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Imaging Mass Spectrometry (imaging + mass_spectrometry)
Kinds of Imaging Mass Spectrometry Selected AbstractsDiscrimination of Human Astrocytoma Subtypes by Lipid Analysis Using Desorption Electrospray Ionization Imaging Mass Spectrometry,ANGEWANDTE CHEMIE, Issue 34 2010Livia Die Differenzierung von astrozytischen Hirntumorgraden kann durch direkte Lipidanalyse mittels Desorptions-Elektrosprayionisations-Massenspektrometrie (DESI-MS) erreicht werden. Charakteristische Lipidprofile sind mit der Tumormalignanz entsprechend den WHO-Graden II, III und IV assoziiert (siehe Bild). [source] Imaging Mass Spectrometry with a Low-Temperature Plasma Probe for the Analysis of Works of Art,ANGEWANDTE CHEMIE, Issue 26 2010Yueying Liu Welch ein Bild! Siegelmuster auf Gemälden und Kalligraphien wurden mit einer massenspektrometrischen Technik abgebildet. Dabei kam eine Niedertemperatur-Plasmasonde zum Einsatz, die eine gute räumliche Auflösung liefert. Mit dieser Methode kann zwischen echten und gefälschten Siegeln unterschieden werden. [source] Perspectives for imaging mass spectrometry in the proteomics landscapePROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 4 2009Luke MacAleese Abstract A number of techniques are used in the field of proteomics that can be combined to get the most molecular information from a specific biological sample, fluid or tissue. Imaging techniques are often used to obtain local information from tissue samples. However, imaging experiments are often staining experiments, which rely on specific or aspecific interactions between fluorescent markers and pre-defined (families of) peptide or protein. Therefore, imaging is often used as a screening or validation tool for the local presence of proteins that have been identified by other means. Imaging mass spectrometry (IMS) combines the advantages of MS and microscopy in a single experiment. It is a technique that does not require any labeling of the analytes and provides a high multiplexing capability combined with the potential for analyte identification. It enables simultaneous detection of potentially all peptides and proteins present at a tissue surface and is used for the determination and identification of tissue-specific disease markers. The workflows of IMS experiments closely resemble those of conventional proteomics. In this review, we describe IMS experiments step-by-step to position and evaluate the role of IMS in a comparative proteomics landscape. We illustrate in a concise review that IMS is a true discovery oriented tool for proteomics that seamlessly integrates in conventional proteomics workflows and can be perceived as either an alternative or complementary proteomics technique. [source] Imaging mass spectrometry: Towards clinical diagnosticsPROTEOMICS - CLINICAL APPLICATIONS, Issue 10-11 2008Erin H. Seeley Abstract Imaging MS (IMS) has emerged as a powerful tool for biomarker discovery. A key advantage of this technique is its ability to probe the proteome directly from a tissue section with preservation of the spatial relationships of the sample and minimal sample preparation. This allows for direct correlation of protein expression with histology. Here, we present the latest developments in imaging MS and their relevance to clinical mass spectral analysis. IMS allows for high throughput analysis of tissue samples and is fully compatible with biostatistical analysis without prior knowledge of protein expression. Several studies are presented of applications in which direct tissue mass spectral analysis has provided insight into clinical questions not readily available by other means. Examples include the determination of lymph node status from investigation of primary breast tumors, prediction of response of breast tumors to chemotherapy, classification and prediction of progression of lung lesions, and exploration of ,molecular' margins in invasive disease. [source] Imaging mass spectrometry for examining localization of polymeric composition in matrix-assisted laser desorption/ionization samplesRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 5 2009Steffen M. Weidner The localization of polymeric composition in samples prepared for matrix-assisted laser desorption/ionization (MALDI) analysis has been investigated by imaging mass spectrometry. Various matrices and solvents were used for sample spot preparation of a polybutyleneglycol (PBG 1000). It was shown that in visibly homogeneous spots, prepared using the ,dried droplet' method, separation between matrix and polymer takes place. Moreover, using , -cyano-4-hydroxycinnamic acid (CCA) as matrix and methanol as solvent molecular mass separation of the polymer homologues in the spots was detectable. In contrast to manually spotted samples, dry spray deposition results in homogeneous layers showing no separation effects. Copyright © 2009 John Wiley & Sons, Ltd. [source] Imaging of uranium on