Plasma gelsolin

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	2FGH, 1H1V, 3CIP, 6QW3, 1D0N, 1KCQ, 1P8X, 3C15, 3FFN, 5DD2, 5UBO, 5ZZ0, 6LJK, 1C0F, 1EQY, 1ESV, 1RGI, 1YAG, 2FH1, 2FH2, 2FH3, 2FH4, 2LLF, 3FFK, 3TU5, 5FAE, 5FAF, 5H3M, 5H3N, 5O2Z, 6JCO, 6JEG, 6JEH, 6LJE, 6Q9R, 6Q9Z, 6QBF, 1SVY, 4CBX, 1D4X, 1MDU, 1NLV, 1NM1, 1NMD, 1NPH, 1P8Z, 1SOL, 1YVN, 2FF3, 2FF6, 3A5L, 3A5M, 3A5N, 3A5O, 3CJB, 3CJC, 5MVV, 1C0G

Plasma Gelsolin
Plasma Gelsolin
	Crystal structure of the cytoplasmic form of human Gelsolin (3FFN)
Identifiers
Symbol	Plasma Gelsolin
Pfam	PF00626
Pfam clan	CL0092
InterPro	IPR007123
SCOP2	1vil / SCOPe / SUPFAM
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary
PDB	2FGH, 1H1V, 3CIP, 6QW3, 1D0N, 1KCQ, 1P8X, 3C15, 3FFN, 5DD2, 5UBO, 5ZZ0, 6LJK, 1C0F, 1EQY, 1ESV, 1RGI, 1YAG, 2FH1, 2FH2, 2FH3, 2FH4, 2LLF, 3FFK, 3TU5, 5FAE, 5FAF, 5H3M, 5H3N, 5O2Z, 6JCO, 6JEG, 6JEH, 6LJE, 6Q9R, 6Q9Z, 6QBF, 1SVY, 4CBX, 1D4X, 1MDU, 1NLV, 1NM1, 1NMD, 1NPH, 1P8Z, 1SOL, 1YVN, 2FF3, 2FF6, 3A5L, 3A5M, 3A5N, 3A5O, 3CJB, 3CJC, 5MVV, 1C0G

Plasma gelsolin (pGSN) is an 83 kDa abundant protein constituent of normal plasma and an important component of the innate immune system. The identification of pGSN in Drosophila melanogaster^[1] and C. elegans^[2] points to an ancient origin early in evolution.^[3] Its extraordinary structural conservation reflects its critical regulatory role in multiple essential functions.^[4] Its roles include the breakdown of filamentous actin released from dead cells, activation of macrophages, and localization of the inflammatory response. Substantial decreases in plasma levels are observed in acute and chronic infection and injury in both animal models and in humans. Supplementation therapies with recombinant human pGSN have been shown effective in more than 20 animal models.

pGSN has a cytoplasmic isoform (cGSN) known to be an actin-binding protein controlling cytoskeletal dynamics. cGSN is expressed from the same gene, and is identical to pGSN except for its lack of a 24 amino acid N-terminal extension.

^ Shi, Yigong (2004-08-01). "Caspase activation, inhibition, and reactivation: A mechanistic view". Protein Science. 13 (8): 1979–1987. doi:10.1110/ps.04789804. ISSN 0961-8368. PMC 2279816. PMID 15273300.
^ Klaavuniemi, Tuula; Yamashiro, Sawako; Ono, Shoichiro (2008-09-19). "Caenorhabditis elegans Gelsolin-like Protein 1 Is a Novel Actin Filament-severing Protein with Four Gelsolin-like Repeats". Journal of Biological Chemistry. 283 (38): 26071–26080. doi:10.1074/jbc.M803618200. ISSN 0021-9258. PMC 2533794. PMID 18640981.
^ Archer, Stuart K.; Claudianos, Charles; Campbell, Hugh D. (2005). "Evolution of the gelsolin family of actin-binding proteins as novel transcriptional coactivators". BioEssays. 27 (4): 388–396. doi:10.1002/bies.20200. ISSN 1521-1878. PMID 15770676. S2CID 40585071.
^ Cite error: The named reference Lee1992 was invoked but never defined (see the help page).

[1] Shi, Yigong (2004-08-01). "Caspase activation, inhibition, and reactivation: A mechanistic view". Protein Science. 13 (8): 1979–1987. doi:10.1110/ps.04789804. ISSN 0961-8368. PMC 2279816. PMID 15273300.

[2] Klaavuniemi, Tuula; Yamashiro, Sawako; Ono, Shoichiro (2008-09-19). "Caenorhabditis elegans Gelsolin-like Protein 1 Is a Novel Actin Filament-severing Protein with Four Gelsolin-like Repeats". Journal of Biological Chemistry. 283 (38): 26071–26080. doi:10.1074/jbc.M803618200. ISSN 0021-9258. PMC 2533794. PMID 18640981.

[3] Archer, Stuart K.; Claudianos, Charles; Campbell, Hugh D. (2005). "Evolution of the gelsolin family of actin-binding proteins as novel transcriptional coactivators". BioEssays. 27 (4): 388–396. doi:10.1002/bies.20200. ISSN 1521-1878. PMID 15770676. S2CID 40585071.

[Lee1992-4] Cite error: The named reference Lee1992 was invoked but never defined (see the help page).

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