Alternative titles; symbols
HGNC Approved Gene Symbol: FN1
SNOMEDCT: 254078005, 722759007;
Cytogenetic location: 2q35 Genomic coordinates (GRCh38) : 2:215,360,865-215,436,068 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 2q35 | Glomerulopathy with fibronectin deposits 2 | 601894 | Autosomal dominant | 3 |
| Spondylometaphyseal dysplasia, corner fracture type | 184255 | Autosomal dominant | 3 |
Fibronectin-1 belongs to a family of high molecular weight glycoproteins that are present on cell surfaces, in extracellular fluids, connective tissues, and basement membranes. Fibronectins interact with other extracellular matrix proteins and cellular ligands, such as collagen, fibrin, and integrins. Fibronectins are involved in adhesive and migratory processes of cells. Two major forms of fibronectin exist: a plasma soluble form and a cellular form (summary by Muro et al., 2003).
Kornblihtt et al. (1983) isolated clones corresponding to the human fibronectin gene from a human carcinoma cDNA library. The sequence showed approximately 90% homology to the bovine sequence. Fibronectin mRNA was estimated to be 7.9 kb. The data suggested that fibronectin is coded by a single gene and that the cellular and plasma proteins arise from post-transcriptional events.
Kornblihtt et al. (1984) identified 2 different fibronectin cDNA clones and corresponding mRNAs that differed by the presence or absence of a 270-bp internal fragment (termed ED for 'extra domain,' EDA, or EDIIIA) that encodes a 90-residue domain of type III homology found in the bovine protein. This 90-residue fragment is in the C terminus between the cell attachment and heparin-binding domains of the protein. Human liver produced mainly the form without the internal fragment.
Kornblihtt et al. (1985) determined that the fibronectin gene encodes a polypeptide of 2,146 to 2,325 residues, depending on which internal splicing has taken place. The primary structure of the protein contains several internal homologous regions, reflecting high complexity. Different motifs showed specific binding domains for fibrin, heparin, collagen, and DNA.
Sekiguchi et al. (1986) also found that liver fibronectin cDNAs lacked the ED segment that is present in most cDNAs encoding cellular fibronectin. Furthermore, 2 liver cDNAs differed in sequence at the 'type III connecting segment' (IIICS) region by the presence or absence of 192 bp with flanking regions. Cellular FN1 cDNAs contained the 192-base IIICS region. Thus, cellular fibronectin appears to have extra peptide segments, encoded by the IIICS region and its flanking segments as well as the 270-base ED region, that are mostly absent in liver fibronectin.
Gutman and Kornblihtt (1987) described a third region of variability in human fibronectin in addition to the EDA and IIICS regions. This third region resembles the EDA and consists of a 273-nucleotide exon (termed 'EDII,' EDB, or EDIIIB) encoding exactly one 91-amino acid repeat of type III homology located between the DNA- and the cell-binding domains of FN. The 2 corresponding mRNA variants were present in cells known to synthesize the cellular form of FN. Liver cells, which are the source of plasma FN, produced only messengers without the EDB. Gutman and Kornblihtt (1987) concluded that both the EDA and EDB sequences are restricted to cellular FN. Combination of all the possible patterns of splicing in the 3 regions described could theoretically generate as many as 20 distinct FN polypeptides from a single gene.
Using human-mouse somatic cell hybrids, Koch et al. (1982) mapped the FN1 gene to chromosome 2, and Prowse et al. (1986) confirmed this assignment with a cDNA probe applied to somatic cell hybrids. Henry et al. (1985) assigned FN1 to 2q23.2-qter with a genomic probe in somatic cell hybrids with rearranged human chromosomes. Wu et al. (1993) mapped FN1 to 2q34 by fluorescence in situ hybridization.
Skow et al. (1987) mapped the mouse Fn1 gene to the midregion of chromosome 1, about 4 cM distal to the Cryg locus (123660). The mapping was done by study of recombinant inbred strains of mice and a RFLP identified with a cDNA for human fibronectin. Zneimer and Womack (1988) mapped fibronectin to mouse chromosome 1 by in situ hybridization.
Pseudogene
In meiotic chromosomes, Jhanwar et al. (1986) observed 2 sites of FN hybridization on chromosome 2, 2p16-p14 and 2q34-q36, and 1 on chromosome 11, 11q12.1-q13.5. Only the chromosome 2 sites showed hybridization in somatic cells. The authors suggested that 1 of the 2 sites on chromosome 2 might represent a pseudogene.
