Fibronectin

FN1
Available structures
PDBOrtholog search: H0Y7Z1%20or%20B7ZLE5 PDBe H0Y7Z1,B7ZLE5 RCSB
Identifiers
AliasesFN1, CIG, ED-B, FINC, FN, FNZ, GFND, GFND2, LETS, MSF, fibronectin 1, SMDCF
External IDsOMIM: 135600; MGI: 95566; HomoloGene: 1533; GeneCards: FN1; OMA:FN1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)Chr 2: 215.36 – 215.44 MbChr 1: 71.62 – 71.69 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
The modular structure of fibronectin and its binding domains

Fibronectin is a high-molecular weight (~500-~600 kDa)[5] glycoprotein of the extracellular matrix that binds to membrane-spanning receptor proteins called integrins.[6] Fibronectin also binds to other extracellular matrix proteins such as collagen, fibrin, and heparan sulfate proteoglycans (e.g. syndecans).

Fibronectin exists as a protein dimer, consisting of two nearly identical monomers linked by a pair of disulfide bonds.[6] The fibronectin protein is produced from a single gene, but alternative splicing of its pre-mRNA leads to the creation of several isoforms.

Two types of fibronectin are present in vertebrates:[6]

  • soluble plasma fibronectin (formerly called "cold-insoluble globulin", or CIg) is a major protein component of blood plasma (300 μg/ml) and is produced in the liver by hepatocytes.
  • insoluble cellular fibronectin is a major component of the extracellular matrix. It is secreted by various cells, primarily fibroblasts, as a soluble protein dimer and is then assembled into an insoluble matrix in a complex cell-mediated process.

Fibronectin plays a major role in cell adhesion, growth, migration, and differentiation, and it is important for processes such as wound healing and embryonic development.[6] Altered fibronectin expression, degradation, and organization has been associated with a number of pathologies, including cancer, arthritis, and fibrosis.[7][8]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000115414Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026193Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Mitrović S, Mitrović D, Todorović V (July 1995). "[Fibronectin--a multifunctional glycoprotein]". Srpski Arhiv Za Celokupno Lekarstvo. 123 (7–8): 198–201. PMID 17974429. Archived from the original on February 9, 2022.
  6. ^ a b c d Pankov R, Yamada KM (October 2002). "Fibronectin at a glance". Journal of Cell Science. 115 (Pt 20): 3861–3. doi:10.1242/jcs.00059. PMID 12244123.
  7. ^ Williams CM, Engler AJ, Slone RD, Galante LL, Schwarzbauer JE (May 2008). "Fibronectin expression modulates mammary epithelial cell proliferation during acinar differentiation". Cancer Research. 68 (9): 3185–92. doi:10.1158/0008-5472.CAN-07-2673. PMC 2748963. PMID 18451144.
  8. ^ Kragstrup TW, Sohn DH, Lepus CM, Onuma K, Wang Q, Robinson WH, et al. (2019). "Fibroblast-like synovial cell production of extra domain A fibronectin associates with inflammation in osteoarthritis". BMC Rheumatology. 3: 46. doi:10.1186/s41927-019-0093-4. PMC 6886182. PMID 31819923.