TY - JOUR
T1 - Mass spectrometry imaging and profiling of single cells
AU - Lanni, Eric J.
AU - Rubakhin, Stanislav S.
AU - Sweedler, Jonathan V.
N1 - Funding Information:
This work was supported by Award No. P30 DA018310 from the National Institute on Drug Abuse (NIDA) and the Department of Energy by Award No. DE-SC0006642 . The content is solely the responsibility of the authors and does not necessarily represent the official views of the funding agencies. We also thank Stephanie Baker for assistance with manuscript preparation and reviewers for helpful feedback. The authors declare they have no conflicts of interest.
PY - 2012/8/30
Y1 - 2012/8/30
N2 - Mass spectrometry imaging and profiling of individual cells and subcellular structures provide unique analytical capabilities for biological and biomedical research, including determination of the biochemical heterogeneity of cellular populations and intracellular localization of pharmaceuticals. Two mass spectrometry technologies-secondary ion mass spectrometry (SIMS) and matrix assisted laser desorption/ionization mass spectrometry (MALDI MS)-are most often used in micro-bioanalytical investigations. Recent advances in ion probe technologies have increased the dynamic range and sensitivity of analyte detection by SIMS, allowing two- and three-dimensional localization of analytes in a variety of cells. SIMS operating in the mass spectrometry imaging (MSI) mode can routinely reach spatial resolutions at the submicron level; therefore, it is frequently used in studies of the chemical composition of subcellular structures. MALDI MS offers a large mass range and high sensitivity of analyte detection. It has been successfully applied in a variety of single-cell and organelle profiling studies. Innovative instrumentation such as scanning microprobe MALDI and mass microscope spectrometers enables new subcellular MSI measurements. Other approaches for MS-based chemical imaging and profiling include those based on near-field laser ablation and inductively-coupled plasma MS analysis, which offer complementary capabilities for subcellular chemical imaging and profiling.This article is part of a Special Issue entitled: Imaging Mass Spectrometry: A User's Guide to a New Technique for Biological and Biomedical Research.
AB - Mass spectrometry imaging and profiling of individual cells and subcellular structures provide unique analytical capabilities for biological and biomedical research, including determination of the biochemical heterogeneity of cellular populations and intracellular localization of pharmaceuticals. Two mass spectrometry technologies-secondary ion mass spectrometry (SIMS) and matrix assisted laser desorption/ionization mass spectrometry (MALDI MS)-are most often used in micro-bioanalytical investigations. Recent advances in ion probe technologies have increased the dynamic range and sensitivity of analyte detection by SIMS, allowing two- and three-dimensional localization of analytes in a variety of cells. SIMS operating in the mass spectrometry imaging (MSI) mode can routinely reach spatial resolutions at the submicron level; therefore, it is frequently used in studies of the chemical composition of subcellular structures. MALDI MS offers a large mass range and high sensitivity of analyte detection. It has been successfully applied in a variety of single-cell and organelle profiling studies. Innovative instrumentation such as scanning microprobe MALDI and mass microscope spectrometers enables new subcellular MSI measurements. Other approaches for MS-based chemical imaging and profiling include those based on near-field laser ablation and inductively-coupled plasma MS analysis, which offer complementary capabilities for subcellular chemical imaging and profiling.This article is part of a Special Issue entitled: Imaging Mass Spectrometry: A User's Guide to a New Technique for Biological and Biomedical Research.
KW - Elemental imaging
KW - Mass cytometry
KW - Matrix assisted laser desorption/ionization
KW - Secondary ion mass spectrometry
KW - Subcellular profiling
KW - Tissue imaging
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U2 - 10.1016/j.jprot.2012.03.017
DO - 10.1016/j.jprot.2012.03.017
M3 - Review article
C2 - 22498881
AN - SCOPUS:84865179242
SN - 1874-3919
VL - 75
SP - 5036
EP - 5051
JO - Journal of Proteomics
JF - Journal of Proteomics
IS - 16
ER -