Publications by authors named "L Drobot"

Background: Cell surface plasmin is involved in tumor growth and metastatic dissemination by regulating cancer cells adhesion, migration and invasion. Plasmin-induced cell detachment is accompanied by an increased rate of reactive oxygen species (ROS) generation and cell death. However, cancer cells acquire the ability to develop adaptive mechanisms to resist ROS-mediated apoptosis.

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Article Synopsis
  • Berberine alkaloids, a type of isoquinoline alkaloids, have shown potential in inhibiting breast cancer development, but their exact mechanisms of action remain unclear.
  • These compounds were found to suppress breast cancer cell proliferation, migration, and invasion through various assays, and they induced apoptosis via intrinsic and extrinsic pathways.
  • The results indicated that these alkaloids affect the Wnt/β-catenin signaling pathway and epithelial to mesenchymal transition (EMT), with different effects on breast cancer cell lines, suggesting their potential for breast cancer treatment.
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Effective targeting of metastasis is considered the main problem in cancer therapy. The development of herbal alkaloid Berberine (Ber)-based anticancer drugs is limited due to Ber' low effective concentration, poor membrane permeability, and short plasma half-life. To overcome these limitations, we used Ber noncovalently bound to C fullerene (C).

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C fullerene has received great attention as a candidate for biomedical applications. Due to unique structure and properties, C fullerene nanoparticles are supposed to be useful in drug delivery, photodynamic therapy (PDT) of cancer, and reversion of tumor cells' multidrug resistance. The aim of this study was to elucidate the possible molecular mechanisms involved in photoexcited C fullerene-dependent enhancement of cisplatin toxicity against leukemic cells resistant to cisplatin.

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The EGFR adaptor protein, CIN85, has been shown to promote breast cancer malignancy and hypoxia-inducible factor (HIF) stability. However, the mechanisms underlying cancer promotion remain ill defined. Here we show that CIN85 is a novel binding partner of the main HIF-prolyl hydroxylase, PHD2, but not of PHD1 or PHD3.

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