Fibbi G, Dini G, Pasquali F, Pucci M, Del Rosso M
Biochim Biophys Acta. 1986 Mar 14;885(3):301-8. doi: 10.1016/0167-4889(86)90245-4.
We have found the existence of specific receptors for the plasminogen activator, urokinase, in A431 human epidermoid carcinoma cells, cultures in plasminogen-free conditions. Two subsets of receptors have been recognized on the basis of 125I-labelled urokinase binding analysis: about 1 X 10(3) high-affinity (Kd = 5.0 X 10(-11) M) and 1 X 10(5) low-affinity (Kd = 9 X 10(-9) M) receptors per cell. The electron microscopic observation of a urokinase: ferritin conjugate has shown single and clustered receptors at the cell surface. Down-regulation of the receptors (T1/2 = 3.77 h) follows the binding of urokinase. The binding does not involve an intact catalytic site and is inhibited by a monoclonal antibody against the Mr 17500 proteolytic fragment of the A chain of urokinase.
我们发现在无纤溶酶原条件下培养的A431人表皮样癌细胞中存在纤溶酶原激活剂——尿激酶的特异性受体。根据¹²⁵I标记的尿激酶结合分析,已识别出两类受体:每个细胞约有1×10³个高亲和力(Kd = 5.0×10⁻¹¹M)受体和1×10⁵个低亲和力(Kd = 9×10⁻⁹M)受体。对尿激酶:铁蛋白结合物的电子显微镜观察显示,细胞表面存在单个和聚集的受体。尿激酶结合后会导致受体下调(半衰期= 3.77小时)。这种结合不涉及完整的催化位点,并且可被针对尿激酶A链Mr 17500蛋白水解片段的单克隆抗体抑制。