. Hermansson, M., Sawaji, Y., Bolton, M., Alexander, S. et al., Proteomic analysis of articular cartilage shows increased type II collagen synthesis in osteoarthritis and expression of inhibin betaA (activin A), a regulatory molecule for chondrocytes. J. Biol. Chem. 2004, 279, 43514-43521.
9. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-684.
10. Schevchenko, V. A., Akayeva, E. A., Yeliseyeva, I. M., Yelisova, T. V. et al., Human cytogenetic consequences of the Chernobyl accident. Mutat. Res. 1996, 361, 29-34.
11. Sechi, S., Chait, B. T., Modification of cysteine residues by alkylation. A tool in peptide mapping and protein identification. Anal. Chem. 1998, 70, 5150-5158.
12. Kang, H. S., Welch, W. J., Characterization and purification of the 94-kDa glucose-regulated protein. J. Biol. Chem. 1991, 266, 5643-5649.
13. Little, E., Ramakrishnan, M., Roy, B., Gazit, G., Lee, A. S., The glucose-regulated proteins (GRP78 and GRP94): Functions, gene regulation, and applications. Crit. Rev. Eukaryot. Gene Expr. 1994, 4, 1-18.
14. The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review. Pharmacol. Ther. 1998, 79, 129-168.
15. Flores-Diaz, M., Higuita, J. C., Florin, I., Okada, T. et al., A cellular UDP-glucose deficiency causes over-expression of glucose/oxygen- regulated proteins independent of the endoplasmic reticulum stress elements. J. Biol. Chem. 2004, 279, 21724-21731.
16. Liu, H., Bowes, R. C., III, van de Water, B., Sillence, C., Nagelkerke, J. F., Stevens, J. L., Endoplasmic reticulum chaperones GRP78 and calreticulin prevent oxidative stress, Ca2+ disturbances, and cell death in renal epithelial cells. J. Biol. Chem. 1997, 272, 21751-21759.
17. Fehrenbach, E., Niess, A. M., Role of heat shock proteins in the exercise response. Exerc. Immunol. Rev. 1999, 5, 57-77.
18. Kubo, T., Towle, C. A., Mankin, H. J., Treadwell, B. V., Stress-induced proteins in chondrocytes from patients with osteoarthritis. Arthritis Rheum. 1985, 28, 1140-1145.
19. Johnson, K., Svensson, C. I., Etten, D. V., Ghosh, S. S. et al., Mediation of spontaneous knee osteoarthritis by progressive chondrocyte ATP depletion in Hartley guinea pigs. Arthritis Rheum. 2004, 50, 1216-1225.
20. Groop, P. H., Forsblom, C., Thomas, M. C., Mechanisms of disease: Pathway-selective insulin resistance and microvascular complications of diabetes. Nat. Clin. Pract. Endocrinol. Metab. 2005, 1, 100-110.
21. Guingamp, C., Gegout-Pottie, P., Philippe, L., Terlain, B. et al., Mono-iodoacetate-induced experimental osteoarthritis: A dose-response study of loss of mobility, morphology, and biochemistry. Arthritis Rheum. 1997, 40, 1670-1679.
22. Grossin, L., Cournil-Henrionnet, C., Pinzano, A., Gaborit, N. et al., Gene transfer with HSP70 in rat chondrocytes confers cytoprotection in vitro and during experimental osteoarthritis. FASEB J. 2006, 20, 65-75.
23. Terauchi, R., Takahashi, K. A., Arai, Y., Ikeda, T. et al., HSP70 prevents nitric oxide-induced apoptosis in articular chondrocytes. Arthritis Rheum. 2003, 48, 1562-1568.
24. Kim, J. Y., Kim, S. M., Ko, J. H., Yim, J. H. et al., Interaction of pro-apoptotic protein HGTD-P with heat shock protein 90 is required for induction of mitochondrial apoptotic cascades. FEBS Lett. 2006, 580, 3270-3275.
25. López-Armada, M. J., Caramés, B., Lires-Deán, M., Cillero-Pastor, B. et al., Mitochondrial activity is modulated by TNFalpha and IL-1beta in normal human chondrocyte cells. Osteoarthr. Cartil. 2006, 14, 1011-1022.
26. Blanco, F. J., Ochs, R., Schwarta, H., Lotz, M., Chondrocyte apoptosis induced by nitric oxide, Am. J. Pathol. 1995, 146, 75-85.
27. Parente, L., Solito, E., Annexin 1: More than an anti-phospholipase protein. Inflamm. Res. 2004, 53, 125-132.
28. Kim, S.-W., Rhee, H. J., Ko, J., Kim, Y. J. et al., Inhibition of cytosolic phospholipase A2 by annexin I. Specific interaction model and mapping of the interaction site. J. Biol. Chem. 2001, 276, 15712-15719.
29. Sudlow, A. W., Carey, F., Forder, R., Rothwell, N. J., The role of lipocortin-1 in dexamethasone-induced suppression of PGE2 and TNF alpha release from human peripheral blood mononuclear cells. Br. J. Pharmacol. 1996, 117, 1449-1456.
30. de Coupade, C., Ajuebor, M. N., Russo-Marie, F., Perretti, M., Solito, E., Cytokine modulation of liver annexin 1 expression during experimental endotoxemia. Am. J. Pathol. 2001, 159, 1435-1443.
31. Minghetti, L., Nicolini, A., Polazzi, E., Greco, A. et al., Down-regulation of microglial cyclo-oxygenase-2 and inducible nitric oxide synthase expression by lipocortin 1. Br. J. Pharmacol. 1999, 126, 1307-1314.
32. Yang, Y. H., Morand, E. F., Getting, S. J., Paul-Clark, M. et al., Modulation of inflammation and response to dexamethasone by Annexin 1 in antigen-induced arthritis. Arthritis Rheum. 2004, 50, 976-984.
33. Yang, Y., Leech, M., Hutchinson, P., Holdsworth, S. R., Morand, E. F., Antiinflammatory effect of lipocortin 1 in experimental arthritis. Inflammation 1997, 21, 583-596.
34. Sampey, A. V., Hutchinson, P., Morand, E. F., Annexin I and dexamethasone effects on phospholipase and cyclooxygenase activity in human synoviocytes. Mediators Inflamm. 2000, 9, 125-132.
35. Frova, C., Glutathione transferases in the genomics era: New insights and perspectives. Biomol. Eng. 2006, 23, 149-169.
36. Ruiz-Laguna, J., Abril, N., Prieto-Alamo, M. J., Lopez-Barea, J., Pueyo, C., Tissue, species, and environmental differences in absolute quantities of murine mRNAs coding for alpha, mu, omega, pi, and theta glutathione S-transferases. Gene Expr. 2005, 12, 165-176.
37. Li, Y. J., Scott, W. K., Zhang, L., Lin, P. I. et al., Revealing the role of glutathione S-transferase omega in age-at-onset of Alzheimer and Parkinson diseases. Neurobiol. Aging 2006, 27, 1087-1093.
38. Laliberte, R. E., Perregaux, D. G., Hoth, L. R., Rosner, P. J. et al., Glutathione S-transferase omega 1-1 is a target of cytokine release inhibitory drugs and may be responsible for their effect on interleukin-1- posttranslational processing. J. Biol. Chem. 2003, 278, 16567-16578.