Abstract:
:The assembly of the collagenous organic matrix prior to mineralization is a key step in the formation of bones and teeth. This process was studied in the predentin of continuously forming rat incisors, using unstained vitrified ice sections examined in the transmission electron microscope. Progressing from the odontoblast surface to the mineralization front, the collagen fibrils thicken to ultimately form a dense network, and their repeat D-spacings and banding patterns vary. Using immunolocalization, the most abundant noncollagenous protein in dentin, phosphophoryn, was mapped to the boundaries between the gap and overlap zones along the fibrils nearest the mineralization front. It thus appears that the premineralized collagen matrix undergoes dynamic changes in its structure. These may be mediated by the addition and interaction with the highly anionic noncollagenous proteins associated with collagen. These changes presumably create a collagenous framework that is able to mineralize.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
Beniash E,Traub W,Veis A,Weiner Sdoi
10.1006/jsbi.2000.4320keywords:
subject
Has Abstractpub_date
2000-12-01 00:00:00pages
212-25issue
3eissn
1047-8477issn
1095-8657pii
S1047-8477(00)94320-Xjournal_volume
132pub_type
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abstract::Trypsin treatment of staphylococcal alpha-toxin cleaves the molecule into two roughly equally sized parts, which results in inactivation of the toxin. Tetragonal arrays of oligomers, closely resembling the native ones, can however be formed on lipid layers. From tilted views of negatively stained crystals a 3D structu...
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pub_type: 杂志文章
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