By NMR spectroscopy, Schwarz-Linek et al. (2003) determined the structure of a streptococcal (S. dysgalactiae) fibronectin-binding protein peptide (B3) in complex with the module pair (1)F1(2)F1 of human fibronectin. This identified the (1)F1- and (2)F1-binding motifs in B3 that form additional antiparallel beta-strands on sequential F1 modules--the first example of a tandem beta-zipper. Sequence analyses of larger regions of the fibronectin-binding proteins from S. pyogenes and S. aureus revealed a repeating pattern of F1-binding motifs that match the pattern of F1 modules in the N-terminal bacterium-binding site of fibronectin. Schwarz-Linek et al. (2003) concluded that in the process of fibronectin-mediated invasion of host cells, the bacterial proteins seem to exploit the modular structure of fibronectin by forming extended tandem beta-zippers.
A major function of the fibronectins is in the adhesion of cells to extracellular materials such as solid substrata and matrices. Bing et al. (1982) showed that fibronectin binds to C1q (see 120550) in the same manner that it binds collagen. Because fibronectin stimulates endocytosis and promotes the clearance of particulate material from the circulation, Bing et al. (1982) suggested that fibronectin functions in the clearance of C1q-coated material such as immune complexes or cellular debris.
Matsuura et al. (1988) found that a single glycosylation at a defined threonine residue of the IIICS region of fibronectin defines an antigenic epitope recognized by monoclonal antibody FDC-6, which specifically recognizes fibronectin isolated from fetal and malignant cells and tissues.
Commenting on the use of high-density DNA microarrays in gene expression profiling, Ridley (2000) pointed out that the results of Clark et al. (2000) and Bittner et al. (2000) indicated that fibronectin is required for the metastasis of melanoma cells.
Alternatively spliced FN1 EDA and EDB are prominently expressed during wound healing, lung, liver and kidney fibrosis, vascular intimal proliferation, and cardiac transplantation. Liao et al. (2002) found that the EDA segment of cellular FN1 binds integrins ITGA9 (603963)-ITGB1 (135630) and ITGA3 (605025)-ITGB1 on cells. The findings established a mechanism by which cell adhesion to fibronectin can be regulated by alternative splicing.
Sakai et al. (2003) demonstrated that fibronectin is essential for cleft formation during the initiation of epithelial branching in the formation of salivary glands. Fibronectin mRNA and fibrils appeared transiently and focally in forming cleft regions of submandibular salivary gland epithelia, accompanied by an adjacent loss of E cadherin (192090) localization. Decreasing fibronectin blocked cleft formation and branching, whereas exogenous fibronectin accelerated it. Similar effects of fibronectin suppression and augmentation were observed in developing lung and kidney. Mechanistic studies revealed that fibrillar fibronectin could induce cell-matrix adhesions on cultured human salivary epithelial cells with a local loss of cadherins at cell-cell junctions. The findings indicated that fibronectin expression is required for branching morphogenesis associated with the conversion of cell-cell adhesions to cell-matrix adhesions.
Jiang et al. (2003) observed that the soluble trimeric, but not monomeric, fibronectin domain FNIII7-10 bound specifically to integrin ITGAV (193210)-ITGB3 (173470) on the leading edge of migratory cells. Studies using force breakage indicated that the actin-binding protein talin-1 (TLN1; 186745) initially forms a molecular bond between closely packed fibronectin-integrin complexes and the actin cytoskeleton before the recruitment of other proteins. These mechanical forces on matrix-integrin-cytoskeleton linkages are crucial for cell viability, morphology, and organ function.
Matsunaga et al. (2003) found that VLA4 (see 192975)-positive leukemic cells acquired resistance to anoikis (loss of anchorage) or drug-induced apoptosis through the phosphatidylinositol-3-kinase (see 601232)/AKT (164730)/BCL2 (151430) signaling pathway, which is activated by the interaction of VLA4 and fibronectin. This resistance was negated by VLA4-specific antibodies. In a mouse model of minimal residual disease, Matsunaga et al. (2003) achieved a 100% survival rate by combining VLA4-specific antibodies and cytosine arabinoside, whereas cytosine arabinoside alone prolonged survival only slightly. In addition, overall survival at 5 years was 100% for 10 VLA4-negative patients and 44.4% for 15 VLA4-positive patients. Matsunaga et al. (2003) concluded that the interaction between VLA4 on leukemic cells and fibronectin on stromal cells may be crucial in bone marrow minimal residual disease and prognosis in acute myelogenous leukemia.
