What is the Difference Between Fibronectin and Vitronectin?

🆚 Go to Comparative Table 🆚

Fibronectin and vitronectin are both cell adhesive glycoproteins found in the extracellular matrix, but they have different molecular weights and functions. The key differences between fibronectin and vitronectin include:

  1. Molecular Weight: Fibronectin is a high molecular weight glycoprotein, while vitronectin is a low molecular weight glycoprotein.
  2. Location: Fibronectin is found in the interstitial matrix and plasma, while vitronectin is found in serum, extracellular matrix, and bone.
  3. Cell Adhesion: Fibronectin mainly functions in cell migration during development and wound healing, with cell adhesion mediated by RGD (Arg-Gly-Asp) sequences on the fibronectin strand, which are recognized by α5β1 and αVβ3 integrins for binding. Vitronectin, on the other hand, has been found to support human embryonic stem cell (hESC) self-renewal.
  4. Disease Associations: Altered expression, degradation, and organization of fibronectin have been associated with various diseases such as cancer, arthritis, and fibrosis, while altered expression of vitronectin has been involved in diseases such as tumor malignancy.

Both fibronectin and vitronectin are known to support cell adhesion, and they both bind to a cell surface receptor called "integrin".

Comparative Table: Fibronectin vs Vitronectin

Here is a table comparing the differences between fibronectin and vitronectin:

Feature Fibronectin Vitronectin
Molecular Weight High molecular weight Low molecular weight
Location Plasma and extracellular matrix Serum, extracellular matrix, and bone
Cell Surface Receptors Binds to integrin alpha-Vbeta-3 Binds to integrin alpha-Vbeta-3
Other Ligands - Binds to several serine protease inhibitors like serpins
Protein Forms Single-chain form or two chains held together by a disulfide bond Single protein
Involvement in Tumor Malignancy Speculated to be involved Speculated to be involved

Both fibronectin and vitronectin are cell adhesive proteins, glycoproteins, and they both bind to a cell surface receptor called "integrin". They are present in the extracellular matrix, and the altered expression of both proteins can lead to cancer.