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The family of ubiquitin (Ub)-specific proteases (USP) removes Ub from Ub conjugates and regulates a variety of cellular processes. The human genome contains many putative USP-encoding genes, but little is known about USP tissue distribution, pattern of expression, activity, and substrate specificity. We have used a chemistry-based functional proteomics approach to identify active USPs in normal, virus-infected, and tumor-derived human cells. Depending on tissue origin and stage of activation/differentiation, different USP activity profiles were revealed. The activity of specific USPs, including USP5, -7, -9, -13, -15, and -22, was up-regulated by mitogen activation or virus infection in normal T and B lymphocytes. UCH-L1 was highly expressed in tumor cell lines of epithelial and hematopoietic cell origin but was not detected in freshly isolated and mitogen-activated cells. Up-regulation of this USP was a late event in the establishment of Epstein-Barr virus-immortalized lymphoblastoid cell lines and correlated with enhanced proliferation, suggesting a possible role in growth transformation.

Type

Journal article

Journal

Proc Natl Acad Sci U S A

Publication Date

24/02/2004

Volume

101

Pages

2253 - 2258

Keywords

B-Lymphocytes, Cell Line, Cell Line, Tumor, Endopeptidases, Humans, Mass Spectrometry, T-Lymphocytes, Ubiquitin Thiolesterase, Ubiquitin-Specific Peptidase 7, Ubiquitin-Specific Proteases