Instability restricts signaling of multiple fibroblast growth factors

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Authors

BUCHTOVÁ marcela CHALOUPKOVÁ Radka ZAKRZEWSKA Malgorzata VESELÁ Iva CELÁ Petra BARÁTHOVÁ Jana GUDERNOVÁ Iva ZAJICKOVA Renata TRANTÍREK Lukáš MARTIN Jorge KOSTAS Martin OTLEWSKI Jacek DAMBORSKÝ Jiří KOZUBÍK Alois WIEDLOCHA Antoni KREJČÍ Pavel

Year of publication 2015
Type Article in Periodical
Magazine / Source Cellular and Molecular Life Sciences
MU Faculty or unit

Faculty of Medicine

Citation
Web http://www.ncbi.nlm.nih.gov/pubmed/25854632
Doi http://dx.doi.org/10.1007/s00018-015-1856-8
Field Genetics and molecular biology
Keywords Fibroblast growth factor; FGF; Unstable; Proteoglycan; Regulation
Attached files
Description Fibroblast growth factors (FGFs) deliver extracellular signals that govern many developmental and regenerative processes, but the mechanisms regulating FGF signaling remain incompletely understood. Here, we explored the relationship between intrinsic stability of FGF proteins and their biological activity for all 18 members of the FGF family. We report that FGF1, FGF3, FGF4, FGF6, FGF8, FGF9, FGF10, FGF16, FGF17, FGF18, FGF20, and FGF22 exist as unstable proteins, which are rapidly degraded in cell cultivation media. Biological activity of FGF1, FGF3, FGF4, FGF6, FGF8, FGF10, FGF16, FGF17, and FGF20 is limited by their instability, manifesting as failure to activate FGF receptor signal transduction over long periods of time, and influence specific cell behavior in vitro and in vivo. Stabilization via exogenous heparin binding, introduction of stabilizing mutations or lowering the cell cultivation temperature rescues signaling of unstable FGFs. Thus, the intrinsic ligand instability is an important elementary level of regulation in the FGF signaling system.
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