| Full text | |
| Author(s): |
Total Authors: 2
|
| Affiliation: | [1] Univ Sao Paulo, Dept Bioquim, Inst Quim, BR-05508900 Sao Paulo - Brazil
[2] Univ Sao Paulo, Dept Biol Celular & Desenvolvimento, Inst Ciencias Biomed, BR-05508900 Sao Paulo - Brazil
Total Affiliations: 2
|
| Document type: | Journal article |
| Source: | FEBS OPEN BIO; v. 2, p. 93-97, 2012. |
| Web of Science Citations: | 7 |
| Abstract | |
Maspin is a tumor suppressor with many biological activities, multiple ligands and different subcellular localizations. Its underlying molecular mechanism remains elusive. We hypothesized that phosphorylation might regulate maspin localization and function. Using two-dimensional gel electrophoresis with different focusing power followed by Western blot we identified four different maspin forms with the same molecular weight (42 kDa), but different isoelectric points. Three of these forms were sensitive to acidic phosphatase treatment, suggesting that they are phosphorylated. Sodium peroxidovanadate treatment, a protein-tyrosine phosphatase inhibitor, resulted in a rapid increase in maspin protein levels and cytoplasmic accumulation. These data show that there are three different maspin tyrosine phosphoforms. Inhibition of tyrosine phosphatases increased maspin protein levels and leads to its cytoplasmic accumulation. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved. (AU) | |
| FAPESP's process: | 09/12597-6 - Characterization of posttranslational modifications of maspin and correlation with subcellular localization |
| Grantee: | Mariana Tamazato Longhi |
| Support Opportunities: | Scholarships in Brazil - Master |