Abstract
Galectin-7 is a soluble unglycosylated lectin that is able to bind specifically to β-galactosides. It has been described to be involved in apoptosis, proliferation and differentiation, but also in cell adhesion and migration. Several disorders and diseases are discussed by covering the aforementioned biological processes. Structural features of galectin-7 are discussed as well as targeting the protein intracellularly or extracellularly. The exact molecular mechanisms that lie behind many biological processes involving galectin-7 are not known. It is therefore useful to come up with chemical probes or tools in order to obtain knowledge of the physiological processes. The objective of this review is to summarize the roles and functions of galectin-7 in the human body, providing reasons why it is necessary to design inhibitors for galectin-7, to give the reader structural insights and describe its current inhibitors.
Highlights
Extracellular galectin-7 promotes cancer via binding to cell surface receptors of cancer cells and induce de novo transcriptional activation of LGALS7, which in turn render cells resistant to pro-apoptotic drugs. Another example is displayed by the binding of extracellular galectin-7 to glycoreceptors expressed in infiltrated immune cells that triggers a cascade of signaling events, leading to the apoptosis of cancer-killing T cells, or alters their regulatory functions, helping tumors evade anti-tumor immunity [95]
Galectin7 is a member of the prototype galectin family, which is mainly expressed in stratified epithelia of several tissues
Several strategies were developed to knockout galectin-7 or suppress its translation, we believe the field of cellular pathophysiology would benefit from small-molecule inhibitors which can be administered to evaluate its effect on cellular disorders and even diseases such as cancer
Summary
Acting intra- or extracellularly, galectin-7 participates in diverse processes, such as controlling apoptosis, cell migration and cell adhesion It plays a crucial role in the re-epithelialization process of corneal or epidermal wounds and in several human diseases/disorders, such as cancer [12]. As cell migration is an important process involved in proper wound healing, Huang and co-workers demonstrated that a high glucose environment reduced galectin-7 expression in keratinocytes, due to enhanced O-GlcNAc (O-linked N-acetyl-D-glucosamine) glycosylation of certain regulators of galectin-7 expression. A more detailed review regarding the re-epithelialization of skin wounds is reported [26] In their search for novel, galectin-based therapeutic strategies for the treatment of nonhealing corneal tissue epithelial defects, Cao et al demonstrated via Western blot analysis that healing corneas contained increased levels of galectin-7 throughout the epithelium, compared with normal corneas after injury. Er: YAG laser irradiation causes a direct effect of promoting proliferation, migration, and invasion of PDL fibroblasts through the upregulation of galectin-7, yet its signaling pathway needs to be verified [28]
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