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Recombinant arginine‐degrading enzymes in metabolic anticancer therapy and bioanalytics
Author(s) -
Stasyk Oleh V.,
Boretsky Yuriy R.,
Gonchar Mykhailo V.,
Sibirny Andriy A.
Publication year - 2015
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1002/cbin.10383
Subject(s) - arginine deiminase , arginine , arginase , amino acid , enzyme , biochemistry , biology , chemistry
Abstract Tumor cells often exhibit specific metabolic defects due to the aberrations in oncogene‐dependent regulatory and/or signaling pathways that distinguish them from normal cells. Among others, many malignant cells are deficient in biosynthesis of certain amino acids and concomitantly exhibit elevated sensitivity to deprivation of these amino acids. Although the underlying causes of such metabolic changes are still not fully understood, this feature of malignant cells is exploited in metabolic enzymotherapies based on single amino acid, e.g., arginine, deprivation. To achieve efficient arginine depletion in vivo, two recombinant enzymes, bacterial arginine deiminase and human arginase I have been evaluated and are undergoing further development. This review is aimed to summarize the current knowledge on the application of arginine‐degrading enzymes as anticancer agents and as bioanalytical tools for arginine assays. The problems that have to be solved to optimize this therapy for clinical application are discussed.