Cyclophilins are ubiquitous proteins that have important functions both inside cells and as secreted proteins. Acting as peptidyl-prolyl cis/trans isomerases they control shape transitions of proteins by regulating rotation of an amide bond within a peptide chain. Because the shape of a protein determines its function, cyclophilins exert control over the functions of their client proteins, governing the information flow through cellular networks. A particularly important function is control of the fate of cells that are stressed by exogenous factors such as trauma, infection, radiation, or toxins, and also stresses of endogenous origin such as metabolic dysregulation, misfolded proteins or excessive signals from physiological stimuli. Many viruses rely on cyclophilins supplied by their host to establish an infection and bacteria have been shown to secrete cyclophilins to manipulate the immune response of the host. Emerging data suggest as yet poorly understood roles in the innate immune system indicating potential roles in the tumour microenvironment.
Apart from the clinically documented antiviral activity, inhibitors of cyclophilins have a wide spectrum of potential therapeutic applications where broad physiological damage control is essential. These situations include acute diseases caused by tissue injuries (mechanical or surgical injury, trauma, ischaemia, necrosis, stroke, infection), chronic degenerative and fibrotic diseases (neurodegeneration, myopathies, vision/hearing loss, fibrosis of various organs), and oncology.
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