Evaluation of traditional Chinese exercise for knee osteoarthritis (KOA): an overview of systematic reviews.

BACKGROUND: Knee osteoarthritis (KOA) has become a public health issue. Several systematic reviews (SRs) and meta-analyses (MAs) indicate that traditional Chinese exercise (TCE) may be an effective treatment for reducing pain and stiffness and improving physical function in people with knee osteoarthritis (KOA). OBJECTIVES: To evaluate the literature quality and evidence for the systematic reviews of TCE for KOA and provide evidence to support the clinical application of TCE for KOA. METHODS: Eight databases were searched from their inception to January 3, 2023, to retrieve relevant literature, including China National Knowledge Infrastructure (CNKI), Wanfang, Chinese Scientific Journal Database (VIP), China Biology Medical literature database (CBM), PubMed, Embase, Web of Science and Cochrane Library, without restrictions on publication date or language. AMSTAR-2 and PRISMA 2020 assessed the methodological and reporting quality of included SRs/MAs. The Grading of Recommendations Assessment, Development, and Evaluation (GRADE) system was utilized to evaluate the quality of evidence. RESULTS: A total of 18 SRs/MAs were included. The methodological quality was "very low" based on AMSTAR-2. The overall reporting quality was deficient based on PRISMA 2020. The quality of Chinese and English literature differed, with English literature being superior in methodological and reporting quality. Among 93 pieces of evidence obtained, 46 (49.46%) were of very low quality, 34 (36.56%) were of low quality, 13 (13.98%) were of moderate quality, and none were of high quality. TCE was supported by 76 pieces of evidence (81.72%). CONCLUSION: TCE appears beneficial and safe for managing KOA. However, due to the relatively low methodological and evidentiary quality of included SRs/MAs, clinicians should interpret these findings cautiously.

Impact of thermal ultrasound on enzyme inactivation and flavor improvement of sea cucumber hydrolysates.

In this study, the effects of the thermal ultrasonic enzyme inactivation process on flavor enhancement in sea cucumber hydrolysates (SCHs) and its impact on the inactivation of neutral proteases (NPs) were investigated. The body wall of the sea cucumber was enzymatically hydrolyzed with NPs. On the one hand, the structure of NPs subjected to different enzyme inactivation methods was analyzed using ζ-potential, particle size, and Fourier transform infrared (FT-IR) spectroscopy. On the other hand, the microstructure and flavor changes of SCHs were examined through scanning electron microscopy, E-nose, and gas chromatography-ion mobility spectrometry (GC-IMS). The results indicated that thermal ultrasound treatment at 60 °C could greatly affect the structure of NPs, thereby achieving enzyme inactivation. Furthermore, this treatment generated more pleasant flavor compounds, such as pentanal and (E)-2-nonenal. Hence, thermal ultrasound treatment could serve as an alternative process to traditional heat inactivation of enzymes for improving the flavor of SCHs.

Direct Binding of Rap1 to Talin1 and to MRL Proteins Promotes Integrin Activation in CD4+ T Cells.

Agonist-induced Rap1 GTP loading results in integrin activation involved in T cell trafficking and functions. MRL proteins Rap1-interacting adapter molecule (RIAM) and lamellipodin (LPD) are Rap1 effectors that can recruit talin1 to integrins, resulting in integrin activation. Recent work also implicates direct Rap1-talin1 interaction in integrin activation. Here, we analyze in mice the connections between Rap1 and talin1 that support integrin activation in conventional CD4+ T (Tconv) and CD25HiFoxp3+CD4+ regulatory T (Treg) cells. Talin1(R35E, R118E) mutation that disrupts both Rap1 binding sites results in a partial defect in αLß2, α4ß1, and α4ß7 integrin activation in both Tconv and Treg cells with resulting defects in T cell homing. Talin1(R35E,R118E) Tconv manifested reduced capacity to induce colitis in an adoptive transfer mouse model. Loss of RIAM exacerbates the defects in Treg cell function caused by the talin1(R35E,R118E) mutation, and deleting both MRL proteins in combination with talin1(R35E,R118E) phenocopy the complete lack of integrin activation observed in Rap1a/b-null Treg cells. In sum, these data reveal the functionally significant connections between Rap1 and talin1 that enable αLß2, α4ß1, and α4ß7 integrin activation in CD4+ T cells.