Burditt L J, Ratcliffe A, Fryer P R, Hardingham T E
Biochim Biophys Acta. 1985 Feb 21;844(2):247-55. doi: 10.1016/0167-4889(85)90097-7.
Pig laryngeal chondrocytes incubated in the presence of monensin showed inhibition of [35S]sulphate incorporation and decreased secretion of proteoglycan into the culture medium, but no large decrease in protein synthesis. This lead to the intracellular accumulation of proteoglycan protein core, which was detected in immunoprecipitates of cell extracts. Using the same antiserum protein core was localised by electron microscopy with protein A-coated gold. In control chondrocytes, it was detected only in elements of the Golgi and in secretory vesicles, but following monensin treatment labelling was more intense in the Golgi and extended into the distended cisternae of the rough endoplasmic reticulum. The results suggest that monensin blocks proteoglycan protein core translocation between different elements of the Golgi and that this occurs prior to the major site of chondroitin sulphate synthesis on proteoglycan.
在莫能菌素存在的情况下培养的猪喉软骨细胞显示出[35S]硫酸盐掺入受到抑制，蛋白聚糖分泌到培养基中的量减少，但蛋白质合成没有大幅下降。这导致蛋白聚糖蛋白核心在细胞内积累，在细胞提取物的免疫沉淀物中可检测到。使用相同的抗血清，通过蛋白A包被的金进行电子显微镜定位蛋白核心。在对照软骨细胞中，仅在高尔基体成分和分泌小泡中检测到，但在莫能菌素处理后，高尔基体中的标记更强，并延伸到粗面内质网扩张的潴泡中。结果表明，莫能菌素阻断了蛋白聚糖蛋白核心在高尔基体不同成分之间的转运，且这种转运发生在蛋白聚糖硫酸软骨素合成的主要位点之前。