Using ELISA, Grau et al. (2006) found that expression of the serine peptidase HTRA1 (602194) was upregulated in synovial fluid from both osteoarthritis (OA; see 165720) and rheumatoid arthritis (RA; see 180300) patients compared with normal human fluid. HTRA1 was also highly expressed in and secreted by cultured OA and RA synovial fibroblasts, but not by normal human foreskin fibroblasts. Recombinant human HTRA1 lacking its N-terminal domains, representing an autoproteolytically processed form, degraded purified human fibronectin into several fragments. Synovial fibroblasts exposed to these fragments subsequently upregulated mRNA expression and secretion of the matrix metalloproteases MMP1 (120353) and MMP3 (185250). Inhibition of HTRA1 abrogated fibronectin fragment formation and MMP upregulation. Grau et al. (2006) concluded that HTRA1 can contribute to destruction of extracellular matrix through both direct and indirect mechanisms.
Glomerulopathy with Fibronectin Deposits 2
In affected members of 6 unrelated families with glomerulopathy with fibronectin deposits (GFND2; 601894), Castelletti et al. (2008) identified 3 heterozygous mutations in the FN1 gene (135600.0001-135600.0003). Studies of the mutant proteins suggested that GFND-associated mutations in FN1 impair the control of the assembly of FN1 into fibrils and the balance between soluble and insoluble fibronectin. Six (40%) of 15 affected families were found to have FN1 mutations.
Spondylometaphyseal Dysplasia, Corner Fracture Type
In affected individuals from 7 families with the corner fracture type of spondylometaphyseal dysplasia (SMDCF; 184255), Lee et al. (2017) identified heterozygosity for mutations in the FN1 gene (see, e.g., 135600.0004-135600.0006). None of the SMDCF patients showed any evidence of renal disease. The authors noted that GFND2-associated mutations tend to cluster in more C-terminally located regions, whereas the SMDCF-associated mutations are more N-terminally located.
In a 12-year-old girl with SMDCF, Sabir et al. (2021) identified a de novo heterozygous missense mutation in the FN1 gene (C225W; 135600.0007). The mutation was found by trio whole-exome sequencing. Functional studies were not performed.
Early Mapping Studies
In clones derived from human-mouse hybrids, Owerbach et al. (1978) found that LETS segregated with chromosome 8 and with glutathione reductase (GSR; 138300), which is also located on 8p. Smith et al. (1979) concluded that chromosomes 3 and 11 are essential to expression of fibronectin. Eun and Klinger (1980) also found synteny of fibronectin production and chromosome 11. Kurkinen et al. (1980) postulated that the inconsistencies may reflect the synthesis of different polypeptide chains. Using a specific immunoassay for fibronectin in mouse-human cell hybrids, Rennard et al. (1981) found 100% concordance between expression of human fibronectin and glutathione reductase. The authors suggested that a gene on chromosome 8 may control the presence or absence of FN on the cell surface, whereas another gene mapped to chromosome 11 may involve the fibrillar morphology of cellular FN. Smith et al. (1982) also concluded that the production of soluble fibronectin was associated with chromosome 11. Clones that contained human chromosome 3 in the absence of chromosome 11 did not produce fibronectin, and 2 clones that did not produce fibronectin were positive for glutathione reductase. They concluded that the structural gene for FN was on chromosome 11.
To investigate the role of plasma fibronectin in vivo, Sakai et al. (2001) generated plasma fibronectin-deficient adult mice using Cre-loxP conditional gene-knockout technology. Sakai et al. (2001) demonstrated that plasma fibronectin-deficient mice show increased neuronal apoptosis and larger infarction areas following transient focal cerebral ischemia. Surprisingly, plasma fibronectin was not essential for skin wound healing or hemostasis.
Muro et al. (2003) generated mice with constitutive inclusion or complete exclusion of the EDA exon in the Fn1 gene. Both types of homozygous mice developed normally and were viable. However, those without the EDA exon showed abnormal skin wound healing. Adult mice with constitutive expression of the EDA exon showed a major decrease of Fn1 in all tissues. Both mutant mice had significantly shorter life spans compared to wildtype mice. The findings indicated that EDA splicing regulation is necessary for long-term maintenance of biologic functions.
