Odom A R, Misra U K, Pizzo S V
Department of Pathology, The Duke University Medical Center, Durham, North Carolina 27710, USA.
Biochemistry. 1997 Oct 14;36(41):12395-9. doi: 10.1021/bi970806k.
A previous study demonstrated that activated alpha2-macroglobulin (alpha2M*) binding to the low-density receptor-related protein/alpha2-macroglobulin receptor (LRP/alpha2MR) is blocked by Ni2+ [Hussain, M. M., et al. (1995) Biochemistry 34, 16074-16081]. We now report that the effect of Ni2+ is on a region of the alpha2M molecule upstream of the carboxyl terminal receptor recognition domain. This observation is consistent with previous observations from this laboratory suggesting that alpha2M* binding to LRP/alpha2MR involves a region of the alpha2M molecule immediately upstream of the receptor recognition domain [Enghild, J. J., et al. (1989) Biochemistry 28, 1406-1412]. We further demonstrate that Ni2+ has no effect on the binding of alpha2M* or a cloned and expressed receptor binding fragment (RBF) to the recently described alpha2M signaling receptor as assessed by direct binding and signal transduction studies.
先前的一项研究表明，镍离子（Ni2+）可阻断活化的α2-巨球蛋白（α2M*）与低密度受体相关蛋白/α2-巨球蛋白受体（LRP/α2MR）的结合[侯赛因，M.M.等人（1995年）《生物化学》34卷，第16074 - 16081页]。我们现在报告，Ni2+的作用位点在α2M分子羧基末端受体识别结构域上游的区域。这一观察结果与本实验室先前的观察结果一致，即α2M与LRP/α2MR的结合涉及α2M分子中紧邻受体识别结构域上游的区域[恩希尔德，J.J.等人（1989年）《生物化学》28卷，第1406 - 1412页]。我们进一步证明，通过直接结合和信号转导研究评估，Ni2+对α2M或克隆并表达的受体结合片段（RBF）与最近描述的α2M信号受体的结合没有影响。
