Goldenberg R, Fine R E
Biochim Biophys Acta. 1985 Nov 13;826(2-3):101-7. doi: 10.1016/0167-4781(85)90114-9.
Fragments of the amino-terminal propeptide of procollagen have been shown to inhibit the synthesis of procollagen in cultured cells and in a reticulocyte lysate cell-free system (for review see Timpl, R. and Glanville, R.W. (1981) Clin. Orth. Rel. Res. 158, 224-242). In this report, we show that the full-length amino-terminal propeptide of chick pro alpha1(I) chains inhibits the translation of chick tendon mRNA and rat brain mRNA in a reticulocyte lysate cell-free system. The synthesis of procollagen and non-collagenous proteins was equally affected. Inhibition was dose-dependent up to 10 microM. A similar pattern of inhibition was observed for the collagenase-resistant fragment, col 1(I).
原胶原氨基端前肽片段已被证明可抑制培养细胞和网织红细胞裂解物无细胞系统中原胶原的合成(综述见Timpl, R.和Glanville, R.W. (1981) Clin. Orth. Rel. Res. 158, 224 - 242)。在本报告中,我们表明鸡原α1(I)链的全长氨基端前肽在网织红细胞裂解物无细胞系统中抑制鸡肌腱mRNA和大鼠脑mRNA的翻译。原胶原和非胶原蛋白的合成受到同等影响。抑制作用在高达10微摩尔时呈剂量依赖性。对于抗胶原酶片段col 1(I)也观察到类似的抑制模式。