Guasha-induced hepatoprotection in chronic active hepatitis B: a case study

BackgroundHeme oxygenase-1 (HO-1) has demonstrated hepatoprotective effect in animal hepatitis models. HO-1 was also reported to be upregulated with Guasha, an ancient therapeutic technique which applies instrument assisted press-stroking to treat many disorders.MethodsWe report a case on the changes of liver function, plasma HO-1 and T-helper (Th) cytokine balance in a chronic active hepatitis B carrier before and after Guasha. The patient presented with increased activities of liver enzymes (ALT and AST), indicating inflammatory damage in liver before Guasha.ResultsForty-eight hours after receiving Guasha, the patient showed changes in a number of serum markers: a decline of liver enzymes (ALT and AST) indicating reduced chronic inflammation, an elevated plasma HO-1, and a modulation of T-helper (Th)1/Th2 balance.ConclusionsGuasha was shown to transiently reduce the inflammatory markers of liver injury in human, together with an enhancement of HO-1 which might be responsible for the hepatoprotective action.     

Investigation of PEG crystallization in frozen and freeze-dried PEGylated recombinant human growth hormone-sucrose systems: implications on storage stability

The objectives of the current study were to investigate (i) the phase behavior of a PEGylated recombinant human growth hormone (PEG-rhGH, ～60 kDa) during freeze-drying and (ii) its storage stability. The phase transitions during freeze-thawing of an aqueous solution containing PEG-rhGH and sucrose were characterized by differential scanning calorimetry. Finally, PEG-rhGH and sucrose formulations containing low, medium, and high polyethylene glycol (PEG) to sucrose ratios were freeze-dried in dual-chamber syringes and stored at 4°C and 25°C. Chemical decomposition (methionine oxidation and deamidation) and irreversible aggregation were characterized by size-exclusion and ion-exchange chromatography, and tryptic mapping. PEG crystallization was facilitated when it was covalently linked with rhGH. When the solutions were frozen, phase separation into PEG-rich and sucrose-rich phases facilitated PEG crystallization and the freeze-dried cake contained crystalline PEG. Annealing caused PEG crystallization and when coupled with higher drying temperatures, the primary drying time decreased by up to 51%. When the freeze-dried cakes were stored at 4°C, while there was no change in the purity of the PEG-rhGH monomer, deamidation was highest in the formulations with the lowest PEG to sucrose ratio. When stored at 25°C, this composition also showed the most pronounced decrease in monomer purity, the highest level of aggregation, and deamidation. Furthermore, an increase in PEG crystallinity during storage was accompanied by a decrease in PEG-rhGH stability. Interestingly, during storage, there was no change in PEG crystallinity in formulations with medium and high PEG to sucrose ratios. Although PEG crystallization during freeze-drying did not cause protein degradation, crystallization during storage might have influenced protein stability.