Romero et al.16 reported that the region (225–240 aa) of PD-L1 was the potential surface metalloproteases (ADAM10/17) cleavage site in triple-negative breast cancer, which subsequently generated N-terminal (~24 kDa) fragments that were released outside and C-terminal (~13 kDa) fragments that were degraded by lysosomes, and the activators of ADAM10/17 (ionomycin/PMA) enhanced this event, whereas the mechanism of PD-L1 degradation by lysosomes is still unclear. This evidence concerns the gene CD274 and triple-negative breast carcinoma.