Annexin A1
Annexin A1 (ANXA1), also known as lipocortin I, is a protein encoded by the ANXA1 gene in humans. It is part of the annexin family of proteins, which are characterized by their ability to bind phospholipids in a calcium-dependent manner.
Function[edit | edit source]
Annexin A1 has several important functions within the body. It is involved in the regulation of inflammatory responses and immune cell migration. It also plays a role in the apoptotic process, helping to mediate the removal of dying cells.
Structure[edit | edit source]
The structure of Annexin A1 is characterized by a core domain consisting of four alpha-helices and a variable amino-terminal domain. The core domain is responsible for the protein's ability to bind to phospholipids in a calcium-dependent manner, while the amino-terminal domain is thought to be involved in regulating the protein's function.
Clinical significance[edit | edit source]
Alterations in the expression of Annexin A1 have been associated with a variety of diseases, including cancer, autoimmune diseases, and inflammatory diseases. For example, overexpression of Annexin A1 has been observed in several types of cancer, including breast cancer, prostate cancer, and lung cancer. In contrast, reduced expression of Annexin A1 has been associated with autoimmune diseases such as rheumatoid arthritis and systemic lupus erythematosus.
Research[edit | edit source]
Research into Annexin A1 is ongoing, with scientists seeking to better understand its functions and potential role in disease. This research could potentially lead to the development of new therapeutic strategies for treating diseases associated with alterations in Annexin A1 expression.
See also[edit | edit source]
References[edit | edit source]
Annexin A1 Resources | |
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Annexin+A1 at the US National Library of Medicine Medical Subject Headings (MeSH)
Human ANXA1 genome location and ANXA1 gene details page in the UCSC Genome Browser. Overview of all the structural information available in the PDB for UniProt: P04083 (Annexin A1) at the PDBe-KB.
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