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1.
Journal of Experimental Hematology ; (6): 636-640, 2022.
Article in Chinese | WPRIM | ID: wpr-928767

ABSTRACT

Hemolytic uremic syndrome (HUS) is clinically rare, with high mortality and case fatality rates. In recent years, the research on HUS has been intensified and the pathophysiological mechanism has been continuously improved. At present, the main mechanism of pathogenesis is the excessive activation of complement alternative pathways mediated by complement-related gene mutations or the existence of antibodies. The treatment methods and strategies are also constantly updated, mainly including complement-blocking drugs such as Eculizumab, Lavalizumab, and Ravulizumab. In this review, the new developments in the pathogenesis and treatment of HUS is summarized, and provide references for the clinical treatment of HUS.


Subject(s)
Humans , Complement System Proteins/therapeutic use , Hemolytic-Uremic Syndrome/therapy , Mutation
2.
International Eye Science ; (12): 1085-1089, 2005.
Article in Chinese | WPRIM | ID: wpr-641786

ABSTRACT

AIM: To explore whether carnosine can protect α -crys-tallin modification and decreased chaperone by a steroid,and whether carnosine could directly react with a steroid.METHODS: Bovine lens α L-crystallin was separated by size-exclusion chromatography on a Sephacyl S-300 HR column. α L-Crystallin was incubated with different concentrations of prednisolone-21-hemisuccinate (P-21-H)with or without carnosine for different times. The chaperone activity of α L-crystallin was monitored using the prevention thermal aggregation of α L-crystallin. The modified α L-crystallinwas examined by SDS-PAGE and fluorescence measurements. The absorbance spectra of solutions of carnosine and P-21-H were investigated.RESULTS: P-21-H decreased the chaperone activity ofα L-crystallin in a concentration- and time-dependent fashion. Carnosine only worsened this effect. The tryptophan fluorescence intensity of α L-crystallin modified by P-21-H was significantly decreased compared to unmodified crystallin, whereas its non-tryptophan fluorescence was increased with a shift to longer wavelengths in a time- and dose-dependent manner, suggesting that new fluorophores are possibly formed. Carnosine readily reacted with P-21-H thereby inhibiting steroid-mediated protein modification as revealed electrophoretically. The increased absorbance was time-dependent, suggesting adducts may be formed between carnosine and P-21-H.CONCLUSION: Carnosine reacts with P-21-H, which suggests carnosine's potential as a possible anti-seroid agent.

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