GSN Human C-Terminal Half of Recombinant Protein

The protein encoded by this gene binds to the "plus" ends of actin monomers and filaments to prevent monomer exchange. The encoded calcium-regulated protein functions in both assembly and disassembly of actin filaments. Defects in this gene are a cause of familial amyloidosis Finnish type (FAF). Multiple transcript variants encoding several different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

Gelsolin: a calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed. Its expression is significantly decreased in many tumors and transformed cell lines. Gelsolin and other proteins including E-cadherin, BRCA, p21WAF, HoxA5, and retinoic acid receptor II are regulated by epigenetic changes in breast cancers. Gelsolin helps mediate the ability of HDAC inhibitors to protect neurons from oxygen/glucose deprivation. Two human isoforms are produced by alternative initiation.

Protein type: Nuclear receptor co-regulator; Secreted, signal peptide; Secreted; Motility/polarity/chemotaxis; Actin-binding

Chromosomal Location of Human Ortholog: 9q33

Cellular Component: ruffle; focal adhesion; protein complex; perinuclear region of cytoplasm; lamellipodium; extracellular region; cytosol; actin cytoskeleton

Molecular Function: protein binding; calcium ion binding; actin binding

Biological Process: regulation of cell adhesion; actin filament severing; phosphoinositide-mediated signaling; apoptosis; actin nucleation; vesicle-mediated transport; response to ethanol; actin filament polymerization; tissue regeneration; response to folic acid; oligodendrocyte development; barbed-end actin filament capping; cell structure disassembly during apoptosis; aging

Disease: Amyloidosis, Finnish Type