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Biology subjects

Venka, K.

Publications and source records attributed to Venka, K..

2 recordsLinked to original sources

Cisplatin resistance reversal with treatment of Citric acid in cisplatin-resistant cell lines

Gastric cancer (GC) is a prevalent and aggressive malignancy with significant morbidity and mortality rates, posing a major threat to human health globally. While surgery remains the preferred clinical treatment, chemotherapy continues to be the cornerstone for perioperative care, adjuvant therapy, and palliative treatment for patients with advanced stages of GC. Among the chemotherapeutic agents, cisplatin (DDP) has been widely used for decades as a first-line treatment for various solid tumors. However, its therapeutic efficacy is frequently undermined by the development of resistance, which is attributed to the complex interplay of multiple proteins and signaling pathways involved in the resistance mechanisms. In this study, the issue of cisplatin resistance is addressed by employing citric acid as a treatment in cell lines. The findings demonstrate that citric acid effectively reverses cisplatin resistance, suggesting the potential involvement of a novel DNA damage repair mechanism. These results pave the way for further investigation into innovative therapeutic approaches to enhance the efficacy of cisplatin in treating gastric cancer.

pharmacology and toxicology↗

Identification and Pharmacological Characterization of Multiple Allosteric Binding Sites on the Free Fatty Acid 1 Receptor

Free fatty acid receptor 1 (FFA1 or GPR40), activated by medium- and long-chain fatty acids, amplifies glucose-stimulated insulin secretion, making it a promising target for type 2 diabetes. Radioligand studies revealed distinct binding sites for partial and full agonists, with full agonists showing positive cooperativity. Functional assays demonstrated positive cooperativity between agonists and varying interactions with the endogenous fatty acid DHA. These findings suggest three allosterically linked binding sites on FFA1, with activation influenced by key arginine residues. Potent ligands with strong cooperativity hold significant therapeutic potential.

pharmacology and toxicology↗