HspBP1 in Complex with the Peptide of the Innate Immunity Protein Tag7 is Able to Lyse Tumor Cells Carrying TNFR1 Receptor.

Autor: Romanova EA; Institute of Gene Biology, Russian Academy of Sciences, Moscow, Russia., Yurkina DM; Institute of Gene Biology, Russian Academy of Sciences, Moscow, Russia., Yashin DV; Institute of Gene Biology, Russian Academy of Sciences, Moscow, Russia. yashin_co@mail.ru., Sashchenko LP; Institute of Gene Biology, Russian Academy of Sciences, Moscow, Russia., Georgiev GP; Institute of Gene Biology, Russian Academy of Sciences, Moscow, Russia.
Jazyk: angličtina
Zdroj: Doklady. Biochemistry and biophysics [Dokl Biochem Biophys] 2024 Apr; Vol. 515 (1), pp. 36-40. Date of Electronic Publication: 2024 Jan 08.
DOI: 10.1134/S1607672923700631
Abstrakt: The search for new cytotoxic agents capable of lysing tumor cells is an important task in the fight against cancer. Here we have shown that the HspBP1 protein, the chaperone of the heat shock protein Hsp70, is able to form a complex with the previously discovered peptide (17.1) of the innate immunity protein Tag7. Experiments using thermophoresis demonstrated that the affinity of the Tag7 protein peptide 17.1 to the HspBP1 molecule is 100 times higher than that of the full-sized Tag7 molecule. The addition of the 17.1-HspBP1 complex to tumor cells induces apoptosis and necroptosis in them. The results obtained in this work can be used to develop promising antitumor drugs.
(© 2024. The Author(s).)
Databáze: MEDLINE
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