Profiling and imaging proteins in the mouse epididymis by imaging mass spectrometry.
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.
Mass Spectrometry Research Center and Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, USA.
Pierre
P
Chaurand
Sophie
S
Fouchécourt
Beverly B
BB
DaGue
Baogang J
BJ
Xu
Michelle L
ML
Reyzer
Marie-Claire
MC
Orgebin-Crist
Richard M
RM
Caprioli
D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D030562:Databases, Protein; D030501:Epididymal Secretory Proteins / Q000032:analysis / Q000737:chemistry*; D004822:Epididymis / Q000737:chemistry* / Q000166:cytology; D004847:Epithelial Cells / Q000737:chemistry* / Q000166:cytology / Q000378:metabolism; D008297:Male; D051379:Mice; D008969:Molecular Sequence Data; D011506:Proteins / Q000032:analysis / Q000737:chemistry*; D013094:Spermatozoa / Q000737:chemistry* / Q000166:cytology
D030501:Epididymal Secretory Proteins; D011506:Proteins