| Grant number: | 15/21786-8 |
| Support Opportunities: | Regular Research Grants |
| Start date: | March 01, 2016 |
| End date: | May 31, 2018 |
| Field of knowledge: | Biological Sciences - Biochemistry - Molecular Biology |
| Principal Investigator: | Deborah Schechtman |
| Grantee: | Deborah Schechtman |
| Host Institution: | Instituto de Química (IQ). Universidade de São Paulo (USP). São Paulo , SP, Brazil |
Abstract
Data from the literature sugests that one of the problems to study the role of PKCs is the lack of tools that can distinguish specifically the inactive from active forms of the different protein kinase C (PKC) isoenzymes. Differently than other kinases, for example, ERK and JNK in which activation is determined by phosphorylation of the activation loop. Phosphorylations suffered in particular by classical cPKCs are part of the maturation/ folding process of these kinases. and does not correlate with their activation. Complete activation of cPKCs is seen by binding to activating lipids and conformational changes that expose substrate and ATP interaction sites. Based on conformational changes that ocurr in cPKCs upon their activation our group developed poly and mono clonal antibodies that specificaly recognize active cPKCs. In the present project we wish to continue characterizing these antibodies and with this new tool continue to study the activity of cPKCs and interactions with its substratesin breast cancer cell lines estrogen receptor positive (ER+)and triple negative, and in samples from patients with these tumors. We will also verrify the activity of cPKCs in other models. (AU)
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