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140 mouse brain proteins identified by Ca2+-calmodulin affinity chromatography and tandem mass spectrometry.

Author:
  • Tord Berggård
  • Giorgio Arrigoni
  • Olof Olsson
  • Malin Fex
  • Sara Linse
  • Peter James
Publishing year: 2006
Language: English
Pages: 669-687
Publication/Series: Journal of Proteome Research
Volume: 5
Issue: 3
Document type: Journal article
Publisher: The American Chemical Society

Abstract english

Calmodulin is an essential Ca2+-binding protein that binds to a variety of targets that carry out critical signaling functions. We describe the proteomic characterization of mouse brain Ca2+-calmodulin-binding proteins that were purified using calmodulin affinity chromatography. Proteins in the eluates from four different affinity chromatography experiments were identified by 1-DE and in-gel digestion followed by LC-MS/MS. Parallel experiments were performed using two related control-proteins belonging to the EF-hand family. After comparing the results from the different experiments, we were able to exclude a significant number of proteins suspected to bind in a nonspecific manner. A total of 140 putative Ca2+-calmodulin-binding proteins were identified of which 87 proteins contained calmodulin-binding motifs. Among the 87 proteins that contained calmodulin-binding motifs, 48 proteins have not previously been shown to interact with calmodulin and 39 proteins were known calmodulin-binding proteins. Many proteins with ill-defined functions were identified as well as a number of proteins that at the time of the analysis were described only as ORFs. This study provides a functional framework for studies on these previously uncharacterized proteins.

Keywords

  • Basic Medicine
  • calcium
  • protein-protein interactions
  • calmodulin
  • proteomics
  • brain

Other

Published
  • Diabetes and Celiac Unit
  • ISSN: 1535-3893
Peter James
E-mail: peter [dot] james [at] immun [dot] lth [dot] se

Professor

Department of Immunotechnology

+46 46 222 14 96

+46 70 247 79 60

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