CT-guided stereotactic surgery for evacuation of hypertensive intracerebral hematoma

During the last 3 years, 46 cases of hypertensive intracerebral hemorrhage were treated by CT-guided stereotactic surgery. Our present report is concerned with the evaluation of this procedure in the treatment of hypertensive intracerebral hematoma, in terms of the rate of aspirated hematoma and follow-up study of patients. It is difficult to draw any definite conclusion about the operative indications. CT-guided stereotactic aspiration, however, can be evaluated as a less invasive and more definitive treatment of intracerebral hematoma in the basal ganglia and thalamus.     

A new apparatus for CT-guided stereotactic surgery

Combining whole-body CT scan with a stereotactic system, the authors have developed and applied clinically an apparatus which readily provides intraoperative CT images, making it possible to confirm the location of the target point and ascertain the intraoperative environment. It takes about 9 s to obtain a CT image. Our purpose is to make stereotactic surgery, a kind of blind surgery, as safe and reliable as a visualized procedure by intraoperative CT scanning. By the method, in which there is very little invasion under local anesthesia, evacuation of deep-seated intracerebral hematomas as well as brain abscesses and also biopsy or brachytherapy of brain tumors in the brain can be done with safety and reliability.     

Evidence of the growth factor in mouse serum infected with Spirometra erinacei plerocercoids

To investigate the action of the growth factor secreted by Spirometra erinacei plerocercoids, various organ weights, body weight and head-body length were measured in Snell normal and dwarf mice after injection with the serum from mice and rats. Serum from mice infected with the plerocercoids caused significant increases in the weights of the liver and spleen, in the same manner as mice infected with the plerocercoids. However, serum from rats infected with plerocercoids did not cause significant changes in these parameters. The growth factor in the serum of mice infected with plerocercoids was stable at -20 degrees C for at least 6 months and easily passed through the peritoneum.     

Assay of thiols and disulfides based on the reversibility of N-ethylmaleimide alkylation of thiols combined with electrolysis

A simple and specific method for analyzing thiols and disulfides on the basis of the reversibility of N-ethylmaleimide (NEM) alkylation of thiols is described. When the adduct of NEM and glutathione (GSH) was electrolyzed at neutral pH, all of the GSH was recovered. When the adduct was exposed to pH 11.0 for 15 min at 30°C before electrolysis, GSH was not detected. The same behavior was observed after protein thiols reacted with NEM. This pH-dependent production of thiol from the adduct was used to assay GSH and oxidized glutathione in yeast cells, to assay sulfhydryl groups and disulfide bonds in authentic proteins, and to protect thiols from oxidation during enzymatic digestion of protein. This method is useful for assay of thiols and disulfides of both small and large molecules and can be used to identify labile thiols in biological samples that are oxidized during extraction procedures.     

Autophagosome formation can be achieved in the absence of Atg18 by expressing engineered PAS-targeted Atg2

The Atg2-Atg18 complex is essential for autophagosome formation in Saccharomyces cerevisiae. In this paper, we show that partial induction of autophagy can proceed in cells expressing engineered variants of Atg2 capable of localizing to the pre-autophagosomal structure (PAS) in the absence of Atg18. Specifically, through the construction of fusion proteins, we show that the fusion to Atg2 of either the phosphatidylinositol 3-phosphate-binding FYVE domain or the core autophagy protein Atg8 allowed limited Atg18-independent recovery of autophagosome formation. These results indicate that effective targeting of Atg2 to the PAS can compensate for loss of Atg18 function in autophagy.     

Assay of thiols and disulfides based on the reversibility of N-ethylmaleimide alkylation of thiols combined with electrolysis.

A simple and specific method for analyzing thiols and disulfides on the basis of the reversibility of N-ethylmaleimide (NEM) alkylation of thiols is described. When the adduct of NEM and glutathione (GSH) was electrolyzed at neutral pH, all of the GSH was recovered. When the adduct was exposed to pH 11.0 for 15 min at 30 degrees C before electrolysis, GSH was not detected. The same behavior was observed after protein thiols reacted with NEM. This pH-dependent production of thiol from the adduct was used to assay GSH and oxidized glutathione in yeast cells, to assay sulfhydryl groups and disulfide bonds in authentic proteins, and to protect thiols from oxidation during enzymatic digestion of protein. This method is useful for assay of thiols and disulfides of both small and large molecules and can be used to identify labile thiols in biological samples that are oxidized during extraction procedures.