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Journal of Biochemistry Advance Access originally published online on May 28, 2008
Journal of Biochemistry 2008 144(3):343-347; doi:10.1093/jb/mvn072
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© 2008 The Japanese Biochemical Society

ATP-binding on Fibroblast Growth Factor 2 Partially Overlaps with the Heparin-binding Domain

Karsten Rose, Stefanie Pallast, Susanne Klumpp and Josef Krieglstein*

Institut für Pharmazeutische und Medizinische Chemie, Westfälische Wilhelms-Universität Münster, Hittorfstr. 58-62, 48149 Münster, Germany

*To whom correspondence should be addressed. Tel: 049(0)2518332210, Fax: 049(0)2518332211, E-mail: krieglst{at}uni-muenster.de

Received March 13, 2008; Accepted May 20, 2008


  Abstract

Fibroblast growth factor 2 (FGF2), an intensively studied heparin-binding cytokine, is an important modulator of cell growth and differentiation under both physiological and pathophysiological conditions. It has been shown recently that ATP binds to FGF2 and that this binding is crucial for its biological function. In this study we demonstrated that divalent cations were not necessary for binding of ATP to FGF2, but it could be demonstrated that heparin blocked the labelling of FGF2 with ATP indicating an involvement of the heparin-binding domain (aa 128–144) in ATP-binding. FGF2, bound to Heparin Sepharose, could be eluted with ATP and GTP, but not with cAMP, AMP or ADP. Successive mutation of positively charged amino acid residues located in the heparin-binding domain drastically reduced the signal intensity of [{gamma}-32P]ATP labelled FGF2 indicating that this domain is not only important for heparin binding to FGF2 but also for ATP-binding.

Key Words: ATP, bFGF, complex, FGF2, heparin, heparin-binding domain

Abbreviations: ADP, adenosine diphosphate; AMP, adenosine monophosphate; APAF-1, apoptotic protease factor 1; ATP, adenosine triphosphate; DTT, dithiotreithol; GTP, guanosine triphosphate; HSP90, heat shock protein 90; HSPG, heparin sulphate proteoglycans


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