ARGINASE ACTIVITY AND EXPRESSION IN THE PERIPHERAL BLOOD CELLS OF PATIENTS WITH THE DIFFERENT FORMS OF LEUKEMIA
Keywords:
Summary. Objective: to study arginase activity/expression in the peripheral blood cells of patients with the different forms of leukemia. Object and methods: arginase activity was measured in the peripheral blood lymphocytic fraction of patients with B-cell chronic lymphoid leukemia (71 patient); different kinds (M1–M5) of acute myeloid leukemia (53 patients); B-cell acute lymphoid leukemia (8 patients); different forms of non-Hodgkin’s lymphoma (30 patients) and 10 donors. Also, there was measured Arg I protein expression in the cellular extracts of the same blood fraction. Results: arginase activity of the B-cell chronic lymphoid leukemia patients’ lymphocytes was found to be significantly highest between all patients been studied. The lowest arginase activity was found in the lymphocytic fraction of the B-cell acute lymphoid leukemia patients. Conclusion: measurement of the arginase activity/expression in the peripheral blood lymphocytic fraction may be proposed as a supplement criterion to specify diagnosis of some forms of leukemia.Abstract
Summary. Objective: to study arginase activity/expression in the peripheral blood cells of patients with the different forms of leukemia. Object and methods: arginase
activity was measured in the peripheral blood lymphocytic fraction of patients with B-cell chronic lymphoid leukemia (71 patient); different kinds (M1–M5) of acute
myeloid leukemia (53 patients); B-cell acute lymphoid
leukemia (8 patients); different forms of non-Hodgkin’s
lymphoma (30 patients) and 10 donors. Also, there was
measured Arg I protein expression in the cellular extracts
of the same blood fraction. Results: arginase activity of the
B-cell chronic lymphoid leukemia patients’ lymphocytes
was found to be significantly highest between all patients
been studied. The lowest arginase activity was found in
the lymphocytic fraction of the B-cell acute lymphoid leukemia patients. Conclusion: measurement of the arginase
activity/expression in the peripheral blood lymphocytic fraction may be proposed as a supplement criterion to
specify diagnosis of some forms of leukemia.
References
Akram J, Mahmoud A, Hamid-Reza R. Rhodanese and arginase activity in normal and cancerous tissues of human breast, esophagus, stomach and lung. Arch Irn Med 2001; 4: 88–92.
Ahmed MM, Said ZS, Montaser SA. Chronic myelogenous leukemia: cytogenetic and biochemical consequences and
applications for diagnosis and judgment. J Cytol Histol 2014; S4:2.doi: DOI: 10.4172/2157–7099: 4–15.
Konarska L, Widzynska I, Zienkiewicz H, Sulek K. Arginase activity alterations in peripheral blood lymphocytes in
the human chronic lymphocytic leukemia. Acta Biochim Polonica 1993; 40 (1): 160–3.
Tipathi AK, Chaturvedi R, Ahmad R, et al. Peripheral blood leukocytes ornіthine decarboxylase activity in chronic
myeloid leukemia patients: prognostic and therapeutic implications. Leukemia Res 2002; 26 (2): 349–54.
Pirnes-Karhu S, Mantymaa P, Sironen R, et al. Enhanced polyamine catabolism disturbs hematopoietic lineage
commitment and leads to a myeloproliferative disease in mice overexpressing spermidine/spermine N¹-acetyltransferase. Amino Acids 2014; 46 (3): 689–700.
Gluzman DF, Sklyarenko LM, Nadgornaya VА. Diagnostics oncohematology. Кyiv, DIA 2011. 256 с.
Corraliza IM, Campo ML, Soler G, Modolell M. Determination of arginase activity in macrophages: a micromethod.
J Immunol Methods 1994; 174 (1–2): 231–5.
Laemmli UK. Cleavage of structural proteins during
the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–5.
Sovak M, Bellas R, Kim D, et al. Aberrant nuclear factor-kB/Rel expression and pathogenesis of breast cancer. J
Clin Invest 1997; 100: 2952–60.
Bradford M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72: 248–54.
Mussai F, De Santo C, Abu-Dayyeh I, et al. Acute myeloid leukemia creates an arginase-dependent immunosuppressive microenvironment. Blood 2013; 122 (5): 749–58.
Mussai F, Egan S, Higginbotham-Jones J, et al. Arginine dependence of acute myeloid leukemia blast proliferation: a novel therapeutic target. Blood 2015; 125 (15): 2386–96.
Orlovsky ОА, Klenov ОО, Bentrad VV, et al. Certain features of polyamine metabolism and pathogenetic functions in the mononuclear cells of the patients with chronic В-lymphocytic leukemia and acute monoblastic leukemia (М5). Clin oncol 2018; 4 (32): 45–51.
Deignan JL, Livesay JC, Shantz LM, Grody WW. Polyamine homeostasis in arginase knockout mice. AJP Cell Physiol 2007; 293 (4): 1296–301.
