Direct cellular assays using off-line capillary electrophoresis with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

Page, Jason S.; Rubakhin, Stanislav S.; Sweedler, Jonathan V.

doi:10.1039/a909738d

Cited by 35 publications

(57 citation statements)

References 51 publications

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“…After the tissue was placed on the target, matrix was applied. The CHCA and SA matrices [15-20 mg/mL 3:2 (vol/vol) acetonitrile:0.3 % TFA] were deposited in multiple layers with electrospray using a modified homebuilt electrophoresis apparatus described previously [23] or by micro-spotting using a capillary micropipette device [15]. Briefly, for electrospray matrix deposition a syringe pump (Harvard Apparatus, South Natick, MA) delivered matrix to the tip of a 50 m i.d./150 m o.d.…”

Section: Sample Preparationmentioning

confidence: 99%

Spatial profiling invertebrate ganglia using MALDI MS

Kruse

Sweedler

2003

J. Am. Soc. Mass Spectrom.

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108

100

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The ability of MALDI TOF MS to spatially map peptides and proteins directly from a tissue is an exciting advance to imaging mass spectrometry. Recent advances in instrumentation for MS have resulted in instruments capable of achieving several micron spatial resolution while acquiring high-resolution mass spectra. Currently, the ability to obtain high quality mass spectrometric images depends on sample preparation protocols that often result in limited spatial resolution. A number of sample preparation and matrix deposition protocols are evaluated for spatial profiling of Aplysia californica exocrine gland and neuronal tissues. Such samples are different from mammalian tissues, but make good targets for method optimization because of the wealth of biochemical information available on neuropeptide processing and distribution. Electrospray matrix deposition and a variety of freezing methods have been found to be optimum for these invertebrate tissues,

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Section: Sample Preparationmentioning

confidence: 99%

Spatial profiling invertebrate ganglia using MALDI MS

Kruse

Sweedler

2003

J. Am. Soc. Mass Spectrom.

Self Cite

108

100

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show abstract

“…A large number of single-cell studies employing MALDI-MS were conducted in the group of Sweedler. Methods for analysis of peptides and proteins in single neurons of animals, such as Aplysia californica, have been developed [55,56,[62][63][64]. MALDI-MS has also been shown to have outstanding sensitivity for primary metabolites, such as nucleotides [65]: the sensitivity is sufficient to detect nucleotides in single yeast cells.…”

Section: Electrochemical Detectionmentioning

confidence: 99%

Analytical techniques for single-cell metabolomics: state of the art and trends

2010

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Single-cell metabolomics is an emerging field that addresses fundamental biological questions and allows one to observe metabolic phenomena in heterogeneous populations of single cells. In this review, we assess the suitability of different detection techniques and present considerations on sample preparation for single-cell metabolomics. Although targeted analysis of single cells can readily be conducted using fluorescent probes and optical instruments (microscopes, fluorescence detectors), a comprehensive metabolomic approach requires a powerful label-free method, such as mass spectrometry (MS). Mass-spectrometric techniques applied to study small molecules in single cells include electrospray MS, matrix-assisted laser desorption/ionization MS, and secondary ion MS. Sample preparation is an important aspect to be taken into account during further development of methods for single-cell metabolomics.

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“…There are a variety of examples where CE has been combined with MALDI-MS. These methods range from continuous deposition of the CE effluent onto a membrane [15,16] to the collection of fractions in small vials or directly onto a MALDI target [17][18][19][20]. In our method, nanoliter-volume fractions were directly spotted onto MALDI target plates.…”

Section: Introductionmentioning

confidence: 99%

Comprehensive two‐dimensional chromatography and capillary electrophoresis coupled with tandem time‐of‐flight mass spectrometry for high‐speed proteome analysis

Zhang

Gao

et al. 2004

Electrophoresis

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A comprehensive two-dimensional capillary liquid chromatography and capillary zone electrophoresis system coupled with tandem matrix assisted laser desorption/ionization-time of flight-time of flight-mass spectrometry (MALDI-TOF-TOF-MS) proteomics analyzer is presented. Protein/peptide samples were separated by capillary high-performance liquid chromatography (cHPLC). The effluents from cHPLC (the first dimension) were continuously transferred into capillary zone electrophoresis (CZE, the second dimension) through a novel valve-free hydrodynamic sampling interface. The CZE effluents were mixed with alpha-cyano-4-hydroxycinnamic acid (CHCA) matrix sheath flow via CE-MALDI interface, and then directly deposited on the MALDI target at a 3 s time-interval for further MS analysis. The high efficiency of the overall system was demonstrated by analysis of proteins in D20 (human hepatocellular carcinoma model in nude mice with high metastatic potential) liver cancer tissue. More than 300 proteins were identified, which proved the system potential for high-throughput analysis and application in proteomics.

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Direct cellular assays using off-line capillary electrophoresis with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

Cited by 35 publications

References 51 publications

Spatial profiling invertebrate ganglia using MALDI MS

Spatial profiling invertebrate ganglia using MALDI MS

Analytical techniques for single-cell metabolomics: state of the art and trends

Comprehensive two‐dimensional chromatography and capillary electrophoresis coupled with tandem time‐of‐flight mass spectrometry for high‐speed proteome analysis

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