Abstract

The assembly of discontinuous fibril segments and bundles was studied in 14-day chicken embryo tendons by using serial sections, transmission electron microscopy, and computer-assisted image reconstruction. Fibril segments were first found in extracytoplasmic channels, the sites of their polymerization; they also were found within fibril bundles. Single fibril segments were followed over their entire length in consecutive sections, and their lengths ranged from 7 to 15 microns. Structural differences in the ends of the fibril segments were identified, suggesting that the amino/carboxyl polarity of the fibril segment is reflected in its architecture. Our data indicate that fibril segments are precursors in collagen fibril formation, and we suggest that postdepositional fusion of fibril segments may be an important process in tendon development and growth.

Keywords

FibrilFibrillogenesisCollagen fibrilBiophysicsChemistryTendonCrystallographyTransmission electron microscopyAnatomyMaterials scienceBiologyNanotechnology

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Publication Info

Year
1989
Type
article
Volume
86
Issue
12
Pages
4549-4553
Citations
154
Access
Closed

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David E. Birk, Emanuel Zycband, Donald A. Winkelmann et al. (1989). Collagen fibrillogenesis in situ: fibril segments are intermediates in matrix assembly.. Proceedings of the National Academy of Sciences , 86 (12) , 4549-4553. https://doi.org/10.1073/pnas.86.12.4549

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DOI
10.1073/pnas.86.12.4549