title: Annexin A1 localization and its relevance to cancer.
abstract: Annexin A1 (ANXA1) is a Ca(2+)-regulated phospholipid-binding protein involved in various cell processes. ANXA1 was initially widely studied in inflammation resolution, but its overexpression was later reported in a large number of cancers. Further in-depth investigations have revealed that this protein could have many roles in cancer progression and act at different levels (from cancer initiation to metastasis). This is partly due to the location of ANXA1 in different cell compartments. ANXA1 can be nuclear, cytoplasmic and/or membrane associated. This last location allows ANXA1 to be proteolytically cleaved and/or to become accessible to its cognate partners, the formyl-peptide receptors. Indeed, in some cancers, ANXA1 is found at the cell surface, where it stimulates formyl-peptide receptors to trigger oncogenic pathways. In the present review, we look at the different locations of ANXA1 and their association with the deregulated pathways often observed in cancers. We have specifically detailed the non-classic pathways of ANXA1 externalization, the significance of its cleavage and the role of the ANXA1-formyl-peptide receptor complex in cancer progression.
authors.affiliation: Clermont Université, Université d'Auvergne, Imagerie Moléculaire et Thérapie Vectorisée, BP 10448, F-63000 Clermont-Ferrand, France INSERM, U 990, F-63000 Clermont-Ferrand, France boudhra.zied@gmail.com.
authors.forename: Zied
authors.initials: Z
authors.lastname: Boudhraa
authors.affiliation: Clermont Université, Université d'Auvergne, Imagerie Moléculaire et Thérapie Vectorisée, BP 10448, F-63000 Clermont-Ferrand, France INSERM, U 990, F-63000 Clermont-Ferrand, France.
authors.forename: Bernadette
authors.initials: B
authors.lastname: Bouchon
authors.affiliation: Clermont Université, Université d'Auvergne, Imagerie Moléculaire et Thérapie Vectorisée, BP 10448, F-63000 Clermont-Ferrand, France INSERM, U 990, F-63000 Clermont-Ferrand, France.
authors.forename: Claire
authors.initials: C
authors.lastname: Viallard
authors.affiliation: Clermont Université, Université d'Auvergne, Imagerie Moléculaire et Thérapie Vectorisée, BP 10448, F-63000 Clermont-Ferrand, France INSERM, U 990, F-63000 Clermont-Ferrand, France.
authors.forename: Michel
authors.initials: M
authors.lastname: D'Incan
authors.affiliation: Clermont Université, Université d'Auvergne, Imagerie Moléculaire et Thérapie Vectorisée, BP 10448, F-63000 Clermont-Ferrand, France INSERM, U 990, F-63000 Clermont-Ferrand, France.
authors.forename: Françoise
authors.initials: F
authors.lastname: Degoul
mesh_terms: D000818:Animals; D017305:Annexin A1 / Q000737:chemistry / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D002467:Cell Nucleus / Q000378:metabolism; D003593:Cytoplasm / Q000378:metabolism; D006801:Humans; D009369:Neoplasms / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D059748:Proteolysis; D044042:Receptors, Formyl Peptide / Q000378:metabolism; D015398:Signal Transduction; D013329:Structure-Activity Relationship
chemical_list: D017305:Annexin A1; D044042:Receptors, Formyl Peptide
keywords: ANXA1; Cancer; FPRs; Secretory pathways; Structure; cancer; oncogenic pathways; proteolytic cleavage; signalling pathway; subcellular localization