Annexin A8 (ANXA8)

**Annexin A8** is a member of the annexin family of evolutionarily conserved, calcium-dependent, phospholipid-binding proteins[1][4]. Structurally, all annexins share a conserved core facilitating Ca²⁺-dependent membrane binding with an N-terminal region imparting specificity for protein interactions[1]. Annexin A8 is specifically associated with the limiting membrane of multivesicular late endosomes and is involved in their organization, morphology, and positioning by coupling these membranes to actin filaments[1]. It is also required for the efficient trafficking of CD63 to Weibel-Palade bodies in endothelial cells, thereby influencing the surface presentation of P-selectin and modulating leukocyte recruitment during inflammation[2]. Overexpression or altered function can affect endosomal cargo transport, receptor downregulation (e.g. EGFR), and prolong downstream signal transduction, processes implicated in cancer biology and immune responses[1][2][4]. Associations with leukemia and roles in anticoagulation have been described, though the detailed physiological and pathological mechanisms are still emerging[3][4]. No known drugs directly target annexin A8 as of current knowledge.

Other names

Annexin A8ANXA8ANX8VAC-betaAnnexin VIIIAnnexin-8Vascular anticoagulant-betaCH17-360D5.2