Akademik Veri Yönetim Sistemi
MIMIC-VI, İstanbul, Türkiye, 28 - 30 Nisan 2025, ss.99, (Özet Bildiri)
Objective PSTPIP1 (Proline-Serine-Threonine Phosphatase Interacting Protein 1) encodes a protein that plays a crucial role in the immune system and cellular signaling. We previously showed that PSTPIP1 p.Arg228Cys variant has an increased interaction with pyrin in FMF patients. The aim of this project is to investigate the relationship between the rare missense variants p.Arg228Cys (NM_003978.5: c.C682T, rs781341816) and p.Ala372Val (NM_003978.5: c.C1115T, rs200188483) in PSTPIP1 and PTP-PEST in vitro cell culture models. Materials and Methods Vectors containing wild type and variant forms of PSTPIP1 were transfected into HEK293FT cell line using lipofectamine. Co-immunoprecipitation was utilized using PSTPIP1 (SantaCruz, B-10) antibody. The protein-antibody mixture was then incubated with Dynabeads® Protein G, and immunoblotting was performed using PSTPIP1 and PTP-PEST antibodies. GAPDH was used as the loading control. Results Overexpression of PSTPIP1 was determined by comparing the transcript levels between the transfected and untransfected samples (2-ΔΔCT method). According to the immunoblotting results, no significant difference was observed between the wild-type and variant forms in their interaction with PTP-PEST. The results were analyzed using GraphPad Prism 8 software (GraphPad Software, San Diego, USA) Conclusion In this study, we investigated the interaction of wild-type and PSTPIP1 variants with PTP-PEST in HEK293FT cells. These findings suggest that the variants do not alter the interaction of PSTPIP1 with PTP-PEST under the experimental conditions used. Further studies, including functional assays and structural analyses, may be required to elucidate the potential impact of these variants on PSTPIP1-associated signaling pathways.