Fibronectin: Organizing Cell Activity across the ECM

Mon, 07/08/2013 - 12:00

Fibronectin is a glycoprotein found in the extracellular matrix (ECM) that binds to integrins and other components of the ECM such as collagen and fibrin. Under normal physiological conditions, fibronectin is an important factor in cell adhesion, growth, differentiation, and migration. Binding of integrin receptors to fibronectin converts it to an active form, which through interactions with other fibronectin dimers, leads to the formation of a fibrin-fibronectin matrix. Formation of this matrix facilitates epidermal cell migration and proliferation that is required for a number of processes, including wound healing (1, 2). Conversely, under pathophysiological conditions, the fibrin-fibronectin matrix can be disrupted, leading to cell dispersal. Such dispersal resulting from alterations to the fibrin-fibronectin matrix may underlie links between fibronectin and cancer progression. Adipogenic stromal cells in patients with breast cancer, for example, partially unfold the fibronectin matrices, which contributes to mammary tumor angiogenesis and further alters the behavior of the stromal cells (3).

Immunocytochemistry/Immunofluorescence: Fibronectin Antibody Immunocytochemistry/Immunofluorescence: Fibronectin Antibody

Fibronectin plays many other important biological roles.  For instance, fibronectin facilitates the formation of connective tissue by inducing migration and adhesion of fibroblasts to the fibronectin-fibrin matrix.  Accordingly, recent research has exploited this role of the fibronectin-fibrin matrix to aid in arranging biomaterials to facilitate development of synthetic tissues. In addition to the formation of the fibrin-fibronectin matrix, fibronectin itself may bind biomaterials including various polymers and titanium which helps create a microenvironment that is suitable for growth and differentiation of these synthetic tissues (4). This is due to the fact that when fibronectin binds to a cell of any material, the shape of the cell changes to better fit both growth factors and those necessary for differentiation. Fibronectin’s ability to bond with synthetic materials is a result of a similar conformation change that occurs when the protein interacts with the anions that reside on the surface of metals, such as titanium.

  1. PMID: 23742140
  2. PMID:12857786
  3. PMID: 23567798
  4. PMID: 23568025

Novus Biologicals offers various Fibronectin reagents for your research needs including:

Written by Allie Wilson

Blog Topics