AnxA8

Annexin A8 (ANXA8, AnxA8) is a Ca²⁺-dependent phospholipid-binding member of the annexin family that participates in membrane organization and membrane-cytoskeleton interactions through binding to F-actin and phosphoinositides^[1]. Mechanistically, ANXA8 regulates intracellular membrane trafficking and endocytosis, and it contributes to leukocyte-endothelium adhesion through control of CD63 sorting and membrane presentation, linking membrane dynamics to cell adhesion pathways^[1]. ANXA8 also influences extracellular matrix adhesion through integrin β1-dependent processes and therefore contributes to cellular migration, invasion, and adhesion, biological programs frequently altered during tumor progression^[1]. Consistent with these functions, ANXA8 is commonly described as a tumor-promoting factor and is overexpressed in multiple human malignancies^[1][2]. In disease-related experimental settings, ANXA8 mRNA is markedly overexpressed in metastatic lymph nodes from oral squamous cell carcinoma and improves molecular detection of lymph node metastasis when combined with KRT19-based assays^[3]. This application highlights its value as a biomarker in translational cancer research and metastatic disease modeling rather than as a validated therapeutic target^[3]. Compared with related annexin isoforms, ANXA8 shows a more restricted tissue distribution and has been particularly linked to membrane trafficking, endocytic regulation, and adhesion-associated functions, supporting its use in studies of membrane biology and cancer progression^[1]. Current literature primarily emphasizes biomarker and mechanistic applications, whereas selective ANXA8 agonists or inhibitors remain insufficiently established for routine experimental use^[1][3].

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