Alpha-Parvin is a focal-adhesion associated protein found in most cell types and our work hopes to use the protein as novel model for studying quantifiable differences in a cells ability to metastasize. Alpha-Parvin has not been looked at in the uterus before. The phosphorylation of alpha-parvin has been shown to be associated with cell movement and focal adhesion disassembly. MAPK/Erk is a protein which has been shown to phosphorylate alpha-parvin which increases cell movement and adhesive degradation. By studying the localisation of these two proteins during early pregnancy in the rat, we have been able to research the role that the protein plays in focal adhesion disassembly, as during the time of implantation these adhesive complexes in the epithelium lining the lumen disassemble to facilitate blastocyst attachment.
By determining the localization and amount of alpha-parvin and MAPK/Erk in early pregnancy, we suggest a relationship between the two in coordinating focal adhesion disassembly.
Using immunohistochemical and western blotting techniques, we looked at the amount and localisation of Alpha-Parvin during early pregnancy. Alpha-Parvin is present and basally located at the time of fertilization, which shows its association as a focal adhesion protein. At the time of implantation, when the complexes are disassembled, Alpha-Parvin is significantly decreased. We also showed that phosphorylated Alpha-Parvin has a reciprocal relationship, in that it is significantly increased at implantation suggesting its role in focal adhesion disassembly. Preliminary MAPK/Erk results also show a similar localisation to phosphorylated alpha-parvin at the time of implantation.
We show for the first time that Alpha-Parvin is phosphorylated prior to focal adhesion disassembly during early pregnancy and that this phosphorylation could be indicative of a phosphorylation-dependent focal adhesion disassembly.