Tissue factor derived β-hairpin peptides that bind and inhibit FVII activity.

The formation of the Tissue Factor(TF):Factor VII(FVII) complex is a pivotal event that initiates coagulation; targeting this early step allows for the prevention of the subsequent cascade amplification driven by positive feedback loops. For this reason, the TF:FVII complex is attracting increasing interest as a potential therapeutic target for regulating the coagulation cascade in a specific and timely manner. In order to generate TF-mimics capable of inhibiting this protein-protein interaction, we have designed four small cyclic peptides that simulate a TF region containing the two antiparallel β-strands: 106-110 (RVFSY) and 123-128 (EPLYEN).

Intron retention in PI-PLC γ1 mRNA as a key mechanism affecting MMP expression in human primary fibroblast-like synovial cells.

The intron retention (IR) is a phenomenon utilized by cells to allow diverse fates at the same mRNA, leading to a different pattern of synthesis of the same protein. In this study, we analyzed the modulation of phosphoinositide-specific phospholipase C (PI-PLC) enzymes by Harpagophytum procumbens extract (HPE) in synoviocytes from joins of osteoarthritis (OA) patients. In some samples, the PI-PLC γ1 isoform mature mRNA showed the IR and, in these synoviocytes, the HPE treatment increased the phenomenon.