Gelsolin (GSN) ELISA Kit for Human

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

Chromosomal Location of Human Ortholog: 9q33.2

Cellular Component: actin cap; actin cytoskeleton; blood microparticle; cortical actin cytoskeleton; cytoplasm; cytosol; extracellular exosome; extracellular region; extracellular space; ficolin-1-rich granule lumen; focal adhesion; lamellipodium; myelin sheath; nucleus; perinuclear region of cytoplasm; plasma membrane; podosome; ruffle; sarcoplasm; secretory granule lumen

Molecular Function: actin binding; actin filament binding; calcium ion binding; myosin II binding; protein binding

Biological Process: actin filament capping; actin filament polymerization; actin filament reorganization; actin filament severing; actin nucleation; aging; amyloid fibril formation; barbed-end actin filament capping; cellular protein metabolic process; cellular response to cadmium ion; extracellular matrix disassembly; negative regulation of virion penetration into host cell; neutrophil degranulation; oligodendrocyte development; phagocytosis, engulfment; phosphoinositide-mediated signaling; positive regulation of actin nucleation; positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; positive regulation of gene expression; positive regulation of keratinocyte apoptotic process; positive regulation of protein processing in phagocytic vesicle; protein destabilization; regulation of establishment of T cell polarity; regulation of plasma membrane raft polarization; regulation of podosome assembly; regulation of receptor clustering; response to ethanol; response to folic acid; sequestering of actin monomers; striated muscle atrophy; tissue regeneration

Disease: Amyloidosis, Finnish Type