Quantitative Imaging of Proteins in Tissue by Stable Isotope Labeled Mimetic Liquid Extraction Surface Analysis Mass Spectrometry

Havlíková, Jana; Randall, Elizabeth C.; Griffiths, Rhonda; Swales, John G.; Goodwin, Richard J. A.; Bunch, Josephine; Styles, Iain B.; Cooper, Helen J.

doi:10.1021/acs.analchem.9b04148

Cited by 23 publications

(21 citation statements)

References 17 publications

(40 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The mimetic tissue model is discussed in further detail in the MALDI imaging section. In one instance, the concentration of ubiquitin in brain tissue was determined using a mimetic tissue model [31]. While results agreed with values found in the literature, the > 50% standard deviation across the sample and estimations in the concentration calculation (e.g., weight of rat and mouse brain) inspires low confidence in the absolute concentrations reported.…”

Section: Tissue Profilingsupporting

confidence: 76%

Spatially resolved absolute quantitation in thin tissue by mass spectrometry

Kertész

Cahill

2020

Anal Bioanal Chem

View full text Add to dashboard Cite

Mass spectrometry (MS) has become the de facto tool for routine quantitative analysis of biomolecules. MS is increasingly being used to reveal the spatial distribution of proteins, metabolites, and pharmaceuticals in tissue and interest in this area has led to a number of novel spatially resolved MS technologies. Most spatially resolved MS measurements are qualitative in nature due to a myriad of potential biases, such as sample heterogeneity, sampling artifacts, and ionization effects. As applications of spatially resolved MS in the pharmacological and clinical fields increase, demand has become high for quantitative MS imaging and profiling data. As a result, several varied technologies now exist that provide differing levels of spatial and quantitative information. This review provides an overview of MS profiling and imaging technologies that have demonstrated quantitative analysis from tissue. Focus is given on the fundamental processes affecting quantitative analysis in an array of MS imaging and profiling technologies and methods to address these biases.

show abstract

Section: Tissue Profilingsupporting

confidence: 76%

Spatially resolved absolute quantitation in thin tissue by mass spectrometry

Kertész

Cahill

2020

Anal Bioanal Chem

View full text Add to dashboard Cite

show abstract

“…For qMSI analysis of intact proteins in tissue, Havlikova et al (2019) constructed a stable isotope labeled mimetic tissue model for the absolute quantification of ubiquitin by spiking C 13 , N 15 ‐labeled ubiquitin into rat and mouse brain sections. Ubiquitin is the low‐molecular weight protein involved in a number of biological processes, such as cell cycle, metabolic regulation, protein degradation and DNA reparation (Kaiser et al, 2011).…”

Section: Quantitative Analysismentioning

confidence: 99%

Three‐dimensional quantitative mass spectrometry imaging in complex system: From subcellular to whole organism

Zhao

Cai

2020

Mass Spectrometry Reviews

View full text Add to dashboard Cite

Mass spectrometry imaging (MSI) has been applied for label-free threedimensional (3D) imaging from position array across the whole organism, which provides high-dimensional quantitative data of inorganic or organic compounds that may play an important role in the regulation of cellular signaling, including metals, metabolites, lipids, drugs, peptides, and proteins.While MSI is suitable for investigation of the spatial distribution of molecules, it has a limitation with visualization and quantification of multiple molecules. 3D-MSI, however, can be applied toward exploring metabolic pathway as well as the interactions of lipid-protein, protein-protein, and metal-protein in complex systems from subcellular to the whole organism through an untargeted methodology. In this review, we highlight the methods and applications of MS-based 3D imaging to address the complexity of molecular interaction from nano-to micrometer lateral resolution, with particular focus on: (a) common and hybrid 3D-MSI techniques; (b) quantitative MSI methodology, including the methods using a stable isotope labeling internal standard (SILIS) and SILIS-free approaches with tissue extinction coefficient or virtual calibration; (c) reconstruction of the 3D organ; (d) application of 3D-MSI for biomarker screening and environmental toxicological research. 3D-MSI quantitative analysis provides accurate spatial information and quantitative variation of biomolecules, which may be valuable for the exploration of the molecular mechanism of the disease progresses and toxicological assessment of environmental pollutants in the whole organism. Additionally, we also discuss the challenges and perspectives on the future of 3D quantitative MSI.

show abstract

“…Other ion mobility separation techniques, for example, trapped ion mobility spectrometry (TIMS) [37], may offer similar advantages. A recent study also investigated the ability to derive quantitative measurements of protein concentration directly from tissue during LESA MS experiments [38].…”

Section: Liquid Extraction Surface Analysis (Lesa)mentioning

confidence: 99%

In situ mass spectrometry analysis of intact proteins and protein complexes from biological substrates

Hale

Cooper

2020

Biochemical Society Transactions

Self Cite

View full text Add to dashboard Cite

Advances in sample preparation, ion sources and mass spectrometer technology have enabled the detection and characterisation of intact proteins. The challenges associated include an appropriately soft ionisation event, efficient transmission and detection of the often delicate macromolecules. Ambient ion sources, in particular, offer a wealth of strategies for analysis of proteins from solution environments, and directly from biological substrates. The last two decades have seen rapid development in this area. Innovations include liquid extraction surface analysis, desorption electrospray ionisation and nanospray desorption electrospray ionisation. Similarly, developments in native mass spectrometry allow protein–protein and protein–ligand complexes to be ionised and analysed. Identification and characterisation of these large ions involves a suite of hyphenated mass spectrometry techniques, often including the coupling of ion mobility spectrometry and fragmentation techniques. The latter include collision, electron and photon-induced methods, each with their own characteristics and benefits for intact protein identification. In this review, recent developments for in situ protein analysis are explored, with a focus on ion sources and tandem mass spectrometry techniques used for identification.

show abstract

Quantitative Imaging of Proteins in Tissue by Stable Isotope Labeled Mimetic Liquid Extraction Surface Analysis Mass Spectrometry

Cited by 23 publications

References 17 publications

Spatially resolved absolute quantitation in thin tissue by mass spectrometry

Spatially resolved absolute quantitation in thin tissue by mass spectrometry

Three‐dimensional quantitative mass spectrometry imaging in complex system: From subcellular to whole organism

In situ mass spectrometry analysis of intact proteins and protein complexes from biological substrates

Contact Info

Product

Resources

About