In affected members of an Italian family with glomerulopathy with fibronectin deposits (601894), Castelletti et al. (2008) identified a heterozygous 5773T-A transversion in exon 36 of the FN1 gene, resulting in a trp1925-to-arg (W1925R) substitution in the III-13 repeat of the HepII heparin-binding domain. The family was first described by Strom et al. (1995). Clinical features included proteinuria, hypertension, microhematuria, slowly decreasing renal function, and the presence of enlarged glomeruli with fibronectin-positive subendothelial and mesangial deposits on renal biopsy. The deposited fibronectin was mainly plasma-derived. In vitro functional expression studies showed that the mutant protein had decreased binding to heparin and to endothelial cells. Castelletti et al. (2008) hypothesized that abnormal fibronectin could disturb cell spreading and the cytoskeleton in glomerular endothelial cells and podocytes, which would alter glomerular properties and induce abnormal protein trafficking. In addition, mutations in the FN1 gene could alter the balance between soluble and insoluble fibronectin.
In affected members of a family from New Zealand with glomerulopathy with fibronectin deposits (601894), Castelletti et al. (2008) identified a heterozygous 5921T-G transversion in exon 37 of the FN1 gene, resulting in a leu1974-to-arg (L1974R) substitution in the III-13 repeat of the HepII heparin-binding domain. In vitro functional expression studies showed that the mutant protein had decreased binding to heparin and to endothelial cells.
In affected members of 4 unrelated families with glomerulopathy with fibronectin deposits (601894), Castelletti et al. (2008) identified a heterozygous 2918A-G transition in the FN1 gene, resulting in a tyr973-to-cys (Y983C) substitution in the III-4 repeat in the HepIII heparin-binding domain. Three of the families had previously been reported by Mazzucco et al. (1992), Assmann et al. (1995), and Niimi et al. (2002). The 4 families were of different ethnic origin and did not share a disease haplotype, thus excluding a founder effect.
In a mother and 2 sons (family 1) with the corner fracture type of spondylometaphyseal dysplasia (SMDCF; 184255), originally reported by Sutton et al. (2005), Lee et al. (2017) identified heterozygosity for a c.260G-T transversion (c.260G-T, NM_212482.2) in the FN1 gene (chr2:g.216,299,436C-A; GRCh37), resulting in a cys87-to-phe (C87F) substitution at a highly conserved residue involved in a disulfide bond within fibronectin domain I-1 in the N-terminal assembly domain. The mutation was not found in the unaffected maternal grandmother or in the ExAC database. Functional analysis in transfected HEK293 cells showed significantly reduced to undetectable secretion of the C87F mutant compared to wildtype, and immunofluorescence analysis demonstrated increased intracellular retention of the mutant protein.
In a mother and daughter (family 4) with the corner fracture type of spondylometaphyseal dysplasia (SMDCF; 184255), Lee et al. (2017) identified heterozygosity for a c.718T-G transversion (c.718T-G, NM_212482.2) in the FN1 gene (chr2:g.216,293,029A-C; GRCh37), resulting in a tyr240-to-asp (Y240D) substitution at a highly conserved residue involved in a disulfide bond within fibronectin domain I-5 in the N-terminal assembly domain. The mutation was not found in an unaffected daughter or in the ExAC database. Western blot analysis of conditioned cell-culture medium from transfected HEK293 cells showed significantly reduced to undetectable secretion of the Y240D mutant compared to wildtype, and immunofluorescence analysis demonstrated increased intracellular retention of the mutant protein.
In 14-year-old boy (family 2) and an unrelated 4-year-old girl (family 7) with the corner fracture type of spondylometaphyseal dysplasia (SMDCF; 184255), Lee et al. (2017) identified heterozygosity for a c.367T-C transition (c.367T-C, NM_212482.2) in the FN1 gene (chr2:g.216,298,095A-G; GRCh37), resulting in a cys123-to-arg (C123R) substitution at a highly conserved residue involved in a disulfide bond within fibronectin domain I-2 in the N-terminal assembly domain. The mutation occurred de novo in both children, and was not found in the ExAC database.
In a 12-year-old girl with the corner fracture type of spondylometaphyseal dysplasia (SMDCF; 184255), Sabir et al. (2021) identified a de novo heterozygous c.675C-G transversion (c.675C-G, NM_212482.2) in the FN1 gene, predicted to result in a cys225-to-trp (C225W) substitution. The mutation was identified by trio whole-genome sequencing. Functional studies were not performed.
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