Management and Use of Protein Anabolic Preparation and Peptide Hormone in Our Hospital / 中国药房

OBJECTIVE: To study the status quo of the use of protein anabolic preparation and peptide hormone in our hospital and to strengthen the standardized management on drug use.METHODS: The protein anabolic preparation and peptide hormone used during Jan 2004～Dec 2007 in our hospital were analyzed statistically in respect of the consumption sum and the drug variety.RESULTS: The protein anabolic preparation totaled 4 kinds and peptide hormone 3 kinds.The consumption sum of protein anabolic preparation plus peptide hormone accounted for about 1% of the total,of which,peptide hormone took a higher proportion.CONCLUSIONS: Both the variety and consumption sum were on the lower side for protein anabolic preparation and peptide hormone used in our hospital,the management of which was standard on the whole;however,there are some defects and the management on the use of those drugs should be intensified.

THE DISTRIBUTON CHARACTERISTIC OF FIVE PEPTIDE HORMONES IN THE ENDOCRINE CELLS IN DIGESTIVE TRACT OF MONOPTERUS ALBUS / 解剖学报

Objective To investigate the localization and distribution of the five endocrine cells in the digestive tract mucosa of ricefield eel(Monopterus albus). Methods Using immunocytochemical technique of strept avidin-biotin-peroxidase complex(SABC) were used. Results At least 5 kinds of immunoreactive endocrine cells distributed in the digestive tract mucosa of M.albus. They were gastrin(Gas),somatostatin(Som),5-hydroxytryptamine(5-HT),insulin(Ins),and neurofilament (NF) immunoreactive endocrine(IRE) cells.Gas and Som-IRE cells distributed between stratified squamous epithelium and goblet cell in esophagus. A large number of Gas-IRE cells were found between gastric fundus epithelium and gastric glands, and only a few in the carcia. Ins, 5-HT and NF-IRE cells distributed in the epithelium pylorus and pyloric glandular tube respectively. No any immunoreactive positive reaction was found in the gut of M.albus.In addition, immunoreactive positive reaction of glucagons was not found in whole digestive tract.All immunoreactive endocrine cells were dark brown in color.Their morphology was irregular, cytoplasmic process was shorter and thicker, their nucleus showed an empty bubble.They distributed between esophageal epithelium and gastric epithelium or glandular epithelium, and cytoplasmic process extended to the gastric lumen and glandular cavity.Conclusion There is a complex endocrine function of the digestive system in ricefield eel (M.albus) at the lowest vertebrate.

Intracellular trafficking and metabolic turnover of yeast prepro-alpha-factor-SRIF precursors in GH3 cells

Chimeric genes coding for prepro region of yeast alpha-factor and anglerfish SRIF were expressed in rat GH3 cells to determine whether yeast signals could regulate hormone processing in mammalian cells. We report that nascent hybrid polypeptides were efficiently targeted to ER, where cleavage of signal peptides and core glycosylation occurred, and were localized mainly in Golgi. These data indicate that prepro region of yeast alpha-factor functions in sorting molecules to secretory pathway in mammalian cells. A hybrid construct with a mutated signal peptide underwent similar ER translocation, whereas such a mutation resulted in defective translocation in yeast (Cheong et al., 1997). This difference may be due to the differences in ER translocation between yeast and mammalian cells, i.e., posttranslational versus cotranslational translocation. Processing and secretion of metabolically labeled hybrid propeptides to mature SRIF peptides were assessed by HPLC. When pulse-labeled cells were chased for up to 2 h, intracellular propeptides disappeared with a half-life of approximately 25 min, showing that -68% of initially synthesized propeptides were secreted constitutively. About 22% of SRIF-related products were proteolytically processed to mature SRIF, of which 38.7% were stored intracellularly with a half-life of - 2 h. In addition, immunocytochemical localization showed that a small proportion of SRIF molecules accumulated in secretory vesicles. All these results suggest that yeast prepropeptide could direct hybrid precursors to translocate into ER lumen and transit through secretory pathway to the distal elements of Golgi compartment, but could process and target it less efficiently to downstream in rat endocrine cells.

Intracellular trafficking and metabolic turnover of yeast prepro-alpha-factor-SRIF precursors in GH3 cells

Chimeric genes coding for prepro region of yeast alpha-factor and anglerfish SRIF were expressed in rat GH3 cells to determine whether yeast signals could regulate hormone processing in mammalian cells. We report that nascent hybrid polypeptides were efficiently targeted to ER, where cleavage of signal peptides and core glycosylation occurred, and were localized mainly in Golgi. These data indicate that prepro region of yeast alpha-factor functions in sorting molecules to secretory pathway in mammalian cells. A hybrid construct with a mutated signal peptide underwent similar ER translocation, whereas such a mutation resulted in defective translocation in yeast (Cheong et al., 1997). This difference may be due to the differences in ER translocation between yeast and mammalian cells, i.e., posttranslational versus cotranslational translocation. Processing and secretion of metabolically labeled hybrid propeptides to mature SRIF peptides were assessed by HPLC. When pulse-labeled cells were chased for up to 2 h, intracellular propeptides disappeared with a half-life of approximately 25 min, showing that -68% of initially synthesized propeptides were secreted constitutively. About 22% of SRIF-related products were proteolytically processed to mature SRIF, of which 38.7% were stored intracellularly with a half-life of - 2 h. In addition, immunocytochemical localization showed that a small proportion of SRIF molecules accumulated in secretory vesicles. All these results suggest that yeast prepropeptide could direct hybrid precursors to translocate into ER lumen and transit through secretory pathway to the distal elements of Golgi compartment, but could process and target it less efficiently to downstream in rat endocrine cells.