Mechanisms of Antiproliferative Effect of Streptococcal Arginine Deiminase on Jurkat Lymphoblastic Leukemia Cells

• Published in: Journal of evolutionary biochemistry and physiology Vol. 59; no. 5; pp. 1622 - 1632
• Main Authors: Starikova, E. A., Mammedova, J. T., Ozhiganova, A., Burova, L. A., Kudryavtsev, I. V.
• Format: Journal Article
• Language: English
• Published: Moscow Pleiades Publishing 01-09-2023; Springer Nature B.V
• Subjects: Animal Physiology; Arginine; Arginine deiminase; Autophagy; Biochemistry; Biomedical and Life Sciences; Cancer therapies; Cell cycle; Cell proliferation; Cell viability; Evolutionary Biology; Experimental Papers; Flow cytometry; Leukemia; Life Sciences; Lymphatic leukemia; Streptococcus pyogenes; streptococcal arginine deiminase; Jurkat cells; autophagy; proliferation; cell cycle
• ISSN: 0022-0930; 1608-3202
• DOI: 10.1134/S0022093023050137

Arginine deprivation strategy is considered as a promising trend in cancer therapy. The aim of the study was to investigate the influence of streptococcal arginine deiminase on Jurkat lymphoblastic leukemia cells. The effects of destroyed (sonicated) streptococcal cell supernatants derived from the parental arginine deiminase-expressing strain (
S. pyogenes
M49-16) and its isogenic mutant with the inactivated arginine deiminase gene
arcA
(
S. pyogenes
M49-16del
ArcA
) were compared. Cell proliferation was evaluated using an MTT assay. The other parameters were examined via flow cytometry. The cell distribution across cell cycle phases was studied using a DAPI dye and anti-cyclin A2 antibody. Autophagy intensity was assessed using the LysoTracker™ Green DND-26 reagent. To investigate cell viability, DAPI staining was performed. Streptococcal arginine deiminase suppressed the proliferative activity of Jurkat lymphoblastic leukemia cells, increased the proportion of cells in the resting G
0
/G
1
phases, reduced it in the synthesis S/G
2
phases, as well as enhanced autophagy, without compromising cell viability. Arginine supplementation leveled the effects of the enzyme. The obtained results open up the possibility of using arginine-hydrolyzing activity of the streptococcal arginine deiminase in combination cancer therapy.