Collagen fibrillogenesis in situ: fibril segments are intermediates in matrix assembly.
Author(s) -
David E. Birk,
Emanuel Zycband,
Donald A. Winkelmann,
Robert L. Trelstad
Publication year - 1989
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.86.12.4549
Subject(s) - fibril , fibrillogenesis , collagen fibril , biophysics , chemistry , tendon , crystallography , transmission electron microscopy , anatomy , materials science , biology , nanotechnology
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.
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