Fibroblast Growth Factors and Their Receptors

The interactions of HS withFGFs involve primarily the NS-domains (see Fig. 2) of the polysaccharide. Biochemical analyses of FGF2 interactions with heparin and HS oligosaccharides implicated a I-Ans-I-Ans-I2s pentasaccharide sequence (for symbols, see Fig. 1 reducing terminus to the right), notably lacking any 6-G-sulfatc groups, as the smallest and least sulfated structure capable 

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Wilkie, A.O.M., Morriss-Kay, G.M., Jones, E.Y., Heath, J.K. (1995). Functions of fibroblast growth factors and their receptors. Curr. Biol. 5, 500-507. 

E. Moroni, P. Dell Era, M. Rusnati, and M. Presta, Fibroblast growth factors and their receptors in hematopoiesis and hematological tumors, J Hematother Stem Cell Res 11, 19-32 (2002). 

Baird, A. and Bbhien, P. (1990) Fibroblast growth factors. In M.B. Sporn and A.B. Roberts (Eds.), Peptide Growth Factors and Their Receptors, Handbook Experimental Pharmacology 95 (/), Springer Verlag, Heidelberg, pp. 369-418. 

Imbalanced expression of pro- and antiangiogenic factors and their receptors on EC may determine the development or regression of new blood vessels. More than 200 pro-angiogenic factors have been identified. Among those, the most important factors include vascular endothelial growth factor (VEGF), fibroblast growth factor (FGF),... 

Powers, C.J., McLeskey, S.W., and Wellstein, A. 2000. Fibroblast growth factors, their receptors and signalling. Endocrine Related Cancer 1(3), 165-197. 

Powers, C. et. al. (2000). Fibroblast growth factors, their receptors and signalling. Endocr. Rel. Cancer 7(3), 165-197. Souchelnytskyi, S. (2002). Transforming growth factor-/) signalling and its role in cancer. Exp. Oncol. 24(1), 3-12. Zhu, X., Komiya, A., Chirino, S. et al. (1991). Three-dimensional structures of acidic and basic fibroblast growth factors. Science 251, 90. 

Does defective lysosomal catabolism in I-cell disease somehow feed back to affect the expression of lysosomal proteins and their receptors Compared with control fibroblasts, twofold increases in man-6-P/IGF-II receptors have been observed for fibroblasts from patients with I-cell disease. This increase in receptor concentration stems from an increased rate of synthesis, not from differences of receptor stability. Interestingly, when they are exposed to insulinlike growth factors I and II or tumor-promoting phorbol esters, I-cell fibroblasts respond differently from control fibroblasts. These observations indicate multiple regulatory sites in the man-6-P/IGF-II receptor pathway. 

Another aspect of lipid-protein interaction that is conve-luently studied in supported bilayers is the lateral diffusion of proteins and lipids and their influence on each other. The regulatory lipid phosphatidyl-inositol-biphosphate (PIP2) slows the diffusion of syntaxin in supported bilayers (37). Conversely, increasing syntaxin concentrations decrease the diffusion of PIP2 and to a lesser extent that of phosphatidylserine. In another system, in which the transmembrane domain of the fibroblast growth factor receptor was incorporated into supported bilay-ers, lipid and protein diffusion were measured (60). Although protein diffusion was slow (0.006 ttm /s), lipid diffusion was fast (2.6 ttm /s). 

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