Fibronetiinin

Fibronetiinin is a term occasionally encountered in older biomedical literature, though it is generally regarded as a misspelling or variant of the glycoprotein fibronectin. Fibronectin itself is a high‑molecular‑weight extracellular matrix protein that plays a key role in cell adhesion, wound healing, embryonic development, and the maintenance of the structural integrity of tissues. It is composed of two identical 250‑kDa subunits linked by disulfide bonds, and the protein is highly conserved across a wide range of vertebrate species.

The functional domains of fibronectin include binding sites for integrins, collagen, heparin, and fibrin, which enable it to act as a scaffold for cell interaction and signaling. It is secreted by a variety of cell types, including fibroblasts, macrophages, and vascular endothelial cells, and is present in large quantities in plasma and in the extracellular matrix of many tissues.

While most contemporary references use the name fibronectin, some older sources and a handful of niche studies refer to “fibronetiinin” when discussing the same protein, often in the context of early polymerization assays or tissue culture experiments. The confusion may stem from typographical errors or from the use of alternative nomenclature in early biochemical texts. In current practice, fibronectin is the accepted term in peer‑reviewed journals, clinical guidelines, and protein databases such as UniProt (accession number P02751).