Kim H J, Hiroi Y, Natori Y
J Biochem. 1976 Apr;79(4):803-8. doi: 10.1093/oxfordjournals.jbchem.a131133.
Administration of excess vitamin A to rats induces labilization of liver lysosomal membranes, as shown by the release of lysosomal cathepsins upon tissue homogenization. The effect of lysosomal labilization on liver protein turnover was investigated. The apparent turnover rate of liver proteins in the hypervitaminotic animals, as measured by a double isotope-labeling technique (Glass and Doyle (1972) J, Biol. Chem, 247, 5234-5242), was found to be the same as that in control animals. Neutral and alkaline fructose-1, 6-biphosphatase [EC 3.3.3.11] activities in the liver were also found to be unchanged in hypervitaminosis A. These data indicate that the rate of intracellular protein degradation is not determined by the level of "free cathepsins. Protein synthesis in the livers of the hypervitaminotic animals was partially imparied, as shown by the shift of polysomal profiles toward lighter aggregates.
给大鼠过量服用维生素A会导致肝溶酶体膜不稳定，这可通过组织匀浆后溶酶体组织蛋白酶的释放得以证明。研究了溶酶体不稳定对肝脏蛋白质周转的影响。通过双同位素标记技术（Glass和Doyle（1972年）《生物化学杂志》，247卷，5234 - 5242页）测定，发现维生素A过多症动物肝脏蛋白质的表观周转率与对照动物相同。还发现维生素A过多症时肝脏中的中性和碱性果糖 - 1,6 - 二磷酸酶[EC 3.3.3.11]活性未发生变化。这些数据表明细胞内蛋白质降解速率并非由“游离组织蛋白酶”水平决定。如多核糖体图谱向较轻聚集体的转移所示，维生素A过多症动物肝脏中的蛋白质合成部分受损。
