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

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140 mouse brain proteins identified by Ca2+-calmodulin affinity chromatography and tandem mass spectrometry. / Berggård, Tord; Arrigoni, Giorgio; Olsson, Olof; Fex, Malin; Linse, Sara; James, Peter.

I: Journal of Proteome Research, Vol. 5, Nr. 3, 2006, s. 669-687.

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T1 - 140 mouse brain proteins identified by Ca2+-calmodulin affinity chromatography and tandem mass spectrometry.

AU - Berggård, Tord

AU - Arrigoni, Giorgio

AU - Olsson, Olof

AU - Fex, Malin

AU - Linse, Sara

AU - James, Peter

PY - 2006

Y1 - 2006

N2 - 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.

AB - 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.

KW - calcium

KW - protein-protein interactions

KW - calmodulin

KW - proteomics

KW - brain

U2 - 10.1021/pr050421l

DO - 10.1021/pr050421l

M3 - Article

VL - 5

SP - 669

EP - 687

JO - Journal of Proteome Research

T2 - Journal of Proteome Research

JF - Journal of Proteome Research

SN - 1535-3893

IS - 3

ER -