Godár S, Horejsi V, Weidle U H, Binder B R, Hansmann C, Stockinger H
Institute of Immunology, Vienna International Research Cooperation Center at NFI, University of Vienna, Austria.
Eur J Immunol. 1999 Mar;29(3):1004-13. doi: 10.1002/(SICI)1521-4141(199903)29:03<1004::AID-IMMU1004>3.0.CO;2-Q.
Transforming growth factor-beta1 (TGF-beta1) is a critical cytokine for cell proliferation and differentiation. It is secreted by many cells in a latent pro-form (LTGF-beta1) from which biologically active TGF-beta1 is released by an in vivo mechanism that is not known. Here we show that the mannose-6-phosphate/insulin-like growth factor II-receptor (M6P/IGFII-R), which binds LTGF-beta1, complexes with urokinase (plasminogen activator)-receptor (uPA-R) on the surface of human monocytes and directly binds plasminogen (Plg). Plasmin generated from Plg in the complex mediates release of TGF-beta1 when M6P/IGFII-R is associated with uPA-R. Thus, this interaction of M6P/IGFII-R and uPA-R suggests a potential mechanism for the generation of TGF-beta1 by cells.
转化生长因子-β1（TGF-β1）是细胞增殖和分化的关键细胞因子。它由许多细胞以无活性前体形式（LTGF-β1）分泌，目前尚不清楚其在体内激活产生生物活性TGF-β1的机制。在此，我们发现与LTGF-β1结合的甘露糖-6-磷酸/胰岛素样生长因子II受体（M6P/IGFII-R），可与人单核细胞表面的尿激酶（纤溶酶原激活物）受体（uPA-R）形成复合物，并直接结合纤溶酶原（Plg）。当M6P/IGFII-R与uPA-R结合时，复合物中由Plg产生的纤溶酶可介导TGF-β1的释放。因此，M6P/IGFII-R与uPA-R的这种相互作用提示了细胞产生TGF-β1的潜在机制。
