Spatial profiling invertebrate ganglia using MALDI MS

Kruse, Rebecca A.; Sweedler, Jonathan V.

doi:10.1016/s1044-0305(03)00288-5

Cited by 108 publications

(102 citation statements)

References 36 publications

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“…Mass resolved images or spectra from regions of interest are then extracted from the dataset. The spatial resolution obtained in MALDI microprobe imaging is typically in the 100 to 200 m range, limited by the size of the laser spot used [31,32]. The development of micrometer resolution has been reported [33], however decreasing spot size has been found to lead to decreasing sensitivity for high mass species.…”

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confidence: 99%

Imaging of peptides in the rat brain using MALDI-FTICR mass spectrometry

Taban

Altelaar

Burgt

et al. 2007

J. Am. Soc. Mass Spectrom.

148

136

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Analytical methods are pursued to measure the identity and location of biomolecules down to the subcellular ( m) level. Available mass spectrometric imaging methods either compromise localization accuracy or identification accuracy in their analysis of surface biomolecules. In this study, imaging FTICR-MS is applied for the spatially resolved mass analysis of rat brain tissue with the aim to optimize protein identification by the high mass accuracy and online MS/MS capabilities of the technique. Mass accuracies up to 6 ppm were obtained in the direct MALDI-analysis of the tissue together with a spatial resolution of 200 m. The spatial distributions of biomolecules differing in mass by less than 0.1 Da could be resolved, and are shown to differ significantly. Online MS/MS analysis of selected ions was demonstrated. A comparison of the FTICR-MS imaging results with stigmatic TOF imaging on the same sample is presented. To reduce the extended measuring times involved, it is recommended to restrict the FTICR-MS analyses to areas of interest as can be preselected by other, faster imaging methods. (J Am Soc Mass Spectrom 2007, 18, 145-151)

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Imaging of peptides in the rat brain using MALDI-FTICR mass spectrometry

Taban

Altelaar

Burgt

et al. 2007

J. Am. Soc. Mass Spectrom.

148

136

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“…It has been roughly 10 years since the first published applications in which MALDI-MS was used to create a chemical images of substrates [4,5]. The intervening decade has seen a considerable growth in techniques and instrumentation for MALDI-MS imaging, developed largely by Caprioli and coworkers [6 -12] with contributions to sampling techniques [13][14][15][16] and instrumentation [17,18] provided by others.It is generally accepted that the maximal spatial imaging or profiling resolution of microprobe imaging techniques is determined by a combination of the size of the microprobe and the precision of the sample or microprobe positioning device. MALDI mass spectrometers typically use lasers having relatively large beam sizes (about 100 m diameter) in the analysis of standard, dried-droplet preparations.…”

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confidence: 99%

“…Some effort has been put into decreasing the size of the laser beam sizes for MALDI-MS imaging and profiling of biological samples, particularly for samples containing a high proportion of peptidergic neurons or other secretory cells. Investigated biological samples of this nature include rat pituitary and rat pancreas [6], mouse brain and human brain tumor xenografts [8,14], rat brain and rat brain tumors [9,19], mouse epididymis [20], molluscan atrial gland [15], and molluscan peptidergic neurons [16].Ideally, the spatial resolution of MALDI-MS imaging of analyte-rich tissues would approach the size of a single mammalian cell, 5 to 20 m in diameter. Several strategies have been used or suggested to decrease the laser beam diameter in imaging applications, including the placement of a pinhole aperture between the outlet of the laser and the focusing optics of the mass spectrometer [6,13], decreasing the size of the fiber optic used to direct the laser into the MALDI source [9], and placing multiple lenses between the laser and the MALDI source [17].…”

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MALDI-MS imaging of features smaller than the size of the laser beam

Jurchen

Rubakhin

Sweedler

2005

J. Am. Soc. Mass Spectrom.

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265

223

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The feasibility of matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) imaging of features smaller than the laser beam size has been demonstrated. The method involves the complete ablation of the MALDI matrix coating the sample at each sample position and moving the sample target a distance less than the diameter of the laser beam before repeating the process. In the limit of complete sample ablation, acquiring signal from adjacent positions spaced by distances smaller than the sample probe enhances image resolution as the measured analyte signal only arises from the overlap of the laser beam size and the non-ablated sample surface. [3] has revolutionized the investigation of biological molecules by providing soft ionization methods linking biochemistry with the powerful analysis tools of mass spectrometry (MS). In the analysis of complex samples, such as biological tissue, MALDI is of particular interest because of its ability to desorb and ionize molecules of high molecular weight, such as proteins and peptides, providing excellent sensitivity while retaining considerable tolerance towards salts and other small molecules found at high concentration in tissue. It has been roughly 10 years since the first published applications in which MALDI-MS was used to create a chemical images of substrates [4,5]. The intervening decade has seen a considerable growth in techniques and instrumentation for MALDI-MS imaging, developed largely by Caprioli and coworkers [6 -12] with contributions to sampling techniques [13][14][15][16] and instrumentation [17,18] provided by others.It is generally accepted that the maximal spatial imaging or profiling resolution of microprobe imaging techniques is determined by a combination of the size of the microprobe and the precision of the sample or microprobe positioning device. MALDI mass spectrometers typically use lasers having relatively large beam sizes (about 100 m diameter) in the analysis of standard, dried-droplet preparations. Some effort has been put into decreasing the size of the laser beam sizes for MALDI-MS imaging and profiling of biological samples, particularly for samples containing a high proportion of peptidergic neurons or other secretory cells. Investigated biological samples of this nature include rat pituitary and rat pancreas [6], mouse brain and human brain tumor xenografts [8,14], rat brain and rat brain tumors [9,19], mouse epididymis [20], molluscan atrial gland [15], and molluscan peptidergic neurons [16].Ideally, the spatial resolution of MALDI-MS imaging of analyte-rich tissues would approach the size of a single mammalian cell, 5 to 20 m in diameter. Several strategies have been used or suggested to decrease the laser beam diameter in imaging applications, including the placement of a pinhole aperture between the outlet of the laser and the focusing optics of the mass spectrometer [6,13], decreasing the size of the fiber optic used to direct the laser into the MALDI source [9], and placing multiple lenses between the laser and the M...

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“…Les études menées par ce dernier groupe ont permis de montrer la faisabilité de la méthode pour suivre les profils d'expression des peptides/protéines directement au sein de tissus sans traitement préalable [8]. Les résultats obtenus par d'autres équipes ont porté sur la cartographie, la distribution spatiale ou la modulation, suite à des traitements, de la libération de neuropeptides dans le système nerveux de différents modèles d'études [9][10][11]. …”

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