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Spatial Metabolomics of the Human Kidney Using MALDI Trapped Ion Mobility Imaging Mass Spectrometry

preprint
revised on 12.05.2020 and posted on 13.05.2020 by Elizabeth Neumann, Lukasz Migas, Jamie L. Allen, Richard Caprioli, Raf Van de Plas, Jeffrey Spraggins

Small metabolites are essential for normal and diseased biological function but are difficult to study because of their inherent structural complexity. MALDI imaging mass spectrometry (IMS) of small metabolites is particularly challenging as MALDI matrix clusters are often isobaric with metabolite ions, requiring high resolving power instrumentation or derivatization to circumvent this issue. An alternative to this is to perform ion mobility separation before ion detection, enabling the visualization of metabolites without the interference of matrix ions. Here, we use MALDI timsTOF IMS to image small metabolites at high spatial resolution within the human kidney. Through this, we have found metabolites, such as arginic acid, acetylcarnitine, and choline that localize to the cortex, medulla, and renal pelvis, respectively. We have also demonstrated that trapped ion mobility spectrometry (TIMS) can resolve matrix peaks from metabolite signal and separate both isobaric and isomeric metabolites with different localizations within the kidney. The added ion mobility data dimension dramatically increased the peak capacity for molecular imaging experiments. Future work will involve further exploring the small metabolite profiles of human kidneys as a function of age, gender, and ethnicity.

Funding

Vanderbilt University Biomolecular Multimodal Imaging Center for 3-Dimensional Tissue Mapping

National Institute of Diabetes and Digestive and Kidney Diseases

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Training Program in Environmental Toxicology

National Institute of Environmental Health Sciences

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Imaging Mass Spectrometry Research Resource at Vanderbilt University

National Institute of General Medical Sciences

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Molecular mapping of microbial communities at the host-pathogen interface by multi-modal 3-dimensional imaging mass spectrometry

National Institute of Allergy and Infectious Diseases

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MRI: Development of a next-generation MALDI ion mobility mass spectrometry platform for molecular imaging and training

Directorate for Engineering

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5 UM1 CA183727-08

History

Email Address of Submitting Author

Elizabeth.neumann@vanderbilt.edu

Institution

Vanderbilt University

Country

United States

ORCID For Submitting Author

0000-0002-6078-3321

Declaration of Conflict of Interest

No Conflict of Interest

Version Notes

Version 0.1

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