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Электронный каталог: Bondarev, N. A. - Methionine Gamma Lyase Fused with S3 Domain VGF Forms Octamers and Adheres to Tumor Cells Via Bin...
Bondarev, N. A. - Methionine Gamma Lyase Fused with S3 Domain VGF Forms Octamers and Adheres to Tumor Cells Via Bin...
Статья
Автор: Bondarev, N. A.
Biochemical and Biophysical Research Communications [Electronic resource]: Methionine Gamma Lyase Fused with S3 Domain VGF Forms Octamers and Adheres to Tumor Cells Via Bin...
б.г.
ISBN отсутствует
Автор: Bondarev, N. A.
Biochemical and Biophysical Research Communications [Electronic resource]: Methionine Gamma Lyase Fused with S3 Domain VGF Forms Octamers and Adheres to Tumor Cells Via Bin...
б.г.
ISBN отсутствует
Статья
Bondarev, N.A.
Methionine Gamma Lyase Fused with S3 Domain VGF Forms Octamers and Adheres to Tumor Cells Via Binding to EGFR / N.A.Bondarev, Yu.L.Ryzhykau, A.I.Kuklin, [et al.] // Biochemical and Biophysical Research Communications [Electronic resource]. – 2024. – Vol. 691. – P. 149319. – URL: https://doi.org/10.1016/j.bbrc.2023.149319. – Bibliogr.: 37.
Methods for targeting enzymes exhibiting anticancer properties, such as methionine γ-lyase (MGL), have not yet been sufficiently developed. Here, we present the data describing the physico-chemical properties and cytotoxic effect of fusion protein MGL-S3 ― MGL from Clostridium sporogenes translationally fused to S3 domain of the viral growth factor of smallpox. MGL-S3 has methioninase activity comparable to native MGL. In solution, MGL-S3 protein primarily forms octamers, whereas native MGL, on the contrary, usually forms tetramers. MGL-S3 binds to the surface of the neuroblastoma SH-SY5Y and epidermoid carcinoma A431 cells and, unlike native MGL, remains there and retains its cytotoxic effect after media removal. In HEK293T cells lacking EGFRs, no adhesion was recorded. Confocal fluorescence microscopy confirms the preferential adhesion of MGL-S3 to tumor cells, while it avoids getting into lysosomes. Both MGL and MGL-S3 arrest cell cycle of SH-SY5Y cells mainly in the G1 phase, while only MGL-S3 retains this ability after washing the cells.
Спец.(статьи,препринты) = С 342 г4 - Биологические исследования с нейтронами
ОИЯИ = ОИЯИ (JINR)2024
Ключевых слов = 20/024
Bondarev, N.A.
Methionine Gamma Lyase Fused with S3 Domain VGF Forms Octamers and Adheres to Tumor Cells Via Binding to EGFR / N.A.Bondarev, Yu.L.Ryzhykau, A.I.Kuklin, [et al.] // Biochemical and Biophysical Research Communications [Electronic resource]. – 2024. – Vol. 691. – P. 149319. – URL: https://doi.org/10.1016/j.bbrc.2023.149319. – Bibliogr.: 37.
Methods for targeting enzymes exhibiting anticancer properties, such as methionine γ-lyase (MGL), have not yet been sufficiently developed. Here, we present the data describing the physico-chemical properties and cytotoxic effect of fusion protein MGL-S3 ― MGL from Clostridium sporogenes translationally fused to S3 domain of the viral growth factor of smallpox. MGL-S3 has methioninase activity comparable to native MGL. In solution, MGL-S3 protein primarily forms octamers, whereas native MGL, on the contrary, usually forms tetramers. MGL-S3 binds to the surface of the neuroblastoma SH-SY5Y and epidermoid carcinoma A431 cells and, unlike native MGL, remains there and retains its cytotoxic effect after media removal. In HEK293T cells lacking EGFRs, no adhesion was recorded. Confocal fluorescence microscopy confirms the preferential adhesion of MGL-S3 to tumor cells, while it avoids getting into lysosomes. Both MGL and MGL-S3 arrest cell cycle of SH-SY5Y cells mainly in the G1 phase, while only MGL-S3 retains this ability after washing the cells.
Спец.(статьи,препринты) = С 342 г4 - Биологические исследования с нейтронами
ОИЯИ = ОИЯИ (JINR)2024
Ключевых слов = 20/024