Peptidyl-prolyl Isomerases in Human Pathologies

Peptidyl-prolyl isomerases (PPIases) are a group of evolutionarily conserved ubiquitous proteins expressed both in prokaryotic and eukaryotic cells. PPIases function as accelerating agents, speeding up the cis/trans conformational switch of specific substrates. Based on the affinity to immunosuppressive drugs cyclosporin A (CsA) and FK506, they are classified into three different structurally and functionally classes: the CsA-binding cyclophilins, the FK506-binding proteins (FKBPs) and the Parvulin-like PPIases, which do not bind immunosuppressant. The PPIase-catalyzed isomerization can serve as signal to other key proteins in different cellular process such as the folding of newly synthesised proteins, immune-response, stress-response, neuronal differentiation and cell cycle control, thus is an important regulatory mechanism in human physiology and pathology. Several studies reported the involvement of PPIases in virion and parasite infection, aging, vascular disease, Alzheimer’s disease and many types of cancer. On this background, the PPIases have been explored as potential diagnostic and therapeutic targets.

The purpose of this Research Topic is to bring together experts in the field of PPIases to generate a discussion regarding the mechanism of pathogenesis, the current status and innovative therapeutic strategies in oncology. High-quality manuscripts describing original research, methods, opinion, perspective and reviews are welcome.