Gelsolin (GSN) Antibody – Goat Polyclonal

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

Chromosomal Location of Human Ortholog: 9q33

Cellular Component: actin cap; actin cytoskeleton; cortical actin cytoskeleton; cytoplasm; cytosol; extracellular region; extracellular space; focal adhesion; lamellipodium; myelin sheath; nucleus; perinuclear region of cytoplasm; plasma membrane; podosome; ruffle; sarcoplasm

Molecular Function: actin binding; calcium ion binding; myosin II binding; protein binding; protein domain specific binding

Biological Process: actin filament capping; actin filament polymerization; actin filament severing; actin nucleation; aging; barbed-end actin filament capping; cellular protein metabolic process; extracellular matrix disassembly; negative regulation of virion penetration into host cell; oligodendrocyte development; phagocytosis, engulfment; phosphoinositide-mediated signaling; positive regulation of actin nucleation; protein destabilization; response to ethanol; response to folic acid; sequestering of actin monomers; striated muscle atrophy; tissue regeneration

Disease: Amyloidosis, Finnish Type