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Profiling and imaging proteins in the mouse epididymis by imaging mass spectrometry
Author(s) -
Chaurand Pierre,
Fouchécourt Sophie,
DaGue Beverly B.,
Xu Baogang J.,
Reyzer Michelle L.,
OrgebinCrist MarieClaire,
Caprioli Richard M.
Publication year - 2003
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200300474
Subject(s) - epididymis , laser capture microdissection , mass spectrometry , mass spectrometry imaging , proteomics , matrix assisted laser desorption/ionization , maldi imaging , chemistry , resolution (logic) , computational biology , biology , chromatography , biochemistry , desorption , computer science , artificial intelligence , gene expression , genetics , gene , organic chemistry , adsorption , sperm
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.