Two-dimensional gel proteome reference map of INS-1E cells

Proteomics

Volumn 11, Issue 7, 2011, Pages 1365-1369

  D'Hertog, Wannes ^a   Maris, Michael ^a   Thorrez, Lieven ^a   Waelkens, Etienne ^b   Overbergh, Lut ^a   Mathieu, Chantal ^a  

^a UNIVERSITY OF LEUVEN   (Belgium)

^b UNIVERSITY HOSPITALS LEUVEN   (Belgium)

Author keywords

Animal proteomics; Diabetes; INS 1E; Proteome reference map

Indexed keywords

INSULIN; PROTEOME;

ANIMAL CELL; ARTICLE; CELL FUNCTION; CELL LINE; CELLULAR DISTRIBUTION; DIABETOGENESIS; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; NUCLEOTIDE SEQUENCE; PANCREAS ISLET BETA CELL; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEOMICS; RAT;

ANIMALS; CELL LINE, TUMOR; DATABASES, PROTEIN; DIABETES MELLITUS; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; GENE EXPRESSION; INSULIN-SECRETING CELLS; INSULINOMA; PANCREATIC NEOPLASMS; PROTEINS; PROTEOME; PROTEOMICS; RATS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

ANIMALIA; RATTUS;

EID: 79953066409     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201000006     Document Type: Article

References (27)

1. Wild, S., Roglic, G., Green, A., Sicree, R. et al., Global prevalence of diabetes: estimates for the year 2000 and projections for 2030. Diabetes Care 2004, 27, 1047-1053.
2. Asfari, M., Janjic, D., Meda, P., Li, G. et al., Establishment of 2-mercaptoethanol-dependent differentiated insulin-secreting cell lines. Endocrinology 1992, 130, 167-178.
3. D'Hertog, W., Overbergh, L., Lage, K., Ferreira, G. B. et al., Proteomics analysis of cytokine-induced dysfunction and death in insulin-producing INS-1E cells: new insights into the pathways involved. Mol. Cell. Proteomics 2007, 6, 2180-2199.
4. Larsen, P. M., Fey, S. J., Larsen, M. R., Nawrocki, A. et al., Proteome analysis of interleukin-1beta-induced changes in protein expression in rat islets of Langerhans. Diabetes 2001, 50, 1056-1063.
5. Sparre, T., Christensen, U. B., Gotfredsen, C. F., Larsen, P. M. et al., Changes in expression of IL-1 beta influenced proteins in transplanted islets during development of diabetes in diabetes-prone BB rats. Diabetologia 2004, 47, 892-908.
6. Sol, E. R., Hovsepyan, M., Bergsten, P., Proteins altered by elevated levels of palmitate or glucose implicated in impaired glucose-stimulated insulin secretion. Proteome Sci. 2009, 7, 24.
7. Hovsepyan, M., Sargsyan, E., Bergsten, P., Palmitate-induced changes in protein expression of insulin secreting INS-1E cells. J. Proteomics 2010, 73, 1148-1155.
8. Cui, Z., Hou, J., Chen, X., Li, J. et al., The profile of Mitochondrial Proteins and their phosphorylation signaling network in INS-1 beta cell. J. Proteome Res. 2010, 9, 2898-2908.
9. Ashburner, M., Ball, C. A., Blake, J. A., Botstein, D. et al., Gene ontology: tool for the unification of biology. The Gene Ontology Consortium. Nat. Genet. 2000, 25, 25-29.
10. Bhatia, V. N., Perlman, D. H., Costello, C. E., McComb, M. E., Software tool for researching annotations of proteins: open-source protein annotation software with data visualization. Anal. Chem. 2009, 81, 9819-9823.
11. Zahedi, R. P., Meisinger, C., Sickmann, A., Two-dimensional benzyldimethyl-n-hexadecylammonium chloride/SDS-PAGE for membrane proteomics. Proteomics 2005, 5, 3581-3588.
12. Gartner, W., Vila, G., Daneva, T., Nabokikh, A. et al., New functional aspects of the neuroendocrine marker secretagogin based on the characterization of its rat homolog. Am. J. Physiol. Endocrinol. Metab. 2007, 293, E347-E354.
13. Portela-Gomes, G. M., Gayen, J. R., Grimelius, L., Stridsberg, M. et al., The importance of chromogranin A in the development and function of endocrine pancreas. Regul. Pept. 2008, 151, 19-25.
14. Helle, K. B., Corti, A., Metz-Boutigue, M. H., Tota, B., The endocrine role for chromogranin A: a prohormone for peptides with regulatory properties. Cell Mol. Life Sci. 2007, 64, 2863-2886.
15. Gayen, J. R., Saberi, M., Schenk, S., Biswas, N. et al., A novel pathway of insulin sensitivity in chromogranin a null mice: A crucial role for pancreastatin in glucose homeostasis. J. Biol. Chem. 2009, 284, 28498-28509.
16. Kim, T., Tao-Cheng, J. H., Eiden, L. E., Loh, Y. P., Chromogranin A, an "on/off" switch controlling dense-core secretory granule biogenesis. Cell 2001, 106, 499-509.
17. Huh, Y. H., Jeon, S. H., Yoo, S. H., Chromogranin B-induced secretory granule biogenesis: comparison with the similar role of chromogranin A. J. Biol. Chem. 2003, 278, 40581-40589.
18. Hickey, A. J., Bradley, J. W., Skea, G. L., Middleditch, M. J. et al., Proteins associated with immunopurified granules from a model pancreatic islet beta-cell system: proteomic snapshot of an endocrine secretory granule. J. Proteome Res. 2009, 8, 178-186.
19. Seidel, B., Dong, W., Savaria, D., Zheng, M. et al., Neuroendocrine protein 7B2 is essential for proteolytic conversion and activation of proprotein convertase 2 in vivo. DNA Cell Biol. 1998, 17, 1017-1029.
20. Davidson, H. W., (Pro)Insulin processing: a historical perspective. Cell Biochem. Biophys. 2004, 40, 143-158.
21. Helle, K. B., The granin family of uniquely acidic proteins of the diffuse neuroendocrine system: comparative and functional aspects. Biol. Rev. Camb. Philos. Soc. 2004, 79, 769-794.
22. Eizirik, D. L., Cardozo, A. K., Cnop, M., The role for endoplasmic reticulum stress in diabetes mellitus. Endocr. Rev. 2008, 29, 42-61.
23. Hartley, T., Brumell, J., Volchuk, A., Emerging roles for the ubiquitin-proteasome system and autophagy in pancreatic beta-cells. Am. J. Physiol, Endocrinol. Metab. 2009, 296, E1-E10.
24. Haas, A. L., Warms, J. V., Hershko, A., Rose, I. A., Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation. J. Biol. Chem. 1982, 257, 2543-2548.
25. Dai, R. M., Li, C. C., Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation. Nat. Cell Biol. 2001, 3, 740-744.
26. Kleizen, B., Braakman, I., Protein folding and quality control in the endoplasmic reticulum. Curr. Opin. Cell Biol. 2004, 16, 343-349.
27. Zaiss, D. M., Standera, S., Holzhutter, H., Kloetzel, P. et al., The proteasome inhibitor PI31 competes with PA28 for binding to 20S proteasomes. FEBS Lett. 1999, 457, 333-338.