Premium
Proteomics of C a CO 3 biomineral‐associated proteins: H ow to properly address their analysis
Author(s) -
Marie Benjamin,
RamosSilva Paula,
Marin Frédéric,
Marie Arul
Publication year - 2013
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201300162
Subject(s) - biomineralization , proteomics , computational biology , nanotechnology , biochemical engineering , biology , chemistry , data science , computer science , bioinformatics , materials science , engineering , biochemistry , astrobiology , gene
In a recent editorial ( Proc. Natl. Acad. Sci ., 2013 110 , E2144–E2146) and elsewhere, questions have been raised regarding the experimental practices in relation to the proteomic analysis of organic matrices associated to the biomineralized C a CO 3 skeletons of metazoans such as molluscan shells and coral skeletons. Indeed, although the use of new high sensitivity MS technology potentially allows to identify a greater number of proteins, it is also equally (or even more) sensitive to contamination of residual proteins from soft tissues, which are in close contact with the biomineral. Based on our own past and present experimental know‐how—observations that are reproducible and coherent with the current understanding of extracellular biomineralization processes—we are convinced that a careful and appropriate cleaning of biominerals prior to any analysis is crucial for accurate proteomic investigations and subsequent pertinent interpretation of the results. Our goal is to alert the scientific community about the associated bias that definitely should be avoided, and to provide critical recommendations on sample preparation and experimental design, in order to better take advantage of the aptness of proteomic approaches aiming at improving our understanding of the molecular mechanisms in biomineralization.