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    重组促血液血管生成素以多具体形式促进细胞粘附并与肝素结合

    2016-11-076311点击

     

    分子医学报道 2013 3，7（3）959-64
    重组促血液血管生成素以多具体形式促进细胞粘附并与肝素结合
         促血液血管生成素（HAPO）是一种能够同时刺激造血干细胞和内皮祖细胞增殖的新型生长因子。原核表达的重组人HAPO能够自我组装成分子量约为129kDa的同源四聚体，表现更稳定的促进HESS-5细胞粘附，及比二聚体更高的肝素亲和力。结构域分析表明生长调节素结构域参与分子自我聚集，肝素集合结构域促进四聚体的形成。
     
    延伸： HAPO 是韩忠朝课题组与2004年发现的一种新型的细胞因子，能够同时刺激造血干细胞和血管内皮细胞增殖。深入研究发现HAPO能够抑制白血病细胞凋亡；基因转染HAPO的基质细胞造血支持作用加强；可以延长化疗小鼠生存期。该课题组进行了原核表达HAPO，制备了抗HAPO的多克隆抗体及单克隆抗体。HAPO的生理意义及药用价值仍然有待进一步研究。
     
    参考文献

    1: Wang LF, Han ZB, Li M, Yang P, Xv B, Zhang JP, Han ZC. Recombinant 

    hemangiopoietin promotes cell adhesion and binds heparin in its multimeric form. Mol Med Rep. 2013 Mar;7(3):959-64. 
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    Mol Med Rep. 2013 Mar;7(3):959-64. doi: 10.3892/mmr.2013.1274. Epub 2013 Jan 15.
    Recombinant hemangiopoietin promotes cell adhesion and binds heparin in its multimeric form.
    Wang LF, Han ZB, Li M, Yang P, Xv B, Zhang JP, Han ZC.
    Source
    Department of Basic Medicine, Zhejiang Medical College, Hangzhou 310053, PR China.
    Abstract
    Hemangiopoietin (HAPO) is a novel growth factor stimulating the proliferation of hematopoietic and endothelial progenitor cells in vitro and in vivo. The native protein is a 294‑amino acid multimodular protein. The N‑terminus constitutes of two somatomedin B (SMB) homology domains that contain 14 cysteines. The central region is a putative heparin‑binding domain (pHBD) and the C‑terminus contains mucin‑like repeats. In the present study, we demonstrated that prokaryotic recombinant human HAPO (rhHAPO) self‑associates into a multimeric form with a mass weight of ~129 kDa, suggesting a homologous tetramer. rhHAPO in its multimeric form was found to be more stable and more potent in promoting HESS‑5 cell adhesion. Multimeric rhHAPO had a higher affinity to heparin compared with its dimeric form, although there was no significant conformational change. C‑terminal repeats-truncated rhHAPO (rhHAPOΔmucin) was also found to be assembled into a multimer, while deletion of pHBD (rhHAPOΔmucin‑pHBD) caused the protein to remain in a dimeric form, demonstrating that SMB domains participate in self‑aggregation of the molecule and that the pHBD region promotes the tetramerization.

     

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