MALDI imaging mass spectrometry to investigate endogenous peptides in an animal model of Usher's disease

Chatterji, Bijon; Dickhut, Clarissa; Mielke, Svenja; Krüger, Jonas; Just, Ingo; Glage, Silke; Meier, Martin; Wedekind, Dirk; Pich, Andreas

doi:10.1002/pmic.201300558

Cited by 16 publications

(10 citation statements)

References 47 publications

(50 reference statements)

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“…MSI also showed a significant increase of endogenous peptides in rats models for Usher's disease, a rare cause of deaf‐blindness. These biomarker candidates were particularly present in the upper colliculi and in the substantia nigra of sick rats . MSI analyses of lenses revealed an increase in sphingomyelin levels, which may have an impact on development of age‐related nuclear cataract .…”

Section: Applications Of Msi In the Understanding Of Pathogenesismentioning

confidence: 99%

MALDI mass spectrometry imaging: A cutting‐edge tool for fundamental and clinical histopathology

Longuespée

Casadonte²,

Kriegsmann

et al. 2016

Proteomics Clinical Apps

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Histopathological diagnoses have been done in the last century based on hematoxylin and eosin staining. These methods were complemented by histochemistry, electron microscopy, immunohistochemistry (IHC), and molecular techniques. Mass spectrometry (MS) methods allow the thorough examination of various biocompounds in extracts and tissue sections. Today, mass spectrometry imaging (MSI), and especially matrix-assisted laser desorption ionization (MALDI) imaging links classical histology and molecular analyses. Direct mapping is a major advantage of the combination of molecular profiling and imaging. MSI can be considered as a cutting edge approach for molecular detection of proteins, peptides, carbohydrates, lipids, and small molecules in tissues. This review covers the detection of various biomolecules in histopathological sections by MSI. Proteomic methods will be introduced into clinical histopathology within the next few years.

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Section: Applications Of Msi In the Understanding Of Pathogenesismentioning

confidence: 99%

MALDI mass spectrometry imaging: A cutting‐edge tool for fundamental and clinical histopathology

Longuespée

Casadonte²,

Kriegsmann

et al. 2016

Proteomics Clinical Apps

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“…The idea that proSAAS plays a role in neurodegenerative proteostasis is further supported by human transcriptomics studies, which indicate increased proSAAS expression during AD progression ( Mathys et al, 2019 ). Increased levels of proSAAS have also been found in brain tissues of patients with CAA ( Inoue et al, 2017 ), as well as in models of neurodegenerative diseases including horses ( McGorum et al, 2016 ) and rats ( Chatterji et al, 2014 ). Lastly, recent data from our laboratory indicate that cellular proSAAS levels are upregulated following ER and even heat stress ( Shakya et al, 2020 ); interestingly, in parallel experiments, similar upregulation was not observed for 7B2.…”

Section: B2 and Prosaasmentioning

confidence: 99%

Secreted Chaperones in Neurodegeneration

Chaplot

Jarvela

Lindberg

2020

Front. Aging Neurosci.

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Protein homeostasis, or proteostasis, is a combination of cellular processes that govern protein quality control, namely, protein translation, folding, processing, and degradation. Disruptions in these processes can lead to protein misfolding and aggregation. Proteostatic disruption can lead to cellular changes such as endoplasmic reticulum or oxidative stress; organelle dysfunction; and, if continued, to cell death. A majority of neurodegenerative diseases involve the pathologic aggregation of proteins that subverts normal neuronal function. While prior reviews of neuronal proteostasis in neurodegenerative processes have focused on cytoplasmic chaperones, there is increasing evidence that chaperones secreted both by neurons and other brain cells in the extracellular – including transsynaptic – space play important roles in neuronal proteostasis. In this review, we will introduce various secreted chaperones involved in neurodegeneration. We begin with clusterin and discuss its identification in various protein aggregates, and the use of increased cerebrospinal fluid (CSF) clusterin as a potential biomarker and as a potential therapeutic. Our next secreted chaperone is progranulin; polymorphisms in this gene represent a known genetic risk factor for frontotemporal lobar degeneration, and progranulin overexpression has been found to be effective in reducing Alzheimer’s- and Parkinson’s-like neurodegenerative phenotypes in mouse models. We move on to BRICHOS domain-containing proteins, a family of proteins containing highly potent anti-amyloidogenic activity; we summarize studies describing the biochemical mechanisms by which recombinant BRICHOS protein might serve as a therapeutic agent. The next section of the review is devoted to the secreted chaperones 7B2 and proSAAS, small neuronal proteins which are packaged together with neuropeptides and released during synaptic activity. Since proteins can be secreted by both classical secretory and non-classical mechanisms, we also review the small heat shock proteins (sHsps) that can be secreted from the cytoplasm to the extracellular environment and provide evidence for their involvement in extracellular proteostasis and neuroprotection. Our goal in this review focusing on extracellular chaperones in neurodegenerative disease is to summarize the most recent literature relating to neurodegeneration for each secreted chaperone; to identify any common mechanisms; and to point out areas of similarity as well as differences between the secreted chaperones identified to date.

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“…MSI was also used in peptidomics, for example, determining the distribution of endogenous peptides in brain tissues (Chatterji et al, ; Chatterji & Pich, ). In the study of a rat model of Usher's disease, a rare disease considered to be a leading cause of deaf‐blindness in humans worldwide, cryosections of brain tissue were analyzed to differentiate between healthy and diseased rats (Chatterji et al, ). Three factors were found to be important for the success of peptide quantitation.…”

Section: Msi‐based Proteomicsmentioning

confidence: 99%

Recent advances in mass spectrometry imaging for multiomics application in neurology

Gao

2018

J of Comparative Neurology

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Mass spectrometry imaging (MSI) has emerged as a powerful tool for multiomics study in neurology. MSI combines the multichannel (m/z) measurement capability of mass spectrometers with a surface sampling process that allows for rapid probing and mapping of the characterized intact proteins, proteolytic digested peptides, released glycans, phospholipids, glycolipids, and small metabolites in brain tissues. The present review is focused on the application of MSI to the study of proteomics, glycomics, peptidomics, metabolomics, and lipidomics in mouse brain tissues. K E Y W O R D Smass spectrometry imaging, mouse brain,

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MALDI imaging mass spectrometry to investigate endogenous peptides in an animal model of Usher's disease

Cited by 16 publications

References 47 publications

MALDI mass spectrometry imaging: A cutting‐edge tool for fundamental and clinical histopathology

MALDI mass spectrometry imaging: A cutting‐edge tool for fundamental and clinical histopathology

Secreted Chaperones in Neurodegeneration

Recent advances in mass spectrometry imaging for multiomics application in neurology

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