Malinovskaia V V, Pokidysheva L N, Balakireva N N
Vopr Virusol. 1980 May-Jun(3):298-303.
The activity (free and total) of cathepsin D and acid phosphatase was studied in cells of peritoneal exudate of mice of different ages in the process of interferon production in the presence of sera from newborn and adult animals. Cathepsin D release in newborn mice upon interferon induction is actively stimulated by serum factors of newborn animals altering lysosome permeability selectively for this enzyme alone. Another lysosomal enzyme, acid phosphatase, was more strongly bound to the structures and showed no such features. With an increased age of the donor the amount of stimulating factors in the serum decreases and that of inhibiting factors increases. Inhibition of cathepsin release from lysosomes by the serum factor of adult animals protects the synthesized interferon molecules from degradation and facilitates intensive interferon production in adult mice. A higher susceptibility of children to virus infections and inefficiency of the earliest defence system, interferon, may be due to degradation of newly synthesized interferon molecules by lysosomal cathepsin D.
在新生动物和成年动物血清存在的情况下，研究了不同年龄小鼠腹腔渗出液细胞在产生干扰素过程中组织蛋白酶D和酸性磷酸酶的活性（游离和总活性）。新生小鼠在干扰素诱导下组织蛋白酶D的释放受到新生动物血清因子的积极刺激，这些血清因子仅选择性地改变该酶的溶酶体通透性。另一种溶酶体酶酸性磷酸酶与结构结合更紧密，没有显示出这样的特征。随着供体年龄的增加，血清中刺激因子的量减少，抑制因子的量增加。成年动物的血清因子对溶酶体组织蛋白酶释放的抑制作用可保护合成的干扰素分子不被降解，并促进成年小鼠大量产生干扰素。儿童对病毒感染的易感性较高以及最早的防御系统干扰素效率低下，可能是由于溶酶体组织蛋白酶D对新合成的干扰素分子的降解所致。
