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Gang Shao et al (2019) Advancements of Annexin A1 in inflammation and tumorigenesis. OncoTargets and Therapy 12 3245 PMID: 31118675
Annexin A1 (2-12) is derived from the Annexin A1 protein which is a member of the Ca2+ dependent phospholipid binding protein family of Annexins A1 to A13. Structurally Annexin is comprised of a C-terminal core region and an N-terminal region. Calcium binding sites featured in the core region allow Annexin A1 to bind to cell membranes to induce membrane aggregation in a calcium dependent manner. Furthermore Annexin A1’s N-terminal region performs extracellular signalling through forming complexes with SH2 domain containing proteins. Different lengths of the Annexin family’s N-terminus contributes to how the Annexins effect key processes such as cell proliferation, apoptosis, growth and differentiation.
Annexin A1 can be categorised as being both anti-inflammatory and pro-inflammatory. One example of how Annexin A1 demonstrates anti-inflammatory properties is through activating the formyl peptide receptor family’s (FGRs) downstream cascade. Consequently the extracellular regulated kinase (ERK) and mitogen-activated protein kinase (MAPK) are phosphorylated, causing subsequent transcription factors involved in the regulation of T cells to generate anti-inflammatory effects. Another is through inhibiting phospholipase A2 which prevents the release of inflammatory factors and the formation of arachidonic acid precursors. This property has contributed inflammation studies such as where the inhibition of pro-inflammatory prostaglandins by Annexin A1 was used to investigate leukocyte aggregation.
During its anti-inflammatory role Annexin A1 uses the active peptide Ac2-26 located on its N-terminus. It is evident Annexin A1 can be labelled as being pro-inflammatory due to it inducing pro-inflammatory cytokines, following its phosphorylation by PKC. This results in its translocation into the nucleus of BV-2 microglial cells.
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