ANGPTL3 negatively regulates IL-1β-induced NF-κB activation by inhibiting the IL1R1-associated signaling complex assembly.

Interleukin-1β (IL-1β)-induced signaling is one of the most important pathways in regulating inflammation and immunity. The assembly of the receptor complex, consisting of the ligand IL-1β, the IL-1 receptor (IL-1R) type 1 (IL1R1), and the IL-1R accessory protein (IL1RAP), initiates this signaling. However, how the IL1R1-associated complex is regulated remains elusive.

A rapid analytical method for the quantitative determination of the sugar in acarbose fermentation by infrared spectroscopy and chemometrics.

In this article, a rapid analytical method for the quantitative determination of the glucose and maltose in the industrial acarbose fermentation was established by the combination application of infrared spectroscopy and chemometrics. The spectra of the 398 acarbose samples were collected by a portable infrared fast analyzer and the concentration of the glucose and maltose in the acarbose fermentation solution were determinate by high performance liquid chromatography (HPLC) as the referent database. Four spectral pretreatment methods, first derivative (FD), second derivative (SD), Savitzky-Golay (SG) convolution smoothing and mean center (MC) were employed to eliminate the optical interference from background and other noise information.

USP15 potentiates NF-κB activation by differentially stabilizing TAB2 and TAB3.

Tumor necrosis factor α (TNFα)- and interleukin 1β (IL-1β)-induced nuclear factor-κB (NF-κB) activation play key roles in inflammation, immunity, and cancer development. Here, we identified one of the deubiquitinating enzymes (DUBs), ubiquitin-specific protease 15 (USP15), as a positive regulator in both TNFα- and IL-1β-induced NF-κB activation. Overexpression of USP15 potentiated TNFα- or IL-1β-triggered NF-κB activation and downstream gene transcription, whereas knockdown of USP15 had opposite effects.