HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Supplemental Data All Versions of this Article: M600443-MCP200v1 M600443-MCP200v2 6/6/1007    most recent Submit a response Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Glossary Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Brunner, Y. Articles by Sanchez, J.-C. Search for Related Content PubMed PubMed Citation Articles by Brunner, Y. Articles by Sanchez, J.-C. Social Bookmarking                      What's this?

Molecular & Cellular Proteomics 6:1007-1017, 2007.
© 2007 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Research

Proteomics Analysis of Insulin Secretory Granules^*,S

Yannick Brunner, Yohann Couté, Mariella Iezzi, Michelangelo Foti, Mitsonuri Fukuda^¶, Denis F. Hochstrasser^,||, Claes B. Wollheim and Jean-Charles Sanchez^,**

From the Biomedical Proteomics Research Group and Department of Cell Physiology and Metabolism, University Medical Center, 1211 Geneva 4, Switzerland, ^¶ Department of Developmental Biology and Neurosciences, Tohoku University, Sendai 980-8578 Japan, and ^|| Central Clinical Chemistry Laboratory, Geneva University Hospital, 1211 Geneva 14, Switzerland

Insulin secretory granules (ISGs) are cytoplasmic organelles of pancreatic ß-cells. They are responsible for the storage and secretion of insulin. To date, only about 30 different proteins have been clearly described to be associated with these organelles. However, data from two-dimensional gel electrophoresis analyses suggested that almost 150 different polypeptides might be present within ISGs. The elucidation of the identity and function of the ISG proteins by proteomics strategies would be of considerable help to further understand some of the underlying mechanisms implicated in ISG biogenesis and trafficking. Furthermore it should give the bases to the comprehension of impaired insulin secretion observed during diabetes. A proteomics analysis of an enriched insulin granule fraction from the rat insulin-secreting cell line INS-1E was performed. The efficacy of the fractionation procedure was assessed by Western blot and electron microscopy. Proteins of the ISG fraction were separated by SDS-PAGE, excised from consecutive gel slices, and tryptically digested. Peptides were analyzed by nano-LC-ESI-MS/MS. This strategy identified 130 different proteins that were classified into four structural groups including intravesicular proteins, membrane proteins, novel proteins, and other proteins. Confocal microscopy analysis demonstrated the association of Rab37 and VAMP8 with ISGs in INS-1E cells. In conclusion, the present study identified 130 proteins from which 110 are new proteins associated with ISGs. The elucidation of their role will further help in the understanding of the mechanisms governing impaired insulin secretion during diabetes.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				F. Xia, L. Xie, A. Mihic, X. Gao, Y. Chen, H. Y. Gaisano, and R. G. Tsushima Inhibition of Cholesterol Biosynthesis Impairs Insulin Secretion and Voltage-Gated Calcium Channel Function in Pancreatic {beta}-Cells Endocrinology, October 1, 2008; 149(10): 5136 - 5145. [Abstract] [Full Text] [PDF]

				S. L. Schwartz, C. Cao, O. Pylypenko, A. Rak, and A. Wandinger-Ness Rab GTPases at a glance J. Cell Sci., November 15, 2007; 120(22): 3905 - 3910. [Full Text] [PDF]