Proteomic identification of cellular protease substrates using isobaric tags for relative and absolute quantification (iTRAQ).

Identification of protease substrates is essential to identify and understand the functional consequences of normal and dysregulated proteolysis in disease on the proteome. Isobaric tags for relative and absolute quantification (iTRAQ) can be used to identify novel protease substrates in the cellular context. An amine-targeted iTRAQ tag labels tryptic peptides generated from the proteins and protease cleavage products of secreted proteins, as well as protein domains shed from the cell membrane or pericellular matrix of protease-transfected cells that have accumulated in conditioned medium; a second iTRAQ tag is used for control cells. MS/MS fragmentation enables sequencing of the pooled pairs of differently labeled but identical peptides and generates a low mass signature ion peak unique for each label. This signature ion peak identifies the peptides originating from the protease-transfected or control cells; comparison of the peak areas enables relative quantitation of the peptide between the samples.

Dean RA ，Smith D ，Overall CM 《-》

Identification of cellular MMP substrates using quantitative proteomics: isotope-coded affinity tags (ICAT) and isobaric tags for relative and absolute quantification (iTRAQ).

Butler GS ，Dean RA ，Morrison CJ ，Overall CM ... -  《-》

Proteomics discovery of metalloproteinase substrates in the cellular context by iTRAQ labeling reveals a diverse MMP-2 substrate degradome.

Dean RA ，Overall CM 《MOLECULAR & CELLULAR PROTEOMICS》

From relative to absolute quantification of tryptic peptides with tandem mass tags: application to cerebrospinal fluid.

Dayon L ，Turck N ，Scherl A ，Hochstrasser DF ，Burkhard PR ，Sanchez JC ... -  《CHIMIA》

Multiplex N-terminome analysis of MMP-2 and MMP-9 substrate degradomes by iTRAQ-TAILS quantitative proteomics.

Prudova A ，auf dem Keller U ，Butler GS ，Overall CM ... -  《-》