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AttributesValues
rdf:type
rdfs:label
  • Fibronectin
equivalentClass
OMIM_Number
  • 135600
Semantic_Type
  • Amino Acid, Peptide, or Protein
  • Biologically Active Substance
Preferred_Name
  • Fibronectin
UMLS_CUI
  • C0016055
ALT_DEFINITION
  • adhesive glycoprotein found in blood (as an opsonin and platelet aggregation factor), connective tissue (as a collagen crosslinker), and bound to cell surfaces (as a cell adhesion protein).CSP2000
Legacy_Concept_Name
  • Fibronectin
FULL_SYN
  • FibronectinPTNCI
  • LETS ProteinSYNCI
  • Cold-Insoluble GlobulinSYNCI
  • Fibronectin 1SYNCI
  • FNABNCI
  • FN1SYNCI
  • CIGABNCI
  • FNZABNCI
  • LETSABNCI
  • Large External Transformation-Sensitive ProteinSYNCI
Swiss_Prot
  • P02751
DEFINITION
  • Encoded as alternative isoforms by human FN1 Gene, 2386-aa 262.6-kD Fibronectin precursor is a sulfated disulfide bound glycoprotein with multiple type I, II, and III fibronectin domains. MSF FN70 is an isoform. Plasma (hepatocytes) and cellular (fibroblasts and epithelia) FN differ in activity. Cell surface cellular FN (di/multimeric) is deposited in the ECM. FN is involved in embryogenesis, cell adhesion, migration, and motility, opsonization, wound healing, coagulation, host defense, cell shape, and metastasis. It stimulates endocytosis and may promote clearance of C1q-coated immune complexes. FN binds cell surface integrin, C1q, collagen, fibrin, hyaluronic acid, heparin, FBLN1, and actin. Most cells depend on FN to bind collagen. Talin-1 may link FN/Integrin with the actin cytoskeleton. FN may promote contact inhibition. (from LocusLink, Swiss-Prot, OMIM, and NCI)NCI
  • Fibronectin (FN) is a multifunctional adhesive glycoprotein found in blood, in connective tissue, and on cell surfaces. The plasma and cellular forms differ in biologic activity and arise from a single gene by alternative splicing. Fibronectins function as adhesive ligand-like molecules in cell adhesion, morphology, and surface architecture. The absence of fibronectin causes a loss of contact inhibition in transformed cells. While hepatocytes and smooth muscle cells have collagen receptors, most other cells depend on fibronectin for binding to collagen and thus adhesion of cells to extracellular substrata and matrices. Separate binding domains in fibronectin have been identified for (NH2-end) heparin, collagen, cells, hyaluronic acid, and heparin (COOH-end). Fibronectin binds to C1q in the same manner that it binds collagen and may promote clearance of C1q-coated immune complexes or cellular debris. (from OMIM and NCI)NCI
  • Fibronectin (FN) is involved in many cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion. Fibronectin exists in two main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the ECM (extracellular matrix), and; 2) as a soluble disulphide linked dimer found in the plasma (plasma FN). The plasma form is synthesized by hepatocytes, and the ECM form is made by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin sometimes serves as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates.NCI
code
  • C16581
sameAs
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