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

Berggård, Tord LU ; Arrigoni, Giorgio LU ; Olsson, Olof LU ; Fex, Malin LU ; Linse, Sara LU and James, Peter LU (2006) In Journal of Proteome Research 5(3). p.669-687
Abstract
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
calcium, protein-protein interactions, calmodulin, proteomics, brain
in
Journal of Proteome Research
volume
5
issue
3
pages
669 - 687
publisher
The American Chemical Society (ACS)
external identifiers
  • wos:000235897000024
  • scopus:33644846044
ISSN
1535-3893
DOI
10.1021/pr050421l
language
English
LU publication?
yes
id
caf5ec96-3fe2-4389-832e-e0961f444199 (old id 154846)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=16512683&dopt=Abstract
date added to LUP
2007-07-10 12:31:48
date last changed
2019-10-23 02:32:58
@article{caf5ec96-3fe2-4389-832e-e0961f444199,
  abstract     = {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.},
  author       = {Berggård, Tord and Arrigoni, Giorgio and Olsson, Olof and Fex, Malin and Linse, Sara and James, Peter},
  issn         = {1535-3893},
  keyword      = {calcium,protein-protein interactions,calmodulin,proteomics,brain},
  language     = {eng},
  number       = {3},
  pages        = {669--687},
  publisher    = {The American Chemical Society (ACS)},
  series       = {Journal of Proteome Research},
  title        = {140 mouse brain proteins identified by Ca2+-calmodulin affinity chromatography and tandem mass spectrometry.},
  url          = {http://dx.doi.org/10.1021/pr050421l},
  volume       = {5},
  year         = {2006},
}