Rabbani S A, Desjardins J, Bell A W, Banville D, Mazar A, Henkin J, Goltzman D
Department of Physiology, McGill University, Montreal, Quebec, Canada.
Biochem Biophys Res Commun. 1990 Dec 31;173(3):1058-64. doi: 10.1016/s0006-291x(05)80893-9.
A peptide mitogen for cultured osteoblast-like cells was purified from serum-free conditioned culture medium of a human prostatic cancer cell line, PC-3. Based on amino acid sequencing and estimated molecular weight, this peptide was identified as an NH2-terminal fragment of urokinase-type plasminogen activator (uPA). Recombinant high molecular weight (HMW) uPA and the NH2-terminal growth factor domain (GFD) of uPA, but not low molecular weight (LMW) uPA (lacking the NH2-terminal region) stimulated [3H] thymidine incorporation and proliferation in osteoblast-like cells, and specific, competitive binding sites for HMW, but not LMW, uPA were demonstrable. These studies demonstrate the production of a mitogenic NH2-terminal fragment of uPA by a human prostatic cancer cell line which may be of importance in the pathogenesis of osteoblastic metastases.
从人前列腺癌细胞系PC-3的无血清条件培养基中纯化出一种用于培养成骨样细胞的肽类促有丝分裂原。根据氨基酸序列和估计的分子量，该肽被鉴定为尿激酶型纤溶酶原激活剂（uPA）的NH2末端片段。重组高分子量（HMW）uPA和uPA的NH2末端生长因子结构域（GFD），但不是低分子量（LMW）uPA（缺乏NH2末端区域）刺激成骨样细胞中的[3H]胸苷掺入和增殖，并且可证明存在针对HMW uPA而非LMW uPA的特异性、竞争性结合位点。这些研究表明人前列腺癌细胞系产生了uPA的促有丝分裂NH2末端片段，这可能在成骨性转移的发病机制中具有重要意义。
