Calcine

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Calcine
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Calcine is a protein that plays a crucial role in calcium signaling within cells. It is a calcium-binding protein that is involved in various cellular processes, including muscle contraction, neurotransmitter release, and gene expression.

Structure[edit | edit source]

Calcine is composed of two subunits: a catalytic subunit (calcineurin A) and a regulatory subunit (calcineurin B). The catalytic subunit contains the active site of the enzyme, while the regulatory subunit binds calcium ions and is essential for the activation of the enzyme.

Function[edit | edit source]

Calcine functions as a phosphatase, specifically a serine/threonine phosphatase. It dephosphorylates various target proteins, which can alter their activity, localization, or interaction with other proteins. This dephosphorylation is crucial for the regulation of many cellular processes.

Role in Calcium Signaling[edit | edit source]

Calcine is activated by an increase in intracellular calcium levels. When calcium binds to the regulatory subunit, it induces a conformational change that activates the catalytic subunit. This activation allows calcine to dephosphorylate its target proteins, thereby modulating their function in response to changes in calcium levels.

Clinical Significance[edit | edit source]

Calcine has been implicated in various diseases and conditions. For example, it is involved in the immune response, and inhibitors of calcine, such as cyclosporine and tacrolimus, are used as immunosuppressive drugs to prevent organ transplant rejection. Additionally, dysregulation of calcine activity has been linked to neurodegenerative diseases and cardiovascular diseases.

Related Proteins[edit | edit source]

Calcine is part of a larger family of calcium-binding proteins, which includes calmodulin, troponin, and S100 proteins. These proteins share the ability to bind calcium ions and play roles in various cellular processes.

See Also[edit | edit source]

References[edit | edit source]

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Contributors: Prab R. Tumpati, MD