Mouse lymphosarcomas sensitive and resistant to cyclophosphamide therapy: activity of cathepsins B, L, and D during various schemes of treatment with cyclophosphamide and SE-glycan.

We measured activities of cysteine (cathepsins B and L) and aspartyl proteinases (cathepsin D) in tumor tissue of mice with sensitive and resistant lymphosarcomas. In cyclophosphamide-resistant lymphosarcoma tissue activities of cathepsins B, L, and D were lower than in cyclophosphamide-sensitive lymphosarcoma. After treatment with cyclophosphamide in high doses enzyme activities in mice with cyclophosphamide-resistant lymphosarcoma increased more significantly than in animals with cyclophosphamide-sensitive lymphosarcoma.

[Immunoenzyme technique for analysis of cystatin C in serum of patients with hemoblastosis].

Cystatin C is a low-molecular endogenous inhibitor of cysteic proteinases. Sets for immune-enzyme assay of cystatin C in human blood serum (KRKK, Slovenia) were made used of in the case study. The concentration of cystatin C (CCC) in blood serum was found to be higher in cases of certain hemoblastoses (Non-Hodgkin's disease, lymphogranulomatosis and multiple myeloma), with the highest concentration of the inhibitor being observed in patients with resistance to the conducted polychemotherapy and a poor prognostication.

Cystatin C and cysteine proteinases during the development and therapy of Lewis lung adenocarcinoma in mice.

We measured plasma cystatin C concentration and activity of cathepsins B and L in tumor tissue as possible markers for the efficiency of antitumor therapy and prognostic criteria for Lewis lung adenocarcinoma in mice. Plasma cystatin C concentration markedly decreased in mice with tumors. During successive therapy the increase in plasma cystatin C concentration correlated with the degree of inhibition of tumor growth.