Influence of various on‐tissue washing procedures on the entire protein quantity and the quality of matrix‐assisted laser desorption/ionization spectra

Enthaler, Bernd; Bussmann, T.; Pruns, Julia K.; Rapp, Claudius; Fischer, Markus; Vietzke, Jens-Peter

doi:10.1002/rcm.6513

Cited by 18 publications

(18 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In order to develop a method for IMS analysis of LNA‐A in tissue sections by MALDI‐MS, pretreatment methods specific for tissue sections need to be established. For IMS analysis of proteins, salts and lipids need to be removed prior to analysis by washing tissue sections on glass slides . In IMS analyses of proteins, washing steps are generally performed with pure water; however, because nucleic acids are water soluble, this could result in loss of distribution information, and therefore different washing protocols are required.…”

Section: Resultsmentioning

confidence: 99%

“…For IMS analysis of proteins, salts and lipids need to be removed prior to analysis by washing tissue sections on glass slides . In IMS analyses of proteins, washing steps are generally performed with pure water; however, because nucleic acids are water soluble, this could result in loss of distribution information, and therefore different washing protocols are required. In this study, we evaluated several washing conditions for tissue sections on glass slides (Table ).…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Development of a detection method for antisense oligonucleotides in mouse kidneys by matrix‐assisted laser desorption/ionization imaging mass spectrometry

Yokoi

Kasahara

Obika

et al. 2018

Rapid Comm Mass Spectrometry

View full text Add to dashboard Cite

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Development of a detection method for antisense oligonucleotides in mouse kidneys by matrix‐assisted laser desorption/ionization imaging mass spectrometry

Yokoi

Kasahara

Obika

et al. 2018

Rapid Comm Mass Spectrometry

View full text Add to dashboard Cite

show abstract

“…Middle‐panel shows control with displayed PEG signal present compared to on‐tissue digests after PEG removal with described aqueous washing protocols. Reprinted with permission from Enthaler et al (), copyright year 2013 (John Wiley & Sons, Ltd.). EtOH, ethanol; PEG, polyethylene glycol; TFA, trifluoroacetic acid…”

Section: Methods To Preserve and Store Tissuesmentioning

confidence: 99%

Proteome analysis of tissues by mass spectrometry

Đapić

Baljeu‐Neuman

Uwugiaren

et al. 2019

Mass Spectrometry Reviews

View full text Add to dashboard Cite

Tissues and biofluids are important sources of information used for the detection of diseases and decisions on patient therapies. There are several accepted methods for preservation of tissues, among which the most popular are fresh‐frozen and formalin‐fixed paraffin embedded methods. Depending on the preservation method and the amount of sample available, various specific protocols are available for tissue processing for subsequent proteomic analysis. Protocols are tailored to answer various biological questions, and as such vary in lysis and digestion conditions, as well as duration. The existence of diverse tissue‐sample protocols has led to confusion in how to choose the best protocol for a given tissue and made it difficult to compare results across sample types. Here, we summarize procedures used for tissue processing for subsequent bottom‐up proteomic analysis. Furthermore, we compare protocols for their variations in the composition of lysis buffers, digestion procedures, and purification steps. For example, reports have shown that lysis buffer composition plays an important role in the profile of extracted proteins: the most common are tris(hydroxymethyl)aminomethane, radioimmunoprecipitation assay, and ammonium bicarbonate buffers. Although, trypsin is the most commonly used enzyme for proteolysis, in some protocols it is supplemented with Lys‐C and/or chymotrypsin, which will often lead to an increase in proteome coverage. Data show that the selection of the lysis procedure might need to be tissue‐specific to produce distinct protocols for individual tissue types. Finally, selection of the procedures is also influenced by the amount of sample available, which range from biopsies or the size of a few dozen of mm2 obtained with laser capture microdissection to much larger amounts that weight several milligrams.

show abstract

“…The typical washing procedure is performed with a gradient of ethanol reagents. Finally, the sections are dried in a vacuum desiccator for 15 min [60]. For the detection of digested peptides, treatment with protease is also performed [61].…”

Section: Sample Pretreatment (Washing Digestion)mentioning

confidence: 99%

Application of Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry Imaging for Food Analysis

Morisasa

Satō

Kimura

et al. 2019

Foods

View full text Add to dashboard Cite

Food contains various compounds, and there are many methods available to analyze each of these components. However, the large amounts of low-molecular-weight metabolites in food, such as amino acids, organic acids, vitamins, lipids, and toxins, make it difficult to analyze the spatial distribution of these molecules. Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) imaging is a two-dimensional ionization technology that allows the detection of small metabolites in tissue sections without requiring purification, extraction, separation, or labeling. The application of MALDI-MS imaging in food analysis improves the visualization of these compounds to identify not only the nutritional content but also the geographical origin of the food. In this review, we provide an overview of some recent applications of MALDI-MS imaging, demonstrating the advantages and prospects of this technology compared to conventional approaches. Further development and enhancement of MALDI-MS imaging is expected to offer great benefits to consumers, researchers, and food producers with respect to breeding improvement, traceability, the development of value-added foods, and improved safety assessments.

show abstract

Influence of various on‐tissue washing procedures on the entire protein quantity and the quality of matrix‐assisted laser desorption/ionization spectra

Abstract: Washing steps have a strong impact on improving the spectral quality, but they may lead to a high decrease in the protein content. Our results show that there is a balancing act between avoiding protein loss and obtaining high spectra quality.

Cited by 18 publications

References 22 publications

Development of a detection method for antisense oligonucleotides in mouse kidneys by matrix‐assisted laser desorption/ionization imaging mass spectrometry

Development of a detection method for antisense oligonucleotides in mouse kidneys by matrix‐assisted laser desorption/ionization imaging mass spectrometry

Proteome analysis of tissues by mass spectrometry

Application of Matrix-Assisted Laser Desorption/Ionization Mass Spectrometry Imaging for Food Analysis

Contact Info

Product

Resources

About