Carnitine palmitoyltransferase 1A facilitates the senescence of human dental pulp stem cells by Parkin succinylation-mediated mitophagy

Figure 5 Carnitine palmitoyltransferase 1A is the succinyltransferase for Parkin and promotes its degradation. A and B: Dental pulp stem cells (DPSCs) were transfected with shNC and shCPT1A, and the succinylation levels of PINK1 and Parkin were measured using immunoprecipitation (IP) with anti-succinyllysine and immunoblotting with anti-PINK1 and anti-Parkin; C: The interaction between CPT1A and Parkin proteins was evaluated in HEK293T cells using co-IP; D: Potential succinylation sites in Parkin were predicted using the GPSuc database; E and F: After wild type or K27R Parkin plasmids were transfected into HEK293T cells, immunoblotting was performed to measure Parkin protein levels, and Parkin succinylation levels were detected by IP using anti-succinyllysine and immunoblotting using anti-Parkin; G and H: DPSCs were transfected with shNC or shCPT1A and then treated with cycloheximide for 0, 8, 16, and 24 hours, and Parkin protein levels were detected using immunoblotting. n = 3/group; P < 0.001 indicates statistically significant differences. CPT1A: Carnitine palmitoyltransferase 1A; WT: Wild type.