Objective:Given the indispensable role played by medical ethics committees in protecting the rights and interests of subjects and researchers, such committees in China are found with weak organizational capacity. This study was designed to analyze the driving factors to improve their organizational capacity.Methods:Form July to September 2020, a survey and interview of 71 tertiary A hospitals in eastern China were conducd, and a total 60 valid samples were obtained. Through crisp-se qualitative comparative analysis(csQCA), the medical ethics committees of 60 tertiary hospitals were analyzed, and the factors affecting the organizational capabilities of the medical ethics committees and their combinations were explored.Results:Protection of rights and interests was key to medical ethics committee′s organizational capacity, while incompetency of the members and the irregular review process were sufficient reasons for the weak organizational capacity. There were six combinations of sufficient conditions for the medical ethics committee to be strong in organizational capacities, which could be explained by the three models of member capacity-orientation, system-process-orientation, and resource-system-orientation.Conclusions:The medical ethics committees are recommended to enhance members capacity, enhance team building; complete rules and regulations, and process mechanism; clarify organization structure, and optimize resource matching, in an effort to enhance the organizational capacity of these committees in China.

The structure of N-glycans on specific proteins can regulate innate and adaptive immunity via sensing environmental signals. Meanwhile, the structural diversity of N-glycans poses analytical challenges that limit the exploration of specific glycosylation functions. In this work, we used THP-1-derived macrophages as examples to show the vast potential of a N-glycan structural interpretation tool StrucGP in N-glycoproteomic analysis. The intact glycopeptides of macrophages were enriched and analyzed using mass spectrometry (MS)-based glycoproteomic approaches, followed by the large-scale mapping of site-specific glycan structures via StrucGP. Results revealed that bisected GlcNAc, core fucosylated, and sialylated glycans (e.g., HexNAc₄Hex₅Fuc₁Neu5Ac₁, N₄H₅F₁S₁) were increased in M1 and M2 macrophages, especially in the latter. The findings indicated that these structures may be closely related to macrophage polarization. In addition, a high level of glycosylated PD-L1 was observed in M1 macrophages, and the LacNAc moiety was detected at Asn-192 and Asn-200 of PD-L1, and Asn-200 contained Lewis epitopes. The precision structural interpretation of site-specific glycans and subsequent intervention of target glycoproteins and related glycosyltransferases are of great value for the development of new diagnostic and therapeutic approaches for different diseases.
Humans ; B7-H1 Antigen ; Glycosylation ; Polysaccharides/metabolism*