Cytotoxic Effect of L-Methioninase from Brevibacterium linens BL2 in Combination with Etoposide against Glioblastoma Cells

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dc.authoridGokturk, Dilek/0000-0002-1195-5828
dc.authoridOzdemir Alkis, Meryem Damla/0000-0002-5728-8004
dc.authoridIPEK, SEMIH LATIF/0000-0002-4661-7765
dc.contributor.authorIpek, Semih Latif
dc.contributor.authorOzdemir, Meryem Damla
dc.contributor.authorGokturk, Dilek
dc.date.accessioned2025-01-06T17:43:31Z
dc.date.available2025-01-06T17:43:31Z
dc.date.issued2023
dc.description.abstractL-methioninase degrades methionine, which is essential in methionine-dependent cancer cells, resulting in specific cell death. Normal cells can synthesize their own methionine amino acids even in the absence of exogenous methionine. This selective targeting of cancer cells makes L-methioninase a promising therapeutic candidate for cancer. In this study, L-methioninase was partially purified from Brevibacterium linens BL2. The specific activity of the enzyme was found as 3.055 units/mg. IC50 values (24 h) of the enzyme were 5.792 units/mL for U87MG cell line and 5.215 units/mL for T98G cell line. When L-methioninase and etoposide were used in combination, synergistic cytotoxic and cell migration inhibition effects on U87MG and T98G cells alongside decreased cytotoxic activity on the Mouse Embryonic Fibroblast and HaCaT cells compared to etoposide alone were observed. Additionally, colony numbers of U87MG cells were significantly reduced by L-methioninase and etoposide administration after 21 days of incubation. Furthermore, L-methioninase suppressed the expression levels of survivin and c-Myc while increasing the expression level of Caspase-3 in both glioblastoma cell lines. These effects were enhanced when etoposide was used in combination with etoposide. This investigation reveals that the L-methioninase enzyme not only exhibited cytotoxic effects on U87MG and T98G cells but also enhanced the anti-proliferative effects of etoposide when used in combination while also demonstrating fewer adverse effects on normal cells.
dc.description.sponsorshipThe authors acknowledge TUBITAK and the ATU Scientific Research Projects unit for their financial assistance in this study. The authors acknowledge that Chr. Hansen Company donated the Brevibacterium linens BL2 strain for this study.; TUBITAK; ATU Scientific Research Projects unit
dc.description.sponsorshipThe authors acknowledge TUBITAK and the ATU Scientific Research Projects unit for their financial assistance in this study. The authors acknowledge that Chr. Hansen Company donated the Brevibacterium linens BL2 strain for this study.
dc.identifier.doi10.3390/app13169382
dc.identifier.issn2076-3417
dc.identifier.issue16
dc.identifier.scopus2-s2.0-85169105488
dc.identifier.scopusqualityQ1
dc.identifier.urihttps://doi.org/10.3390/app13169382
dc.identifier.urihttps://hdl.handle.net/20.500.14669/2679
dc.identifier.volume13
dc.identifier.wosWOS:001055813300001
dc.identifier.wosqualityQ1
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoen
dc.publisherMdpi
dc.relation.ispartofApplied Sciences-Basel
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanı
dc.rightsinfo:eu-repo/semantics/openAccess
dc.snmzKA_20241211
dc.subjectL-methioninase
dc.subjectetoposide
dc.subjectglioblastoma
dc.titleCytotoxic Effect of L-Methioninase from Brevibacterium linens BL2 in Combination with Etoposide against Glioblastoma Cells
dc.typeArticle

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