Abstract
Annexin A2 (AnxA2) is a multifunctional calcium2+ (Ca2+) and phospholipid-binding protein that is expressed in a wide spectrum of cells, including those participating in the inflammatory response. In acute inflammation, the interaction of AnxA2 with actin and adherens junction VE-cadherins underlies its role in regulating vascular integrity. In addition, its contribution to endosomal membrane repair impacts several aspects of inflammatory regulation, including lysosome repair, which regulates inflammasome activation, and autophagosome biogenesis, which is essential for macroautophagy. On the other hand, AnxA2 may be co-opted to promote adhesion, entry, and propagation of bacteria or viruses into host cells. In the later stages of acute inflammation, AnxA2 contributes to the initiation of angiogenesis, which promotes tissue repair, but, when dysregulated, may also accompany chronic inflammation. AnxA2 is overexpressed in malignancies, such as breast cancer and glioblastoma, and likely contributes to cancer progression in the context of an inflammatory microenvironment. We conclude that annexin AnxA2 normally fulfills a spectrum of anti-inflammatory functions in the setting of both acute and chronic inflammation but may contribute to disease states in settings of disordered homeostasis.
Highlights
Inflammation is defined as the local host response to injury caused by infectious or noninfectious agents; it results in elimination or compartmentalization of the inciting agent, clearance of necrotic cells, and repair of damaged tissue [1,2]
Annexin A2 (AnxA2) seemsfacilitation to fulfill many functions, including of additional specialized membrane membrane membrane microdomains, of vesicle budding, andorganization regulation of microdomains, of vesicle budding,endosomal and regulation of additional membrane dynamic events dynamic eventsfacilitation such as fusion, endocytosis, biogenesis, and membrane repair suchIn as view fusion, endosomal biogenesis, and membrane ofendocytosis, this wide array of functions, we have developed repair a working model depicting the
Addition of a peptide that mimics the N-terminal domain of annexin A2 and blocks tissue plasminogen activator (tPA) binding reduced the number of von Willebrand factor positive cells by 80%, whereas a scrambled control peptide had no effect [75]
Summary
Inflammation is defined as the local host response to injury caused by infectious or noninfectious agents; it results in elimination or compartmentalization of the inciting agent, clearance of necrotic cells, and repair of damaged tissue [1,2]. In the later stages of inflammation, AnxA2 likely promotesAnxA2 angiogenesis necessary for biogenesis of the phagophore, a double membrane structure that engulfs and destroys and wound healing by supporting cell surface fibrinolytic activity. States,within excessive angiogenesis that is sustained by AnxA2 may induce tissue damage, as in the diabetic retina, or may support the progression of cancer.
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