Fibronectins proteins

D3. De Petro, G., Tavian, D., Mrchina, E., and Barlati, S., Induction of fibronectin mRNA by urokinase- and tissue-type plasminogen activator in human skin fibroblasts Differential role of u-PA and t-PA at the fibronectin protein level. Biol. Chem. 383, 177-187 (2002). 

Protein hydrolysates, fibronectin. See Hydrolyzed fibronectin Protein hydrolysates, leather, N,N-diethyl, diethyl sulfate, quatemized. See Triethonium hydrolyzed collagen ethosulfate Protein hydrolysates, leather, reaction prods, with (3-chloro-2-hydroxypropyl) trimethylammonium chlorides. See Hydroxypropyltrimonium hydrolyzed collagen Protein hydrolysates, leather, reaction prods, with isooctadecanoyl chloride. See Isostearoyl hydrolyzed collagen... 

Alginate microparticles that deliver VEGF and MCP-1 with distinct release kinetics and that can be integrated into a collagen/fibronectin (protein) gel construct for delivery of endothelial cells have been proposed by Jay et al. (2010). Combined delivery of VEGF and MCP-1 increased functional vessel formation and also led to a higher number of smooth muscle cell-invested vessels. 

Leahy, D.J., Hendrickson, W.A., Aukhil, A., Erickson, H.P. 5tructure of a fibronectin type II domain from tenascin phased by MAD analysis of the selenome-thionyl protein. Science 258 987-991, 1992. 

C, which is found in complement proteins FI, F2, and F3, first found in fibronectin I, the immunoglobulin superfamily domain N, found in some growth factor receptors E, a module homologous to the calcium-binding E-F hand domain and LB, a lectin module found in some cell surface proteins. (Adapted from Baron, M., Norman, D., and Campbell, I., 1991, Protein modnles. Trends in Biochemical Sciences 16 13—1 7.)... 

Protein lateral motion is much slower than that of lipids because proteins are larger than lipids. Also, some membrane proteins can diffuse freely through the membrane, whereas others are bound or anchored to other protein structures in the membrane. The diffusion constant for the membrane protein fibronectin is approximately 0.7 X 10 cmVsec, whereas that for rhodopsin is about 3 X 10 cmVsec. 

Cue D, Southern S, Southern P et al (2000) A non-peptide integrin antagonist can inhibit epithelial cell ingestion of streptococcus pyogenes by blocking a5 31 -fibronectin-Ml protein complexes. Proc Nat Acad Sci 97(6) 2858-2863... 

It is of interest that proteins termed motility factors (55-70 kD) are secreted by fetal cells and some tumor cells. These proteins act as autocrine factors and stimulate rapid movement by these cells. Motility factors induce the formation of cell processes that are packed with actin filaments and have an increased number of receptors for the matrix proteins laminin and fibronectin. The latter enhance the ability of the cells to bind to the extracellular matrix. Thus, it is likely that motility factors influence the organization of the cytoskeleton through changes taking place at the cell surface (reviewed by Warn and Dowrick, 1989). 

Kim J. Han L Kim Y. et al. C-terminal heparin-binding domain of fibronectin regulates integrin-mediated cell spreading but not the activation of mitogen-activated protein kinase / / Biochem. J. 2001. V. 360. P. 239-245. 

Figure 48-5. Schematic representation of fibronectin interacting with an integrin fibronectin receptor situated in the exterior of the plasma membrane of a cell of the ECM and of various attachment proteins interacting indirectly or directly with an actin microfilament in the cytosol. For simplicity, the attachment proteins are represented as a complex.

Have specific interactions with collagen, elastin, fibronectin, laminin, and other proteins such as growth factors... 

The major components of the ECM are the structural proteins collagen, elastin, and fibrihin a number of specialized proteins (eg, fibronectin and laminin) and various proteoglycans. 

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