Imaging mass spectrometry: A new technology for the analysis of protein expression in mammalian tissues

10.1038/86573 ◽  
2001 ◽  
Vol 7 (4) ◽  
pp. 493-496 ◽  
Author(s):  
Markus Stoeckli ◽  
Pierre Chaurand ◽  
Dennis E. Hallahan ◽  
Richard M. Caprioli
Keyword(s):  
Mass Spectrometry ◽  
Protein Expression ◽  
New Technology ◽  
Imaging Mass Spectrometry ◽  
Mammalian Tissues

scholarly journals Three-dimensional visualization of protein expression in mouse brain structures using imaging mass spectrometry

2005 ◽  
Vol 16 (7) ◽  
pp. 1093-1099 ◽  
Author(s):  
Anna C. Crecelius ◽  
D. Shannon Cornett ◽  
Richard M. Caprioli ◽  
Betsy Williams ◽  
Benoit M. Dawant ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Protein Expression ◽  
Mouse Brain ◽  
Imaging Mass Spectrometry ◽  
Three Dimensional ◽  
Brain Structures

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

2020 ◽  
Author(s):  
Elizabeth Neumann ◽  
Lukasz Migas ◽  
Jamie L. Allen ◽  
Richard Caprioli ◽  
Raf Van de Plas ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ion Mobility ◽  
Imaging Mass Spectrometry ◽  
Structural Complexity ◽  
Human Kidney ◽  
Resolving Power ◽  
Mobility Separation ◽  
Trapped Ion ◽  
Mobility Data ◽  
Ion Mobility Separation

<div> <div> <p>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.</p></div></div>

scholarly journals Neurodegenerative Proteinopathies in the Proteoform Spectrum—Tools and Challenges

2021 ◽  
Vol 22 (3) ◽  
pp. 1085
Author(s):  
Aneeqa Noor ◽  
Saima Zafar ◽  
Inga Zerr
Keyword(s):  
Mass Spectrometry ◽  
Neurodegenerative Disorders ◽  
Gel Electrophoresis ◽  
Large Fraction ◽  
Imaging Mass Spectrometry ◽  
Living Tissue ◽  
Disease Prognosis ◽  
Highly Sensitive ◽  
Jakob Disease ◽  
Hydrophobic Nature

Proteinopathy refers to a group of disorders defined by depositions of amyloids within living tissue. Neurodegenerative proteinopathies, including Alzheimer’s disease, Parkinson’s disease, Creutzfeldt–Jakob disease, and others, constitute a large fraction of these disorders. Amyloids are highly insoluble, ordered, stable, beta-sheet rich proteins. The emerging theory about the pathophysiology of neurodegenerative proteinopathies suggests that the primary amyloid-forming proteins, also known as the prion-like proteins, may exist as multiple proteoforms that contribute differentially towards the disease prognosis. It is therefore necessary to resolve these disorders on the level of proteoforms rather than the proteome. The transient and hydrophobic nature of amyloid-forming proteins and the minor post-translational alterations that lead to the formation of proteoforms require the use of highly sensitive and specialized techniques. Several conventional techniques, like gel electrophoresis and conventional mass spectrometry, have been modified to accommodate the proteoform theory and prion-like proteins. Several new ones, like imaging mass spectrometry, have also emerged. This review aims to discuss the proteoform theory of neurodegenerative disorders along with the utility of these proteomic techniques for the study of highly insoluble proteins and their associated proteoforms.

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