FNIII14 is an inhibitor of cell adhesion and a peptide derived from the 14th type III repeat, which is part of heparin-binding domain 2, of human, mouse, and rat fibronectin.1,2 It inhibits the adhesion of A375-SM melanoma cells to fibronectin-coated plates when used at a concentration of 200 ?g/ml.1 FNIII14 (100 ?g/ml) inhibits the binding of an antibody targeting the active conformation of the fibronectin receptor β1 integrin on K562 cells, which endogenously express integrin α5β1 as its only β1 integrin, and induces the differentiation of ST 13 fibroblasts into adipocytes.2 It decreases atherosclerotic plaque formation in Ldlr-/- mice fed a Western diet.3 FNIII14, in combination with the antitumor antibiotic doxorubicin, reduces metastatic tumor burden in a 4T1 murine mammary model of metastasis.4
References:
[1]. Fukai, F., Hasabe, S., Ueki, M., et al.Identification of the anti-adhesive site buried within the heparin-binding domain of fibronectinJ. Biochem.121(2)189-192(1997).
[2]. Kamiya, S., Kato, R., Wakabayashi, M., et al.Fibronectin peptides derived from two distinct regions stimulate adipocyte differentiation by preventing fibronectin matrix assemblyBiochemistry41(9)3270-3277(2002).
[3]. Iyoda, T., Ohishi, A., Wang, Y., et al.Bioactive TNIIIA2 sequence in tenascin-C is responsible for macrophage foam cell transformation; Potential of FNIII14 peptide derived from fibronectin in suppression of atherosclerotic plaque formationInt. J. Mol. Sci.25(3)1825(2024).
[4]. Iyoda, T., Nagamine, Y., Nakane, Y., et al.Coadministration of the FNIII14 peptide synergistically augments the anti-cancer activity of chemotherapeutic drugs by activating pro-apoptotic bimPLoS One11(9)e0162525(2016).