Premium
Direct analysis of laser capture microdissected endometrial carcinoma and epithelium by matrix‐assisted laser desorption/ionization mass spectrometry
Author(s) -
Guo Jingzhong,
Colgan Terence J.,
DeSouza Leroi V.,
Rodrigues Mary Joe,
Romaschin Alexander D.,
Siu K. W. Michael
Publication year - 2005
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.2119
Subject(s) - chemistry , mass spectrometry , desorption , laser , matrix assisted laser desorption electrospray ionization , mass spectrometry imaging , surface enhanced laser desorption/ionization , ionization , matrix (chemical analysis) , matrix assisted laser desorption/ionization , analytical chemistry (journal) , chromatography , sample preparation in mass spectrometry , electrospray ionization , ion , adsorption , optics , organic chemistry , physics
Direct analysis of laser capture microdissected malignant and normal endometrial epithelium using matrix‐assisted laser desorption/ionization (MALDI) time‐of‐flight mass spectrometry (MS) was able to detect a number of proteins that are overexpressed in malignant epithelial cells. A total of 16 physiologic and malignant endometrial samples were laser capture microdissected, including four proliferative and four secretory endometria, and eight endometrioid adenocarcinomas. Two of these proteins, at 10 834 and 10 843 Da, likely correspond to calgranulin A and chaperonin 10, two proteins that had previously been identified in endometrioid adenocarcinoma in whole tissue homogenate by MS analysis. Direct analysis by MALDI‐MS not only confirms that these proteins are overexpressed in endometrial carcinoma, but also localizes them to the epithelial cells, the expected cancer site. Copyright © 2005 John Wiley & Sons, Ltd.