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Maspin alters the carcinoma proteome
Author(s) -
Chen Emily I.,
Florens Laurence,
Axelrod Fumiko T.,
Monosov Edward,
Barbas Carlos F.,
Yates John R.,
FeldingHabermann Brunhilde,
Smith Jeffrey W.
Publication year - 2005
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fj.04-2970fje
Subject(s) - maspin , serpin , proteome , proteomics , proteasome , biology , microbiology and biotechnology , cancer research , cytoskeleton , shotgun proteomics , function (biology) , cancer , cell , metastasis , bioinformatics , biochemistry , genetics , gene
Maspin, a member of the serine protease inhibitor (serpin) family, is a tumor suppressor in breast and prostate cancer. To address molecular mechanisms underlying maspin's activity, we restored its expression in invasive carcinoma cells and analyzed the resulting changes by shotgun proteomics. Using a mass spectrometry‐based multidimensional proteomic method, we observed changes to the expression of ∼27% of the detectable proteome. In particular, we noted changes to the expression of proteins that regulate cytoskeletal architecture, cell death, and protein turnover. In each case, changes in protein expression were accompanied by measurable changes in tumor cell phenotype. Thus, maspin‐expressing cells exhibit a more prominent actin cytoskeleton, a reduced invasive capacity, an increased rate of spontaneous apoptosis, and an altered proteasome function. These observations reveal for the first time the far reaching effects of maspin on multiple protein networks and a new hypothesis of maspin function based on the regulation of proteasome function.