期刊
JOURNAL OF STRUCTURAL BIOLOGY
卷 132, 期 3, 页码 212-225出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1006/jsbi.2000.4320
关键词
biomineralization; dentin; collagen; cryo-microscopy; rat incisor; phosphophoryn
资金
- NIDCR NIH HHS [DE01374, DEO6954] Funding Source: Medline
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. (C) 2000 Academic Press.
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