Galectin-7
Galectin-7 is a small protein in humans produced from the LGALS7 gene. It belongs to the galectin family, a group of proteins that bind sugars called beta-galactosides. Galectin-7 is mainly found in keratinocytes, the skin’s outer layer, and in other stratified (multi-layered) epithelial tissues like the cornea and mucous membranes.
This protein helps cells stick to each other and to the surrounding matrix, and it participates in processes that control cell growth, movement, and survival. Galectin-7 can act both inside cells and outside them, and it can be released from cells through a non-typical secretion pathway. It binds to sugar structures on the surfaces of cells and receptors, influencing signaling events that affect cell behavior.
A key role of galectin-7 is in skin and epithelial repair. It promotes the migration of keratinocytes during wound healing (re-epithelialization), aiding the skin’s barrier to close wounds. When galectin-7 is reduced or defective, wound closure can be slower. It also appears to influence other epithelial repairs, such as those in the kidney, cornea, and uterus, by guiding cell movement and adhesion rather than simply increasing the amount of galectin-7.
Galectin-7 also modulates immune responses in tissues that line surfaces, helping to shape how immune cells respond to injury or infection. Its effects can include altering cytokine production and the way immune cells adhere to each other.
In cancer, galectin-7 has a complex, tissue-dependent role. In some contexts, it helps promote cell death or suppress tumor growth; in others, it may be found at higher levels in tumors and could support cancer progression. The status of the p53 tumor suppressor gene can influence galectin-7’s activity, adding to its context-specific behavior. Because of these varied roles, galectin-7 is being studied as a potential therapeutic target to boost wound healing or to modulate cancer, and as a biomarker for certain epithelial tissues.
Structurally, galectin-7 is about 130 amino acids long and can form dimers, which helps it cross-link sugar-bearing molecules on cell surfaces. Its carbohydrate-recognition domain is tuned to bind beta-galactosides, a key feature that drives many of its signaling effects. In addition to its roles in the skin, galectin-7 is found in primary cilia of some epithelial cells, linking its activities to both cellular movement and sensing the cell’s environment.
This page was last edited on 2 February 2026, at 06:26 (CET).