Decellularization of intact tissue enables MALDI imaging mass spectrometry analysis of the extracellular matrix

Matrix‐assisted laser desorption/ionization imaging mass spectrometry (MALDI IMS) is a powerful molecular mapping technology that offers unbiased visualization of the spatial arrangement of biomolecules in tissue. Although there has been a significant increase in the number of applications employing...

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Bibliographic Details
Published in:Journal of mass spectrometry. 2015-11, Vol.50 (11), p.1288-1293
Main Authors: Gessel, Megan, Spraggins, Jeffrey M, Voziyan, Paul, Hudson, Billy G, Caprioli, Richard M
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
chromosome mapping
Collagen - chemistry
crosslinking
Desorption
Electrochemical machining
extracellular matrix
Extracellular Matrix - chemistry
Extracellular Matrix Proteins - analysis
Freezing
FTICR
Humans
Hydrolysis
image analysis
Image Processing, Computer-Assisted
Imaging
imaging mass spectrometry
Ionization
Lasers
MALDI
MALDI imaging
Mass spectrometry
Mice
Molecular Sequence Data
Peptide Fragments - analysis
peptides
protein synthesis
Proteins
Rats
sodium dodecyl sulfate
Sodium Dodecyl Sulfate - chemistry
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods
Tandem Mass Spectrometry - methods
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Summary:Matrix‐assisted laser desorption/ionization imaging mass spectrometry (MALDI IMS) is a powerful molecular mapping technology that offers unbiased visualization of the spatial arrangement of biomolecules in tissue. Although there has been a significant increase in the number of applications employing this technology, the extracellular matrix (ECM) has received little attention, likely because ECM proteins are mostly large, insoluble and heavily cross‐linked. We have developed a new sample preparation approach to enable MALDI IMS analysis of ECM proteins in tissue. Prior to freezing and sectioning, intact tissues are decellularized by incubation in sodium dodecyl sulfate. Decellularization removes the highly abundant, soluble species that dominate a MALDI IMS spectrum while preserving the structural integrity of the ECM. In situ tryptic hydrolysis and imaging of tryptic peptides are then carried out to accommodate the large sizes of ECM proteins. This new approach allows the use of MALDI IMS for identification of spatially specific changes in ECM protein expression and modification in tissue. Copyright © 2015 John Wiley & Sons, Ltd.
ISSN:1076-5174
1096-9888
DOI:10.1002/jms.3696