Quantitative electron-spectroscopic diffraction (ESD) and electron-spectroscopic imaging (ESI) analyses of dentine mineralisation in rat incisors

被引:9
作者
Arnold, S [1 ]
Plate, U [1 ]
Wiesmann, HP [1 ]
Kohl, H [1 ]
Hohling, HJ [1 ]
机构
[1] UNIV MUNSTER, INST MED PHYS & BIOPHYS, D-48149 MUNSTER, GERMANY
关键词
electron-spectroscopic imaging; electron-spectroscopic diffraction; dentine; biomineralization; crystal nuclei; incremental lines; noncollagenous proteins; rat; (Wistar; Sprague Dawley);
D O I
10.1007/s004410050805
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Primary crystal formations in all hard tissues are, according to our investigations, Ca-phosphate chains composed of nanometer sized particles (dots) which develop along the matrix macromolecules. In circumpulpal dentine the centre-to-centre distances between the dots inside the chains reflect the distances between the crystal nucleating sites (''active sites'') along the collagen matrix macromolecule. The centre-to-centre distances at the surface of the mineralised collagen fibrils probably reflect the distances between nucleating sites of noncollagenous proteins attached to collagen. These needle-like chains of dots coalesce in lateral directions to form ribbon-like crystallites. The morphological results are supported by correlated small area diffraction studies in the same regions of dentine. We have found that the first appearing Bragg-reflection has a lattice spacing value of 0.388 nm, which corresponds to the (111) apatite value. For the earliest crystal formations the intensity of the (002) reflection is higher than that of the (300)-reflection A maximum of the net-signal-intensity ratio of the (002) to (300) Bragg-reflection appears at the mineralisation front. This peak repeats with decreasing height 3 to 5 times with a distance range of about 8-16 mu m through the whole dentine zone, which corresponds to the distances of the incremental lines, called ''von Ebner lines''.
引用
收藏
页码:185 / 190
页数:6
相关论文
共 47 条
  • [1] ARENA J, 1992, P 50 ANN M EMSA, P582
  • [2] ARNOLD S, 1995, EUR J CELL BIOL, V67, P108
  • [3] ARNOLD S, 1994, THESIS MUNSTER
  • [4] ARNOLD S, 1993, EUR J CELL BIOL S39, V61, P105
  • [5] BONAR LC, 1991, J BONE MINER RES, V6, P1167
  • [6] BONAR LC, 1985, CHEM BIOL MINERALIZE, P226
  • [7] BONUCCI E, 1985, ULTRASTRUCTURE CONNE, P165
  • [8] BOYDE A, 1974, CELL TISSUE RES, V152, P543
  • [9] FRATZL P, 1992, J BONE MINER RES, V7, P329
  • [10] FUJISAWA R, 1992, CALCIFIED TISSUE INT, V51, P438