Department of Oral Biology, Center for Craniofacial Regeneration, University of Pittsburgh, School of Dental Medicine, Pittsburgh, PA, USA.
J Struct Biol. 2011 Apr;174(1):100-6. doi: 10.1016/j.jsb.2010.11.013. Epub 2010 Nov 23.
Dentin Matrix Protein 1 (DMP1), the essential noncollagenous proteins in dentin and bone, is believed to play an important role in the mineralization of these tissues, although the mechanisms of its action are not fully understood. To gain insight into DMP1 functions in dentin mineralization we have performed immunomapping of DMP1 in fully mineralized rat incisors and in vitro calcium phosphate mineralization experiments in the presence of DMP1. DMP1 immunofluorescene was localized in peritubular dentin (PTD) and along the dentin-enamel boundary. In vitro phosphorylated DMP1 induced the formation of parallel arrays of crystallites with their c-axes co-aligned. Such crystalline arrangement is a hallmark of mineralized collagen fibrils of bone and dentin. Interestingly, in DMP1-rich PTD, which lacks collagen fibrils, the crystals are organized in a similar manner. Based on our findings we hypothesize, that in vivo DMP1 controls the mineral organization outside of the collagen fibrils and plays a major role in the mineralization of PTD.
牙本质基质蛋白 1(DMP1)是牙本质和骨中的重要非胶原蛋白,被认为在这些组织的矿化中发挥重要作用,尽管其作用机制尚未完全阐明。为了深入了解 DMP1 在牙本质矿化中的功能,我们对完全矿化的大鼠切牙进行了 DMP1 的免疫定位,并在存在 DMP1 的情况下进行了体外磷酸钙矿化实验。DMP1 免疫荧光定位于管周牙本质(PTD)和牙本质-釉质边界处。体外磷酸化 DMP1 诱导形成具有平行排列的晶须,其 c 轴共线。这种晶体排列是骨和牙本质矿化胶原纤维的标志。有趣的是,在缺乏胶原纤维的富含 DMP1 的 PTD 中,晶体以类似的方式排列。基于我们的发现,我们假设,DMP1 在体内控制胶原纤维外的矿物质组织,并在 PTD 的矿化中发挥主要作用。