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Receptor-interacting protein kinase 1 (RIPK1) plays a crucial role in controlling inflammation and cell death. Its function is tightly controlled through post-translational modifications, enabling its dynamic switch between promoting cell survival and triggering cell death. Phosphorylation of RIPK1 at various sites serves as a critical mechanism for regulating its activity, exerting either activating or inhibitory effects. Perturbations in RIPK1 phosphorylation status have profound implications for the development of severe inflammatory diseases in humans. This review explores the intricate regulation of RIPK1 phosphorylation and dephosphorylation and highlights the potential of targeting RIPK1 phosphorylation as a promising therapeutic strategy for mitigating human diseases. [ABSTRACT FROM AUTHOR]

Mesenchymal stem cells (MSCs) can exhibit either prooncogenic or antitumor properties depending on the context. Based on our previous study, we hypothesized that MSCs engineered to deliver IFN-γ would kill cancer cells through persistent activation of the TRAIL pathway. Human bone-marrow (BM-) derived MSCs were isolated, amplified, and transduced with a lentiviral vector encoding the IFN-γ gene under the control of the EF1α promoter. The IFN-γ-modified MSCs effectively secreted functional IFN-γ, which led to long-term expression of TRAIL. More importantly, the IFN-γ-modified MSCs selectively induced apoptosis in lung tumor cells through caspase-3 activation within the target cells. The percentage of activated-caspase-3-positive tumor cells in IFN-γ-modified MSCs cocultures was significantly higher than in control MSCs cocultures. Treatment with anti-TRAIL antibody dramatically suppressed the caspase-3 activation observed in H460 cells. After injection into nude mice, the IFN-γ-modified MSCs inhibited the growth and progression of lung carcinoma compared with control cells. Collectively, our results provide a new strategy for tumor therapy that utilizes IFN-γ-modified MSCs. [ABSTRACT FROM AUTHOR]

Objective: To prepare the polyclonal antibodies against Golgi protein 73 (GP73) and preliminarily establish the particle-enhanced turbidimetric immunoassay., Methods: New Zealand rabbits were immunized with recombinant GP73 protein to obtain the polyclonal antibodies. The antibodies were purified and covalently attached to latex particles. Under the optimized reaction conditions, the covalent latex-antibody complexes were prepared to establish the GP73 particle-enhanced turbidimetric immunoassay., Results: The titer of purified polyclonal antibodies reached 16 000. The best reaction conditions were that the concentration of EDAC/NHS was 10 mg/mL, the reaction solution was PBS (pH6), reaction time was 3 hours at room temperature. Under such conditions, the coupling efficiency was the highest. The particle-enhanced turbidimetric assay showed a good specificity and sensitivity with a good linear relationship in the range of 6.25-200 ng/mL. The determination limit was 10 ng/mL., Conclusion: The study has successfully purified anti-GP73 antibodies, prepared the covalent latex-antibody complexes and established particle-enhanced turbidimetric immunoassay.