Identification and partial characterization of receptor binding sites for HGF on rat hepatocytes.
Identification and partial characterization of receptor binding sites for HGF on rat hepatocytes.
复制标题
大鼠肝细胞上 HGF 受体结合位点的鉴定和部分表征。
DOI：
10.1016/s0006-291x(05)80910-6
复制
发表时间：
1990
影响因子：
3.1
通讯作者：
Michalopoulos,G
中科院分区：
文献类型：
--
作者：
Zarnegar,R;DeFrances,MC;Oliver,L;Michalopoulos,G
肝细胞生长因子（HGF）(也称为肝生成素A [HPTA]（1-9）是肝细胞的异二聚体肝素结合多肽丝裂原，不同于其他已知的生长因子。在这项研究中，生物活性放射性碘化HGF被用于鉴定培养的完整肝细胞上的结合位点。结果表明，由于肝素或肝素样分子的存在，在完整肝细胞的细胞表面存在相对低亲和力的结合位点和高亲和力的特异性受体结合位点。结合数据的Scatchard分析表明，细胞表面受体的表观解离常数（Kd）为3.5 nM，每个肝细胞有120,000个位点。非还原条件下，SDS-PAGE对亲和交联125i - hgf受体复合物进行分析，发现存在明显Mr为23万的条带。这些数据表明，HGF通过一种特异性和独特的细胞表面受体对肝细胞发挥其生物学作用（刺激DNA合成）。
Hepatocyte Growth Factor (HGF) (also known as Hepatopoietin A [HPTA] (1–9) is a heterodimeric heparin-binding polypeptide mitogen for hepatocytes distinct from other well-known growth factors. In this study, biologically active radioiodinated HGF was used to identify binding sites on intact hepatocytes in culture. The results show the presence of relatively low affinity binding sites due to the presence of heparin or heparin-like molecules and high affinity specific receptor binding sites on the cell surface of intact hepatocytes. Scatchard analysis of binding data indicates an apparent dissociation constant (Kd) of 3.5 nM with 120,000 sites per hepatocyte for the cell-surface receptor. Analysis of affinity cross-linked125I-HGF-receptor complex by SDS-PAGE under non-reducing conditions reveals the presence of a distinct band with apparent Mr of 230,000. These data show that HGF exerts its biological effect on hepatocytes (stimulation of DNA synthesis) through a specific and unique cell-surface receptor.