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Multiplex enzyme activity imaging by MALDI-IMS of substrate library conversions
Oliver Klein1, Akvile Haeckel2, Ulf Reimer3
1Berlin-Brandenburg Center for Regenerative Therapies, Charité - Universitätsmedizin Berlin, Augustenburger Platz 1, 13353, Berlin, Germany.
Scientific Reports
|September 24, 2020
Summary
This study introduces enzyme activity imaging mass spectrometry (EA-IMS) to map multiple enzyme activities in tissues. This technique allows for the simultaneous analysis of various enzyme functions within biological samples.
Area of Science:
- Biochemistry
- Analytical Chemistry
- Molecular Imaging
Background:
- Enzymes are crucial for biological processes and implicated in various diseases.
- Current methods for studying enzyme activity are often limited in scope or spatial resolution.
Purpose of the Study:
- To develop and demonstrate a novel method for simultaneously mapping multiple enzyme activities in tissue sections.
- To utilize matrix-assisted laser desorption/ionization imaging mass spectrometry (MALDI-IMS) for enzyme activity analysis.
Main Methods:
- Applied a library of 20 peptide substrates for proteases, kinases, and phosphatases to mouse kidney tissue sections.
- Incubated tissues to allow enzyme conversion of substrates.
- Analyzed substrate conversion and product formation using MALDI-IMS.
Main Results:
- Successfully imaged 16 out of 20 applied substrates, showing time-dependent signal intensities.
- Detected 12 masses corresponding to expected enzyme product formation.
- Demonstrated the capability to visualize multiple enzyme activities within the same tissue sample.
Conclusions:
- Enzyme activity imaging mass spectrometry (EA-IMS) is a powerful tool for studying localized enzyme activities and networks.
- This method has potential for investigating enzyme function and pharmaceutical modulation in situ.
- Further optimization is needed to improve substrate detectability and expand the range of detectable enzymes.
