| Surface plasmon resonance analysis to evaluate the importance of heparin sulfate groups' binding with human aFGF and bFGF |
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| 作者姓名： | 吴小锋 许雅香 沈国新 KAMEI Kaeko TAKANO Ryo HARA Saburo |
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| 作者单位： | College of Animal Sciences，Zhejiang University，Huajiachi Campus，College of Animal Sciences，Zhejiang University，Huajiachi Campus，College of Animal Sciences，Zhejiang University，Huajiachi Campus，Department of Applied Biology，Kyoto Institute of Technology，Department of Applied Biology，Kyoto Institute of Technology，Department of Applied Biology，Kyoto Institute of Technology Hangzhou 310029，China，Hangzhou 310029，China，Hangzhou 310029，China，Kyoto 606，Japan，Kyoto 606，Japan，Kyoto 606，Japan |
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| 基金项目： | TheprojectsupportedbytheScientificResearchFoundationforReturnedOverseasChineseScholars，StateEducationMinistryofChinaandZhejiang
ProvincialNaturalScienceFoundationofChina(3 0 13 0 6) |
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| 摘 要： | ＩＮＴＲＯＤＵＣＴＩＯＮＦｉｂｒｏｂｌａｓｔｇｒｏｗｔｈｆａｃｔｏｒ (ＦＧＦ)ｉｓａｎａｎｇｉｏ ｇｅｎｉｃａｎｄｍｉｔｏｇｅｎｉｃｐｏｌｙｐｅｐｔｉｄｅｔｈａｔｃａｎｐｒｏｍｏｔｅｃｅｌｌｐｒｏｌｉｆｅｒａｔｉｏｎａｎｄｄｉｆｆｅｒｅｎｔｉａｔｉｏｎｉｎａｗｉｄｅｖａ ｒｉｅｔｙｏｆｃｅｌｌｔｙｐｅｓ (Ｇｏｌｄｆａｒｂ ,1 990 ;Ｂａｓｉｌｉｃｏｅｔａｌ.,1 992 ) .ＴｈｅＦＧＦｆａｍｉｌｙｈａｓｍａｎｙｍｅｍｂｅｒｓｗｉｔｈｓｉｍｉｌａｒａｍｉｎｏａｃｉｄｓｅｑｕｅｎｃｅａｎｄｂｉｏｌｏｇｉｃａｌａ…
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Surface plasmon resonance analysis to evaluate the importance of heparin sulfate groups' binding with human aFGF and bFGF |
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| WU Xiao feng,XU Ya xiang,SHEN Guo xin,KAMEI Kaeko ,TAKANO Ryo ,HARA Saburo WT.,.BZ.Surface plasmon resonance analysis to evaluate the importance of heparin sulfate groups'''' binding with human aFGF and bFGF[J].Journal of Zhejiang University Science,2003(1). |
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| Authors: | WU Xiao feng XU Ya xiang SHEN Guo xin KAMEI Kaeko TAKANO Ryo HARA Saburo [WT BZ] |
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| Institution: | WU Xiao feng,XU Ya xiang,SHEN Guo xin,KAMEI Kaeko 2,TAKANO Ryo 2,HARA Saburo 2[WT9.,10.BZ] |
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| 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. |
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| Keywords: | Surface plasmon resonance analyses Heparin Sulfate groups Human aFGF and bFGF |
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