Capping Protein Gelsolin-Like, also known as CapG, is a member of the gelsolin family of actin-modulating proteins. These proteins play a crucial role in the regulation of the actin cytoskeleton, which is essential for various cellular processes such as cell signaling, membrane ruffling, phagocytosis, and motility .
CapG is a calcium-sensitive protein that binds to the barbed ends of actin filaments, thereby capping them and preventing further polymerization. Unlike some other members of the gelsolin family, CapG does not sever preformed actin filaments . This capping activity is regulated by calcium ions and phosphoinositides, which modulate the interaction between CapG and actin filaments .
CapG is ubiquitously expressed in various tissues and has been implicated in several physiological and pathological processes. It is particularly important in macrophage function, where it regulates cytoplasmic and nuclear structures through potential interactions with actin . Additionally, CapG has been shown to play a role in cell migration and invasion, making it a protein of interest in cancer research .
The expression of CapG has been found to be dysregulated in various cancers, including oral squamous cell carcinoma (OSCC). Studies have shown that CapG is upregulated in OSCC and is associated with advanced clinical stages of the disease . This suggests that CapG could serve as a potential biomarker for cancer progression and a therapeutic target .
Recombinant human CapG is produced using recombinant DNA technology, which involves inserting the gene encoding CapG into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of CapG for research and therapeutic purposes. Recombinant CapG retains the functional properties of the native protein, making it a valuable tool for studying the role of CapG in various biological processes and diseases.