Changes at Presentation in Patients With Early Rheumatoid Arthritis: A 24-Year Study of the Early Undifferentiated Polyarthritis (EUPA) Cohort.

Objective: To analyze changes in baseline characteristics of patients with very early rheumatoid arthritis (RA) over 24 years in the Early Undifferentiated Polyarthritis (EUPA) cohort.

Methods: Consecutive patients with recent-onset polyarthritis fulfilling RA classification criteria recruited in EUPA were assessed at baseline. Three successive periods were defined: (1) prior to the general availability of biologics (1998-2004; 245 patients), (2) prior to the implantation of the 2010 classification criteria (2005-2010; 266 patients), and (3) the most recent decade (2011-2022; 329 patients).

SHP-1 dephosphorylates 3BP2 and potentially downregulates 3BP2-mediated T cell antigen receptor signaling.

Src homology 2 (SH2) domain-containing protein tyrosine phosphatase-1 (SHP-1) is a critical inhibitory regulator in T cell-receptor (TCR) signaling. However, the exact molecular mechanism underlying this is poorly defined, largely because the physiological substrates for SHP-1 in T cells remain elusive. In this study, we showed that adaptor protein 3BP2 serves as a binding protein and a physiological substrate of SHP-1.

PTEN associates with the vault particles in HeLa cells.

PTEN is a tumor suppressor that primarily dephosphorylates phosphatidylinositol 3,4,5-trisphosphate to down-regulate the phosphoinositide 3-kinase/Akt signaling pathway. Although the cellular functions of PTEN as a tumor suppressor have been well characterized, the mechanism by which PTEN activity is modulated by other signal molecules in vivo remains poorly understood. In searching for potential PTEN modulators through protein-protein interaction, we identified the major vault protein (MVP) as a dominant PTEN-binding protein in a yeast two-hybrid screen.