Jusal Quanico1, Julien Franck1, Maxence Wisztorski1, Michel Salzet1, and Isabelle Fournier1
- Université de Lille 1, INSERM, U1192—Laboratoire Protéomique, Réponse Inflammatoire et Spectrométrie de Masse (PRISM), Lille, France
Mapping provides a direct means to assess the impact of protein biomarkers and puts into context their relevance in the type of cancer being examined. To this end, mass spectrometry imaging (MSI) was developed to provide the needed spatial information which is missing in traditional liquid-based mass spectrometric proteomics approaches. Aptly described as a “molecular histology” technique, MSI gives an additional dimension in characterizing tumor biopsies, allowing for mapping of hundreds of molecules in a single analysis. A decade of developments focused on improving and standardizing MSI so that the technique can be translated into the clinical setting. This review describes the progress made in addressing the technological development that allows to bridge local protein detection by MSI to its identification and to illustrate its potential in studying various aspects of cancer biomarker discovery.
CovalX Technology Used (Click each option to learn more)
Detection systems such as the CovalX HM1 can be used by researchers to determine masses up to 110 kDa in mass spectrometry imaging applications. This mass spectrometer modification allows for protein detection at higher masses through the use of a dynode array that creates secondary ions from the high-mass ions and then reaccelerates to a secondary electron multiplier, allowing for sufficient velocities to be reached that can improve the sensitivity.