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Image analysis of tendon helical superstructure using interference and polarized light microscopy.
1Department of Cell Biology, Institute of Biology, State University of Campinas (UNICAMP), P.O. Box 6109, CEP 13084-971 Campinas, SP, Brazil. vidal@obelix.unicamp.br
Micron (Oxford, England : 1993)
|December 19, 2003
Summary
Collagen bundles in tendons form a helical superstructure, not planar wave-like structures (WLS). This helical organization, supported by microscopy, reclassifies WLS as a twisted grain boundary.
Area of Science:
- Biophysics
- Materials Science
- Supramolecular Chemistry
Background:
- Wave-like structures (WLS), or crimp, in tendons are traditionally viewed as planar.
- Supramolecular chemistry principles suggest a helical arrangement for collagen bundles is more plausible.
Purpose of the Study:
- To provide further evidence supporting a helical superstructure for collagen bundles within tendons.
- To investigate the structural organization of WLS using advanced microscopy techniques.
Main Methods:
- Cryosections of bovine tendons and resin-embedded rat tail tendons were examined.
- Polarized light, interference, and phase contrast microscopy were employed.
- Image analysis and animation methods were used to characterize WLS morphology.
Main Results:
- Interference microscopy revealed a gradual, intertwined twisted fiber organization in WLS.
- Maltese-cross birefringence images in cross-sections indicated a spiral fiber arrangement.
- Helical fiber orientation was confirmed by focusing through different section planes.
Conclusions:
- The study supports a helical superstructure for collagen bundles in tendons, challenging the planar WLS model.
- The observed superstructure aligns with the twisted grain boundary concept for mesophase classification.