INTERACTION OF ENDOTHELIAL-CELL GROWTH-FACTOR WITH HEPARIN - CHARACTERIZATION BY RECEPTOR AND ANTIBODY RECOGNITION
INTERACTION OF ENDOTHELIAL-CELL GROWTH-FACTOR WITH HEPARIN - CHARACTERIZATION BY RECEPTOR AND ANTIBODY RECOGNITION
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DOI：
10.1073/pnas.82.18.6138
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发表时间：
1985-01-01
影响因子：
11.1
通讯作者：
MACIAG, T
中科院分区：
文献类型：
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作者：
SCHREIBER, AB;KENNEY, J;MACIAG, T
内皮细胞生长因子（ECGF）在体外特异性结合存在于几种细胞类型（包括鼠和人内皮细胞和成纤维细胞）表面上的膜受体。针对ECGF制备的抑制生长因子的促有丝分裂活性的单克隆抗体阻止配体对受体的占据。肝素在结构上与ECGF相互作用[Maciag，T.，Mehlman，T.，弗里吉尔河和Schreiber，A.B.（1948）Science 225，932-935]，增强多肽的促有丝分裂活性，恢复对ECGF的生物活性，增强配体对细胞表面受体的亲和力，并改变ECGF的抗体识别。这些数据表明，肝素和ECGF之间的关联诱导的多肽，增加或稳定的有丝分裂原的生物活性的构象变化。
Endothelial cell growth factor (ECGF) binds specifically in vitro to membrane receptors present on the surface several cell types, including murine and human endothelial cells and fibroblasts. Monoclonal antibodies prepared against ECGF that inhibit the mitogenic activity of the growth factor prevent receptor occupancy by the ligand. Heparin interacts structurally with ECGF [Maciag, T., Mehlman, T., Friesel, R. and Schreiber, A.B. (1948) Science 225, 932-935], potentiates the mitogenic activity of the polypeptide, restores the biological activity to inactivate ECGF, enhances the affinity of the ligand to cell surface receptors, and modifies antibody recognition of ECGF. These data suggest that the association between heparin and ECGF induces a conformational change in the polypeptide that increases or stablizes the biological activity of the mitogen.