Immunophilins

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Immunophilins

Immunophilins (pronounced: im·​mu·​no·​phil·​ins) are a family of proteins that play a role in immunity and cellular signaling. The term "immunophilin" is derived from the words "immune" (referring to the immune system) and "philin" (from the Greek "philos", meaning "loving"), indicating these proteins' affinity for certain immunosuppressive drugs.

Function

Immunophilins are known to bind to immunosuppressants, specifically cyclosporin A, tacrolimus, and sirolimus. They have peptidyl-prolyl isomerase activity, which aids in protein folding. This function is crucial in the regulation of intracellular signaling pathways.

Classification

Immunophilins are classified into two main families: FK506-binding proteins (FKBPs) and cyclophilins (CyPs). Both families are ubiquitous and found in all types of cells and tissues.

FK506-binding proteins

FK506-binding proteins (FKBPs) are named for their ability to bind to the immunosuppressant drug tacrolimus, also known as FK506. They are involved in various cellular processes, including protein folding and trafficking, and the regulation of signal transduction pathways.

Cyclophilins

Cyclophilins (CyPs) are named for their ability to bind to the immunosuppressant drug cyclosporin A. They are involved in protein folding, cellular signaling, and the immune response.

Clinical significance

Immunophilins have been implicated in a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune diseases. They are also the target of several immunosuppressive drugs used in organ transplantation.

See also

References

External links

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