rat brain sections using laser ablation inductively coupled plasma mass spectrometry: a new tool for the study of critical substructures affined to heavy metals in tissuesRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 18 2008J. Sabine Becker The specific toxicity of trace metals and compounds largely depends on their bioavailability in different organs or compartments of the organism considered. Imaging mass spectrometry (IMS) using laser ablation inductively coupled plasma mass spectrometry (LA-ICP-MS) with a spatial resolution in the 100,µm range was developed and employed to study heavy metal distribution in brain tissues for toxicological screening. Rat brain post-mortem tissues were stained in an aqueous solution of either uranium or neodymium (metal concentration 100,µg,g,1) for 3,h. The incubation of heavy metal in thin slices of brain tissue is followed by an imaging mass spectrometric LA-ICP-MS technique. Stained rat brain tissue (thickness 30,µm) were scanned with a focused laser beam (wavelength 266,nm, diameter of laser crater 100,µm and laser power density 3,×,109,W,cm,2). The ion intensities of 235U+, 238U+, 145Nd+ and 146Nd+ were measured by LA-ICP-MS within the ablated area. For quantification purposes, matrix-matched laboratory standards were prepared by dosing each analyte to the pieces of homogenized brain tissue. Imaging LA-ICP-MS allows structures of interest to be identified and the relevant dose range to be estimated. Copyright © 2008 John Wiley & Sons, Ltd. [source] Identification of proteins directly from tissue: in situ tryptic digestions coupled with imaging mass spectrometryJOURNAL OF MASS SPECTROMETRY (INCORP BIOLOGICAL MASS SPECTROMETRY), Issue 2 2007M. Reid Groseclose Abstract A novel method for on-tissue identification of proteins in spatially discrete regions is described using tryptic digestion followed by matrix-assisted laser desorption/ionization (MALDI) imaging mass spectrometry (IMS) with MS/MS analysis. IMS is first used to reveal the protein and peptide spatial distribution in a tissue section and then a serial section is robotically spotted with small volumes of trypsin solution to carry out in situ protease digestion. After hydrolysis, 2,5-Dihydroxybenzoic acid (DHB) matrix solution is applied to the digested spots, with subsequent analysis by IMS to reveal the spatial distribution of the various tryptic fragments. Sequence determination of the tryptic fragments is performed using on-tissue MALDI MS/MS analysis directly from the individual digest spots. This protocol enables protein identification directly from tissue while preserving the spatial integrity of the tissue sample. The procedure is demonstrated with the identification of several proteins in the coronal sections of a rat brain. Copyright © 2007 John Wiley & Sons, Ltd. [source] Perspectives for imaging mass spectrometry in the proteomics landscapePROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 4 2009Luke MacAleese Abstract A number of techniques are used in the field of proteomics that can be combined to get the most molecular information from a specific biological sample, fluid or tissue. Imaging techniques are often used to obtain local information from tissue samples. However, imaging experiments are often staining experiments, which rely on specific or aspecific interactions between fluorescent markers and pre-defined (families of) peptide or protein. Therefore, imaging is often used as a screening or validation tool for the local presence of proteins that have been identified by other means. Imaging mass spectrometry (IMS) combines the advantages of MS and microscopy in a single experiment. It is a technique that does not require any labeling of the analytes and provides a high multiplexing capability combined with the potential for analyte identification. It enables simultaneous detection of potentially all peptides and proteins present at a tissue surface and is used for the determination and identification of tissue-specific disease markers. The workflows of IMS experiments closely resemble those of conventional proteomics. In this review, we describe IMS experiments step-by-step to position and evaluate the role of IMS in a comparative proteomics landscape. We illustrate in a concise review that IMS is a true discovery oriented tool for proteomics that seamlessly integrates in conventional proteomics workflows and can be perceived as either an alternative or complementary proteomics technique. [source] In situ localisation and quantification of surfactins in a Bacillus subtilis swarming community by imaging mass spectrometryPROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 18 2008Delphine Debois Abstract Surfactins are a family of heptacyclopeptides in which the C-terminal carbonyl is linked with the ,-hydroxy group of a fatty acid acylating the N-terminal function of a glutamic acid residue. The fatty acyl chain is 12,16 carbon atoms long. These