Researchers Analyze Microbial Cells via Imaging Mass Spectrometry

2010 ◽  
Vol 5 (12) ◽  
pp. 508-509
Author(s):  
Carol Potera
Keyword(s):  
Mass Spectrometry ◽  
Imaging Mass Spectrometry ◽  
Microbial Cells

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.

scholarly journals Imaging Mass Spectrometry-Based Proteomic Analysis to Differentiate Melanocytic Nevi and Malignant Melanoma

Cancers ◽  
2021 ◽  
Vol 13 (13) ◽  
pp. 3197
Author(s):  
Rita Casadonte ◽  
Mark Kriegsmann ◽  
Katharina Kriegsmann ◽  
Isabella Hauk ◽  
Rolf R. Meliß ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Malignant Melanoma ◽  
Operating Characteristic ◽  
Characteristic Curve ◽  
Imaging Mass Spectrometry ◽  
Independent Set ◽  
Molecular Techniques ◽  
Charge Ratio ◽  
Linear Discriminant ◽  
Melanocytic Nevi

The discrimination of malignant melanoma from benign nevi may be difficult in some cases. For this reason, immunohistological and molecular techniques are included in the differential diagnostic toolbox for these lesions. These methods are time consuming when applied subsequently and, in some cases, no definitive diagnosis can be made. We studied both lesions by imaging mass spectrometry (IMS) in a large cohort (n = 203) to determine a different proteomic profile between cutaneous melanomas and melanocytic nevi. Sample preparation and instrument setting were tested to obtain optimal results in term of data quality and reproducibility. A proteomic signature was found by linear discriminant analysis to discern malignant melanoma from benign nevus (n = 113) with an overall accuracy of >98%. The prediction model was tested in an independent set (n = 90) reaching an overall accuracy of 93% in classifying melanoma from nevi. Statistical analysis of the IMS data revealed mass-to-charge ratio (m/z) peaks which varied significantly (Area under the receiver operating characteristic curve > 0.7) between the two tissue types. To our knowledge, this is the largest IMS study of cutaneous melanoma and nevi performed up to now. Our findings clearly show that discrimination of melanocytic nevi from melanoma is possible by IMS.

MALDI imaging mass spectrometry: an emerging tool in neurology

2021 ◽  
Author(s):  
Laura K. Schnackenberg ◽  
David A. Thorn ◽  
Dustyn Barnette ◽  
E. Ellen Jones
Keyword(s):  
Mass Spectrometry ◽  
Imaging Mass Spectrometry ◽  
Maldi Imaging ◽  
Maldi Imaging Mass Spectrometry

scholarly journals Imaging Mass Spectrometry for Assessing Cutaneous Wound Healing: Analysis of Pressure Ulcers

2014 ◽  
Vol 14 (2) ◽  
pp. 986-996 ◽  
Author(s):  
Domenico Taverna ◽  
Alonda C. Pollins ◽  
Giovanni Sindona ◽  
Richard M. Caprioli ◽  
Lillian B. Nanney
Keyword(s):  
Mass Spectrometry ◽  
Wound Healing ◽  
Pressure Ulcers ◽  
Imaging Mass Spectrometry ◽  
Cutaneous Wound Healing ◽  
Cutaneous Wound

scholarly journals Quantitative imaging mass spectrometry of renal sulfatides: validation by classical mass spectrometric methods

2014 ◽  
Vol 55 (11) ◽  
pp. 2343-2353 ◽  
Author(s):  
Christian Marsching ◽  
Richard Jennemann ◽  
Raphael Heilig ◽  
Hermann-Josef Gröne ◽  
Carsten Hopf ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Quantitative Imaging ◽  
Imaging Mass Spectrometry ◽  
Mass Spectrometric

scholarly journals Imaging mass spectrometry of frontal white matter lipid changes in human alcoholics

Alcohol ◽  
2018 ◽  
Vol 67 ◽  
pp. 51-63 ◽  
Author(s):  
Suzanne M. de la Monte ◽  
Jared Kay ◽  
Emine B. Yalcin ◽  
Jillian J. Kril ◽  
Donna Sheedy ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
White Matter ◽  
Imaging Mass Spectrometry ◽  
Frontal White Matter
Sign in / Sign up

Export Citation Format

Share Document