Laffont-Proust Isabelle, Faucheux Baptiste A, Hässig Raymonde, Sazdovitch Véronique, Simon Stéphanie, Grassi Jacques, Hauw Jean-Jacques, Moya Kenneth L, Haïk Stéphane
INSERM Avenir Team - Human Prion Diseases, IFR70, Neuropathology, Salpêtrière Hospital, F-75013 Paris, France.
FEBS Lett. 2005 Nov 21;579(28):6333-7. doi: 10.1016/j.febslet.2005.10.013. Epub 2005 Oct 19.
Human brain cellular prion protein (PrP(c)) is cleaved within its highly conserved domain at amino acid 110/111/112. This cleavage generates a highly stable C-terminal fragment (C1). We examined the relative abundance of holo- and truncated PrP(c) in human cerebral cortex and we found important inter-individual variations in the proportion of C1. Neither age nor postmortem interval explain the large variability observed in C1 amount. Interestingly, our results show that high levels of C1 are associated with the presence of the active ADAM 10 suggesting this zinc metalloprotease as a candidate for the cleavage of PrP(c) in the human brain.
人脑海绵状蛋白（PrP(c)）在其110/111/112位氨基酸的高度保守结构域内被切割。这种切割产生了一个高度稳定的C末端片段（C1）。我们检测了人大脑皮质中完整型和截短型PrP(c)的相对丰度，发现C1比例存在重要的个体间差异。年龄和死后间隔时间均无法解释所观察到的C1含量的巨大变异性。有趣的是，我们的结果表明，高水平的C1与活性ADAM 10的存在相关，提示这种锌金属蛋白酶是人脑海绵状蛋白切割的候选酶。