compounds, which are secreted by the Gram-positive bacterium Bacillus subtilis in stationary phase in liquid cultures, play an important role in swarming communities on the surface of agar media in the formation of dendritic patterns. TOF secondary ion MS (TOF-SIMS) imaging was used to map surfactins within 16,17,h swarming patterns, with a 2,,m spatial resolution. Surfactins were mainly located in the central mother colony (the site of initial inoculation), in a ,ring' surrounding the pattern and along the edges of the dendrites. In the mother colony and the interior of the dendrites, surfactins with shorter chain lengths are present, whereas in the ring surrounding the swarm community and between dendrites, surfactins with longer fatty acyl chain lengths were found. A quantitative analysis by MALDI-TOF MS showed a concentration gradient of surfactin from the mother colony to the periphery. The concentration of surfactin was ,400,pmol/mL in the mother colony and ,10,pmol/mL at the base of the dendrites, decreasing to 2,pmol/mL at their tips. [source] Matrix-assisted laser desorption/ionization imaging mass spectrometry of oxaliplatin derivatives in heated intraoperative chemotherapy (HIPEC)-like treated rat kidneyRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 4 2010Amina Bouslimani Oxaliplatin [1,2-diaminocyclohexane (dach)-Pt complex] is a platinum anticancer drug which is mainly used in the treatment of advanced colorectal cancer, particularly in Heated Intraoperative Chemotherapy (HIPEC) for the treatment of colorectal peritoneal carcinomatosis. In order to better understand the penetration of oxaliplatin in treated tissues we performed a direct imaging of tissue sections from HIPEC-like treated rat kidney using matrix-assisted laser desorption/ionization (MALDI) mass spectrometry. This procedure allowed the detection and localization of oxaliplatin and its metabolites, the monocysteine and monomethionine complexes, in kidney sections. Specifically, oxaliplatin and its metabolites were localized exclusively in the kidney cortex, suggesting that it did not penetrate deeply into the organ. Based on these results, an imaging analysis of human tumors collected after HIPEC is currently in progress to assess the distribution of oxaliplatin and/or metabolites with the aim of defining clinical conditions to improve drug penetration. Copyright © 2010 John Wiley & Sons, Ltd. [source] Matrix vapor deposition/recrystallization and dedicated spray preparation for high-resolution scanning microprobe matrix-assisted laser desorption/ionization imaging mass spectrometry (SMALDI-MS) of tissue and single cellsRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 3 2010Werner Bouschen Matrix preparation techniques such as air spraying or vapor deposition were investigated with respect to lateral migration, integration of analyte into matrix crystals and achievable lateral resolution for the purpose of high-resolution biological imaging. The accessible mass range was found to be beyond 5000 u with sufficient analytical sensitivity. Gas-assisted spraying methods (using oxygen-free gases) provide a good compromise between crystal integration of analyte and analyte migration within the sample. Controlling preparational parameters with this method, however, is difficult. Separation of the preparation procedure into two steps, instead, leads to an improved control of migration and incorporation. The first step is a dry vapor deposition of matrix onto the investigated sample. In a second step, incorporation of analyte into the matrix crystal is enhanced by a controlled recrystallization of matrix in a saturated water atmosphere. With this latter method an effective analytical resolution of 2,µm in the x and y direction was achieved for scanning microprobe matrix-assisted laser desorption/ionization imaging mass spectrometry (SMALDI-MS). Cultured A-498 cells of human renal carcinoma were successfully investigated by high-resolution MALDI imaging using the new preparation techniques. Copyright © 2010 John Wiley & Sons, Ltd. [source] Selective imaging of positively charged polar and nonpolar lipids by optimizing matrix solution compositionRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 20 2009Yuki Sugiura Previous studies have shown that matrix-assisted laser desorption/ionization,imaging mass spectrometry (MALDI-IMS) is useful for studying the distribution of various small metabolites, particularly lipids. However, in this technique, selective ionization of the target molecules is imperative, particularly when analyzing small molecules. Since the sample clean-up procedures available for the MALDI-IMS of small metabolites are limited, the tissue sample will contain numerous molecular species other than the target molecules. These molecules will compete for ionization resulting in severe ion suppression. Hence, it is necessary to develop and optimize a sample preparation protocol for the target