Reduction of caldesmon expression induces apoptosis and causes disassembly of the sarcomeric protein complex in cardiomyocytes in vivo

Zheng, Peng; Severijnen, Lies‐Anne; Willemsen, Rob; Kros, Johan M.

doi:10.4161/cc.8.2.7344

Cited by 2 publications

(2 citation statements)

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“…A straightforward, conceptually simple semiquantitative way of evaluating IPTL data is provided using Mascot score ratio values. Finally, we show that IPTL can be used for the quantification of complex proteomic changes by providing data replicating the well-documented changes of apoptotic cells upon incubation with STLC or other inducers of apoptosis. − …”

Section: Discussionmentioning

confidence: 58%

Isobaric Peptide Termini Labeling for MS/MS-Based Quantitative Proteomics

et al. 2009

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Since its introduction, isobaric peptide labeling has played an important role in relative quantitative comparisons of proteomes. This paper describes isobaric peptide termini labeling (IPTL), a novel approach for the identification and quantification of two differentially labeled states using MS/MS spectra. After endoproteinase Lys-C digestion, peptides were labeled at C-terminal lysine residues with either 2-methoxy-4,5-dihydro-1H-imidazole (MDHI) or with tetradeuterated MDHI-d(4). Subsequently, their N-termini were derivatized either with tetradeuterated succinic anhydride (SA-d(4)) or with SA. The mixed isotopic labeling results in isobaric masses and provided several quantification data points per peptide. The suitability of this approach is demonstrated with MS and MS/MS analyses of Lys-C digests of standard proteins. A conceptually simple quantification strategy with a dynamic range of 25 is achieved through the use of Mascot score ratios. The utility of IPTL for the analysis of proteomes was verified by comparing the well-characterized effect of the antimitotic inhibitor S-Trityl-l-Cysteine (STLC) on HeLa cells that were treated for either 24 or 48 h with the inhibitor. Many apoptosis-linked proteins were identified as being differentially regulated, confirming the suitability of IPTL for the analysis of complex proteomes.

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