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Galectin-7 is a member of the galectin family of β-galactoside-binding lectins encoded by the LGALS7 gene, primarily expressed in stratified squamous epithelium such as skin keratinocytes[1][3][6]. It modulates cell–cell and cell–matrix interactions essential for normal tissue architecture and epidermal differentiation. Intracellularly, galectin-7 acts as a pro-apoptotic protein, activating the JNK pathway and promoting cytochrome c release from mitochondria, implicating it in programmed cell death[5]. Galectin-7 also exerts important immunomodulatory functions; it binds to immune regulatory receptors like PD-1, leading to SHP-2 recruitment and suppression of T cell receptor signaling, which can diminish anti-tumor immune responses and contribute to immune exhaustion, especially in tumor microenvironments[2]. Its dysregulation has been linked to various diseases, including certain cancers (notably esophageal squamous cell carcinoma) and cerebrovascular disorders such as cerebral amyloid angiopathy and ischemic hemorrhage. There are no approved drugs specifically targeting galectin-7, but its lectin activity can be blocked experimentally by sugars like lactose[2]. Elevated expression can serve as a biomarker for tissue differentiation and disease states, and therapeutic targeting may pose risks due to widespread physiological roles in tissue homeostasis and immune regulation[4][2].
- Galectin-7 binds β-galactoside-containing glycans on cell surface or matrix proteins, influencing cell adhesion and migration[1][3]. - Acts as a ligand for immune regulatory receptors (e.g., Programmed cell death protein 1, PD-1), suppressing TCR signaling via glycosylation-dependent mechanisms and SHP-2 recruitment[2]. - Intracellularly, it may trigger apoptosis through the JNK signaling pathway and mitochondrial cytochrome c release[5].
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