Weigand K, Schmid M, Villringer A, Birr C, Heinrich P C
Biochemistry. 1982 Nov 23;21(24):6053-9. doi: 10.1021/bi00267a005.
Addition of the chemically synthesized proalbumin hexapeptide in a concentration of 110 micro M to the medium of isolated rat hepatocytes decreased net albumin synthesis by 12%. The synthesis of other secretory proteins was not altered. A weaker inhibitory effect on albumin synthesis was found for a tetrapeptide, a possible degradation product of the proalbumin hexapeptide. For the uptake of the hexa- and tetrapeptide into the cells, bovine serum albumin is required. In a reticulocyte and in a wheat germ cell-free system a propeptide concentration of 600 micro M inhibited albumin synthesis by 50%, whereas total protein synthesis was inhibited by 19% only, and the synthesis of alpha 1-antitrypsin was not inhibited. These results suggest that the synthesis of preproalbumin is regulated by a feedback mechanism with its propeptide as inhibitor.
在分离的大鼠肝细胞培养基中添加浓度为110微摩尔的化学合成前清蛋白六肽，可使净清蛋白合成减少12%。其他分泌蛋白的合成未发生改变。对于一种四肽（前清蛋白六肽的一种可能降解产物），发现其对清蛋白合成的抑制作用较弱。细胞摄取六肽和四肽需要牛血清白蛋白。在网织红细胞和无细胞小麦胚芽系统中，600微摩尔的前肽浓度可使清蛋白合成抑制50%，而总蛋白合成仅被抑制19%，α1-抗胰蛋白酶的合成未受抑制。这些结果表明，前清蛋白原的合成受一种反馈机制调节，以前肽作为抑制剂。
