Publications by authors named "Martin Buchold"

Ethyl pyruvate, a known ROS scavenger and anti-inflammatory drug was found to combat leukemia cells. Tumor cell killing was achieved by concerted action of necrosis/apoptosis induction, ATP depletion, and inhibition of glycolytic and para-glycolytic enzymes. Ethyl lactate was less harmful to leukemia cells but was found to arrest cell cycle in the G0/G1 phase.

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Targets that could improve the treatment of brain tumors remain important to define. This study of a transformation-associated isoform of alpha2-macroglobulin (A2M*) and its interaction with the low-density lipoprotein receptor-related protein-1 (LRP1) suggests a new mechanism for abrogating the malignant potential of astrocytoma cells. LRP1 bound A2M* found to be associated with an inhibition of tumor cell proliferation, migration, invasion, spheroid formation, and anchorage-independent growth.

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Article Synopsis
  • Glyoxalases (Glo1 and Glo2) play a crucial role in detoxifying methylglyoxal (MGO) during glycolysis, and their inhibitors, including certain polyphenols like curcumin, are being studied for potential anti-inflammatory and anti-cancer effects.
  • Curcumin was found to be a strong inhibitor of Glo1 compared to other polyphenols, showing a significant impact on pro-inflammatory cytokine production and reducing tumor cell growth while sparing healthy liver cells.
  • The study suggests that curcumin's inhibition of Glo1 may lead to increased levels of harmful MGO and reduced glutathione (GSH), potentially altering various metabolic pathways in cells.
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Esters of alpha-oxo-carbonic acids such as ethyl pyruvate (EP) have been demonstrated to exert inhibitory effects on the production of anti-inflammatory cytokines. So far, there is no information about effects, if any, of ethyl lactate (EL), an obviously inactive analogue of EP, on inflammatory immune responses. In the present study, we provide evidence that the anti-inflammatory action of alpha-oxo-carbonic acid esters is mediated by inhibition of glyoxalases (Glo), cytosolic enzymes that catalyse the conversion of alpha-oxo-aldehydes such as methylglyoxal (MGO) into the corresponding alpha-hydroxy acids using glutathione as a cofactor.

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