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:
https://lup.lub.lu.se/record/154846
- author
- Berggård, Tord
LU
; Arrigoni, Giorgio
LU
; Olsson, Olof
LU
; Fex, Malin
LU
; Linse, Sara
LU
and James, Peter
LU
- organization
- publishing date
- 2006
- 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
- pmid:16512683
- 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
- 2016-04-01 12:28:42
- date last changed
- 2023-10-28 19:01:39
@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}},
keywords = {{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}},
doi = {{10.1021/pr050421l}},
volume = {{5}},
year = {{2006}},
}