molecules. In this study, through model experiments using reference compounds, we optimized the composition of the matrix solution used for positively charged lipids in terms of the concentration of the organic solvent and presence/absence of alkali metal salts. We demonstrated that a high concentration of organic solvent in the matrix solution favors the preferential detection of lipids over peptides. The presence of alkali metal salts in the matrix solution was favorable for the detection of polar lipids, while a salt-free matrix solution was suitable for the detection of nonpolar lipids. Furthermore, potassium salts added to the matrix solution caused merging of various lipid adducts (adducts with proton, sodium, and potassium) into one single potassiated species. Using the optimized protocols, we selectively analyzed phosphatidylcholine (PC) and triacylglycerol (TG) with different fatty acid compositions in a rat kidney section. Copyright © 2009 John Wiley & Sons, Ltd. [source] Imaging mass spectrometry for examining localization of polymeric composition in matrix-assisted laser desorption/ionization samplesRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 5 2009Steffen M. Weidner The localization of polymeric composition in samples prepared for matrix-assisted laser desorption/ionization (MALDI) analysis has been investigated by imaging mass spectrometry. Various matrices and solvents were used for sample spot preparation of a polybutyleneglycol (PBG 1000). It was shown that in visibly homogeneous spots, prepared using the ,dried droplet' method, separation between matrix and polymer takes place. Moreover, using , -cyano-4-hydroxycinnamic acid (CCA) as matrix and methanol as solvent molecular mass separation of the polymer homologues in the spots was detectable. In contrast to manually spotted samples, dry spray deposition results in homogeneous layers showing no separation effects. Copyright © 2009 John Wiley & Sons, Ltd. [source] The molecular scanner in microscope modeRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 22 2006Stefan L. Luxembourg The combination of microscope mode matrix-assisted laser desorption/ionization (MALDI) imaging mass spectrometry (IMS) with protein identification methodology: the molecular scanner, was explored. The molecular scanner approach provides improvement of sensitivity of detection and identification of high-mass proteins in microscope mode IMS. The methodology was tested on protein distributions obtained after separation by sodium dodecyl sulfate/polyacrylamide gel electrophoresis (SDS-PAGE). High-quality, high-spatial-resolution ion images were recorded on a TRIFT-II ion microscope after gold coating of the MALDI sample preparation on the poly(vinylidenedifluoride) capture membranes. The sensitivity of the combined method is estimated to be 5 pmol. The minimum amount of sample consumed, needed for identification, was estimated to be better than 100 fmol. Software tools were developed to analyze the spectral data and to generate broad mass range and single molecular component microscope mode ion images and single mass-to-charge ratio microprobe mode images. Copyright © 2006 John Wiley & Sons, Ltd. [source] Matrix-assisted laser desorption/ionization imaging mass spectrometry for direct measurement of clozapine in rat brain tissueRAPID COMMUNICATIONS IN MASS SPECTROMETRY, Issue 6 2006Yunsheng Hsieh Matrix-assisted laser desorption/ionization hyphenated with quadrupole time-of-flight (QTOF) mass spectrometry (MS) has been used to directly determine the distribution of pharmaceuticals in rat brain tissue slices which might unravel their disposition for new drug development. Clozapine, an antipsychotic drug, and norclozapine were used as model compounds to investigate fundamental parameters such as matrix and solvent effects and irradiance dependence on MALDI intensity but also to address the issues with direct tissue imaging MS technique such as (1) uniform coating by the matrix, (2) linearity of MALDI signals, and (3) redistribution of surface analytes. The tissue sections were coated with various matrices on MALDI plates by airspray deposition prior to MS detection. MALDI signals of analytes were detected by monitoring the dissociation of the individual protonated molecules to their predominant MS/MS product ions. The matrices were chosen for tissue applications based on their ability to form a homogeneous coating of dense crystals and to yield greater sensitivity. Images revealing the spatial localization in tissue sections using MALDI-QTOF following a direct infusion of 3H-clozapine into rat brain were found to be in good correlation with those using a radioautographic approach. The density of clozapine and its major metabolites from whole brain homogenates was further confirmed using fast high-performance liquid chromatography/tandem mass spectrometry (HPLC-MS/MS) procedures. Copyright © 2006 John Wiley & Sons, Ltd. [source] | ||||||||||