Gelsolin (GSN)
The protein contains 782 amino acids for an estimated molecular weight of 85698 Da.
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. Plays a role in ciliogenesis. (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
This protein is annotated as membranous in Gene Ontology.
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Biological Process
Actin filament capping
Actin filament depolymerization
Actin filament polymerization
Actin filament reorganization
Actin filament severing
Actin nucleation
Actin polymerization or depolymerization
Aging
Amyloid fibril formation
Apoptotic process
Barbed-end actin filament capping
Cardiac muscle cell contraction
Cell projection assembly
Cellular component disassembly involved in execution phase of apoptosis
Cellular protein metabolic process
Cellular response to cadmium ion
Cellular response to interferon-gamma
Central nervous system development
Cilium assembly
Hepatocyte apoptotic process
Negative regulation of viral entry into host cell
Neutrophil degranulation
Oligodendrocyte development
Phagocytosis, engulfment
Phosphatidylinositol-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 cell adhesion
Regulation of establishment of T cell polarity
Regulation of plasma membrane raft polarization
Regulation of podosome assembly
Regulation of receptor clustering
Relaxation of cardiac muscle
Renal protein absorption
Response to ethanol
Response to folic acid
Response to muscle stretch
Sequestering of actin monomers
Striated muscle atrophy
Tissue regeneration
Vesicle-mediated transport
Wound healing
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
Obsolete cell
Perinuclear region of cytoplasm
Phagocytic vesicle
Plasma membrane
Podosome
Protein complex
Protein-containing complex
Ruffle
Sarcoplasm
Secretory granule lumen
The reference OMIM entry for this protein is 105120
Amyloidosis, finnish type
Amyloidosis v
Amyloidosis, meretoja type
Amyloid cranial neuropathy with lattice corneal dystrophy
Amyloidosis due to mutant gelsolin cerebral amyloid angiopathy, gsn-related, included
Corneal dystrophy, lattice ty
A number sign (#) is used with this entry because the Finnish type of amyloidosis is caused by mutation in the gelsolin gene (GSN; 137350). See also corneal lattice dystrophy due to local amyloid deposition (122200), which occurs as an isolated dominant.
DESCRIPTION
The Finnish type of systemic amyloidosis is characterized clinically by a unique constellation of features including corneal lattice dystrophy, and cranial neuropathy, bulbar signs, and skin changes. Some patients may develop peripheral neuropathy and renal failure. The disorder is usually inherited in an autosomal dominant pattern; however, homozygotes with a more severe phenotype have also been reported (Meretoja, 1973).CLINICAL FEATURES
In a massive investigation in Finland, Meretoja (1973) identified 207 affected persons. Two patients, whose parents were affected and who were more severely affected than the others, were thought to represent homozygosity. A few of the patients developed nephrotic syndrome and renal failure and some had cardiac involvement. Amyloid involvement was rather widespread at autopsy. Meretoja et al. (1978) collected 307 patients in Finland. Three Czechoslovakian sisters with bulbar palsy, 'cutis hyperelastica,' and lattice dystrophy of the cornea, reported by Klaus et al. (1959), may have had this disorder. Cases were reported from the United States by Sack et al. (1981), Purcell et al. (1983), Darras et al. (1986), and Starck et al. (1991); from Holland by Winkelman et al. (1971); and from Denmark by Boysen et al. (1979). One of the patients reported by Sack et al. (1981) had onset of facial paralysis, which began as inability to control a drooping lower lip, at the age of about 56; the lip became strikingly protuberant and everted with exposure of the lower gingival mucosa. Five years after onset he could not wrinkle his forehead and there was an intermittent twitch of the right side of the lower lip. The extraocular muscles were affected only minimally and there was no ptosis. A striking feature was laxity of the skin, which raised the question of cutis laxa. Slit-lamp examination showed a lattice type of corneal opacity bilaterally. The mother had the identical disorder beginning at about the same stage of life. The proband had bulbar manifestations. Kiuru (1992) reported the clinical findings of 30 patients. Signs of cranial neuropathy especially affecting the facial nerve were found in all, and peripheral polyneuropathy mainly affecting vibration and touch senses was demonstrated in 26 patients. Kiuru et al. (1994) studied the autonomic nervous system and heart in 30 patients. Minor autonomic nervous system dysfunction was found in most patients, but clinically significant autonomic dysfunction or cardiopathy was not characteristic.MOLECULAR GENETICS
Maury et al. (1990) studied amyloid fibrils isolated from the kidney of a patient with the Finnish form. The amino acid sequence determined for part of the protein was identical to that deduced for plasma gelsolin in the region of amino acids 235-269. Using PCR and allele-specific oligonucleotide hybridization analysis of genomic DNA in patients with this disorder, Maury et al. (1990) identified a 654G-A transition in the GSN gene, resulting in an asp187-to-asn substitution (137350.0001), in all 5 unrelated patients studied, but not in 45 unrelated control subjects. Haltia et al. (1990) likewise showed that the amyloid in this disorder is antigenically and str ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 105120 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed