CLC number: Q617
On-line Access: 2024-08-27
Received: 2023-10-17
Revision Accepted: 2024-05-08
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WU Xiao-feng, XU Ya-xiang, SHEN Guo-xin, KAMEI Kaeko, TAKANO Ryo, HARA Saburo. Surface plasmon resonance analysis to evaluate the importance of heparin sulfate groups' binding with human aFGF and bFGF[J]. Journal of Zhejiang University Science A, 2003, 4(1): 86-94.
@article{title="Surface plasmon resonance analysis to evaluate the importance of heparin sulfate groups' binding with human aFGF and bFGF",
author="WU Xiao-feng, XU Ya-xiang, SHEN Guo-xin, KAMEI Kaeko, TAKANO Ryo, HARA Saburo",
journal="Journal of Zhejiang University Science A",
volume="4",
number="1",
pages="86-94",
year="2003",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.2003.0086"
}
%0 Journal Article
%T Surface plasmon resonance analysis to evaluate the importance of heparin sulfate groups' binding with human aFGF and bFGF
%A WU Xiao-feng
%A XU Ya-xiang
%A SHEN Guo-xin
%A KAMEI Kaeko
%A TAKANO Ryo
%A HARA Saburo
%J Journal of Zhejiang University SCIENCE A
%V 4
%N 1
%P 86-94
%@ 1869-1951
%D 2003
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.2003.0086
TY - JOUR
T1 - Surface plasmon resonance analysis to evaluate the importance of heparin sulfate groups' binding with human aFGF and bFGF
A1 - WU Xiao-feng
A1 - XU Ya-xiang
A1 - SHEN Guo-xin
A1 - KAMEI Kaeko
A1 - TAKANO Ryo
A1 - HARA Saburo
J0 - Journal of Zhejiang University Science A
VL - 4
IS - 1
SP - 86
EP - 94
%@ 1869-1951
Y1 - 2003
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.2003.0086
Abstract: Human acidic and basic fibroblast growth factors (aFGF and bFGF) are classic and well characterized members of the heparin-binding growth factor family. heparin is generally thought to play an extremely important role in regulating aFGF and bFGF bioactivities through its strong binding with them. In order to unravel the mechanism of the interactions between heparin and FGFs, and evaluate the importance of heparin sulfate groups' binding with FGFs, surface plasmon resonance analyses were performed using IAsys Cuvettes System. heparin and its regioselectively desulfated derivatives were immobilized on the cuvettes. aFGF and bFGF solutions with different concentrations were pipetted into the cuvettes and the progress of the interaction was monitored in real-time by Windows-based software, yielding kinetic and equilibrium constants for these interactions. In addition, in order to reduce the delicate difference among the cuvettes, inhibition analyses of mixture of FGFs and immobilized native heparin by modified heparins were also done. The data from these two methods were similar, indicating that all sulfate groups at 2-O, 6-O and N- in heparin were required for the binding to aFGF; and that their contribution to the binding was in the order 2-O, N- and 6-O-sulfate group. In contrast, definite contribution of the 6-O-sulfate group to the binding with bFGF was most apparent, while the other two sulfate groups appeared to be necessary in the order 2-O and N-sulfate group. These methods established here can be used for analysing the effect of sulfate groups in heparin on the binding with other human FGF members or other heparin-binding proteins.
[1]Basilico,C. and Moscatelli,D., 1992. The FGF family of growth factors and oncogenes. Adv. Cancer Res. 59: 115-165.
[2]Conrad,H.E., 1997. Heparin-binding proteins. Academic Press, New York, p.302-493.
[3]Fagerstam, L.G., Frostell, A., Karlsson, R., Kullman, M., Malmqvist M. and Butt, H.,1990. Detection of antige N-antibody interactions by surface plasmon resonance: application to epitope mapping. J.Mol. Recogn, 3: 208.
[4]Fernig, D.G. and Gallagher, J.T., 1994. Fibroblast growth factors: an information network controlling tissue growth, morphogenesis and repair. Prog. Growth Factor Res, 5: 353-377.
[5]Goldfarb,M., 1990. The fibroblast growth factor family. Cell growth and differentiation. 1: 439-445.
[6]Hakan,A., IIknur,A., Awlter,J.K. and Seth, P. F., 1999. Potential usefulness of basic fibroblast growth factor as a treatment for stroke. Cerebrovasc Dis, 9: 131-135.
[7]Ishihara,M., Takano, R., Kanda, T., Hayashi, K., Hara, S., Kikuchi, H. and Yoshida, K., 1995. Importance of 6-O-sulfate groups of glucosamine residues in heparin for activation of FGF-1 and FGF-2. J. Biochem, 118: 1255-1260.
[8]Ishihara,M., Kariya,Y., Kikuchi,H., Minamisawa, T. and Yoshida, K., 1997. Importance of 2-O-sulfate groups uronate residues in heparin for activation of FGF-1 and FGF-2. J. Biochem, 121: 345-349.
[9]Liedberg,B., Nylander,C. and Lundstrom,I., 1983. Surface plasmon resonance for gas detection and biosensing. Sens. Actuators, 4: 299.
[10]Mayo,C.S. and Hallock,R.B., 1989. Immunoassay based on surface plasmon oscillations. J. Imm/Lunol. Methods, 120: 105.
[11]Minami,K., 1999. Kinetic measurement of the interaction between rTFPI and chemically modified heparins by means of surface plasmon resonance. (private corresponse)
[12]Myszka,D.G., 1997. Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensor. Current opinion in biotechnology. 8: 50-57.
[13]Sasaki,H., Hayashi,A., Kitagaki-Ogawa,H., Matsumoto,I. and Seno, N., 1987 Improved method for the immobilization of heparin. J. Chromatogr, 400: 123-132.
[14]Shane, R. B., Robert, J. B., David, A. E., Ajay, R. and Volkhard, L., 1999. Vascular remodeling in response to altered blood flow is mediated by fibroblast growth factor-2. Circulation Research, 84: 323-328.
[15]Sun,L., Xu,L., Chang,H., Henry,F.A., Miller,R.M., Harmon,J.M. and Nielsen,T.B., 1997. Transfection with aFGF cDNA improves wound healing. J.Investigative Dermatology,313-318.
[16]Ueda,T., Tsurumaru, M. and Imoto, T., 1998. Kinetic measurement of the interaction between a lysozyme and its immobilized substrate analogue by means of surface plasmon resonance. J. Bioche, 124: 712-716.
[17]Wu Xiaofeng, Kamei Kaeko, Sato Hideki, Sato Shin-ichi, Takano Ryo, Ichida Masatoshi, Mori Hajime and Hara Saburo., 2001. High-level expression of human acidic and basic fibroblast growth factors in the silkworm, Bombyx mori L. using recombinant baculovirus. Protein Expression and Purification, 21(1): 192-200.
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