Open AccessSpatial profiling invertebrate ganglia using MALDI MS
Author(s) -
Rebecca A. Kruse,
Jonathan V. Sweedler
Publication year - 2003
Publication title -
journal of the american society for mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.961
H-Index - 127
eISSN - 1879-1123
pISSN - 1044-0305
DOI - 10.1016/s1044-0305(03)00288-5
Subject(s) - maldi imaging , chemistry , aplysia , mass spectrometry , mass spectrometry imaging , electrospray , chromatography , high resolution , matrix (chemical analysis) , matrix assisted laser desorption/ionization , biological system , computational biology , neuroscience , biology , remote sensing , organic chemistry , adsorption , desorption , geology
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, with the exact protocols being tissue dependent.