[Proteolytic enzymes in human lymphocytic leukemia cells. II. Comparative characteristics of proteolytic enzymes and their inhibitors in three differing types of lymphoid cells].

A comparative study of proteolytic enzymes and their inhibitors in three human leukemic lymphoid cell populations has been carried out. The lysates of all lymphoid cells contained cathepsins D, B, L and H as well as serine trypsin-like proteinases, several aminopeptidases, dipeptidyl aminopeptidase IV and plasminogen activator (urokinase type). The activities of individual proteinases and their ratios in all cell types under study varied essentially, suggesting that lymphoid cells with different functions have different sets of proteolytic enzymes.

[Proteolytic enzymes in human lymphocytic leukemia cells. I. Activity of dipeptidylaminopeptidase IV, plasminogen activator and cathepsins B and L in cells with different immunologic phenotype].

Immunological and biochemical study of lymphoid cells obtained from 20 patients with various forms of lymphoproliferative disorders has been carried out. It was found that different phenotypes of lymphoid cells at various stages of differentiation have different activity levels of dipeptidyl aminopeptidase IV (DAP IV), plasminogen activator (urokinase type) and cathepsins B + L. The highest proteinase activity values were found in the lysates of just those leukemic T-cells whose phenotypes corresponded to the initial stages of thymic differentiation or to activated T-cells.

Dipeptidylpeptidase IV in human leukemic B- and T-cells.

Dipeptidylpeptidase IV (DPP-IV) activity in lymphoid cells of patients with various lymphoproliferative diseases has been assayed. The enzyme activity was detected in lysates of all leukemic T- and B-cells studied. High DPP-IV activity levels (5-7 fold higher than those in mature Th and Ts) were found in T-cells with phenotypes corresponding either to the early thymic stages of maturation, or to activated T-lymphocytes, or to some atypic T-cells.

[Protein kinase activity in lymphoid cells in various forms of lymphoproliferative disorders].

Activities of dipeptidyl-aminopeptidase IV, urokinase-like plasminogen activator, cathepsins B and L were studied in lymphoid cells of patients with various forms of lymphoproliferative disorders. Activity of the enzymes studied was found in all the T- and B-cell, although rate and ratio of the enzymatic activity were dissimilar in various cell types. The highest rate of activity exhibited cells at early stages of maturation obtained from patients with acute lymphoblastic leukemia, while low level of the proteinase activity was detected in cells of patients with chronic lymphoid leukemia, non-Hodgkin lymphoma, hairy cell leukemia and Sezary disease, corresponding to mature T- and B-subpopulations.

Activity of some proteinases and glycosidases in human leukemic lymphoid cells at various stages of differentiation.

Activities of some glycosidases and proteinases in human leukemic lymphoid cells at various stages of differentiation have been compared. It was found that cells with different immunological phenotypes gave different enzymic spectra. Glycosidases and proteinases in lymphoid cell precursors had higher activity level than the enzymes in mature T- and B- cells.