Journal
PROTEOMICS
Volume 3, Issue 11, Pages 2221-2239Publisher
WILEY
DOI: 10.1002/pmic.200300474
Keywords
epididymis; imaging; laser capture microdissection; mass spectrometry
Funding
- NICHD NIH HHS [HD 36900] Funding Source: Medline
- NIGMS NIH HHS [GM 58008] Funding Source: Medline
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Different aspects of matrix-assisted laser desorption/ionization (MALDI) imaging mass spectrometry (IMS) have been used as discovery tools to obtain global and time-correlated information on the local proteomic composition of the sexually mature mouse epididymis from both qualitative and semiquantitative points of view. Tissue sections and laser captured microdissected cells and secretory products were analyzed by MALDI-MS and from the recovered protein profiles, over 400 different proteins were monitored. Over 50 of these, some of which have been identified, displayed regionalized behavior from caput to cauda within the epididymis. Combining the information obtained from high-resolution imaging mass spectrometry and laser captured microdissection experiments, numerous proteins were localized within the epididymis at the cellular level. Furthermore, from the signal intensities observed in the different protein profiles organized in space, semiquantitative information for each protein was obtained.
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