Extracellular signal-regulated kinases, P38 and c-Jun N-terminal kinases phosphorylation changes in PC12 cells with diabetic disturbances and comorbid excitotoxicity - a preliminary report.

This study investigated ERK, p38 and JNK protein kinases phosphorylation changes in diabetic in vitro conditions with accompanying excitotoxicity reflected by high L-glutamate concentrations. An InstantOne ELISA test in cell lysates was performed to evaluate the intensity of phosphorylation of ERK, p38 and JNK occurring as a result of the incubation of undifferentiated PC12 cells with solutions of glucose (G1,G2), insulin (I1,I2) and L-glutamate (L1,L2). We observed increased phosphorylation of JNK (Thr183/Tyr185) and p38 (Thr180/Tyr182) kinases. For both these kinases, we have shown an increase in phosphorylation in case of double combinations for the following reagents: G1I1, G1I2, G2I1, G2I2, G2L1, I2L2 and the triple ones: G1I2L1 and G2I1L2. The research based on the analysis of selected protein kinases under diabetic conditions with accompanying excitotoxicity, represents an important cognitive issue for research on neurodegenerative disorders resulting from long-term type 2 diabetes. The confirmed changes in protein phosphorylation of p38 and JNK kinases suggests changes in the conformation and activity of these proteins under conditions of increased excitotoxicity resulting from diabetes. PMID: 33475090 [PubMed - in process]
Source: Journal of Physiology and Pharmacology - Category: Drugs & Pharmacology Tags: J Physiol Pharmacol Source Type: research