Calcineurin

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Calcineurin (pronounced: kal-sin-ur-in) is a type of protein phosphatase that plays a crucial role in various biological processes. It is also known as Protein Phosphatase 2B or PP2B.

Etymology

The term "Calcineurin" is derived from the Latin words calcis (lime) and neur (nerve), indicating its role in calcium and nerve cell function.

Function

Calcineurin is a calcium/calmodulin-dependent serine/threonine protein phosphatase. It is involved in various cellular processes, including T-cell activation, neuronal plasticity, cardiac hypertrophy, and apoptosis. It dephosphorylates the Nuclear Factor of Activated T-cells (NFAT), allowing it to translocate to the nucleus and initiate the transcription of genes involved in the immune response.

Structure

Calcineurin is a heterodimeric protein composed of a 61-kDa catalytic subunit (CnA) and a 19-kDa regulatory subunit (CnB). The CnA subunit contains a catalytic domain, a calmodulin-binding domain, and an autoinhibitory domain. The CnB subunit contains four EF-hand motifs, which bind to calcium ions.

Clinical Significance

Calcineurin inhibitors, such as cyclosporine and tacrolimus, are commonly used in organ transplantation to prevent organ rejection. They work by inhibiting the phosphatase activity of calcineurin, thereby suppressing the immune response.

Related Terms

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