Collagen fibril ultrastructure and course were examined in different connective tissues by PLM, SEM, TEM, and AFM. In tendons, collagen fibrils were large and heterogeneous with a straight subfibrillar arrangement. They ran densely packed, parallel, and straight changing their direction only in periodic crimps where fibrils showed a local deformation (fibrillar crimps). Other tissues such as aponeurosis, fascia communis, skin, aortic wall, and tendon and nerve sheaths showed thinner uniform fibrils with a helical subfibrillar arrangement. These fibrils appeared in parallel or helical arrangement following a wavy, undulating course. Ligaments showed large fibrils as in tendon, with fibrillar crimps but less packed. Thinner uniform-sized fibrils also were observed. Fibrillar crimps seem to be related to the subfibrillar arrangement being present only in large fibrils with a straight subfibrillar arrangement. These stiffer fibrils respond mainly to unidirectional tensional forces, whereas the flexible thinner fibrils with helical subfibrils can accommodate extreme curvatures without harm, thus responding to multidirectional loadings.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1080/03008200801913635 | DOI Listing |
Acta Biomater
January 2018
School of Optometry and Vision Sciences, Cardiff University, Maindy Road, Cathays, Cardiff CF24 4HQ, UK; Cardiff Institute of Tissue Engineering and Repair, Cardiff University, 10 Museum Place, Cardiff CF10 3BG, UK.
Unlabelled: Fibrillar collagen in the human cornea is integral to its function as a transparent lens of precise curvature, and its arrangement is now well-characterised in the literature. While there has been considerable effort to incorporate fibrillar architecture into mechanical models of the cornea, the mechanical response of corneal collagen to small applied loads is not well understood. In this study the fibrillar and molecular response to tensile load was quantified using small and wide angle X-ray scattering (SAXS/WAXS), and digital image correlation (DIC) photography was used to calculate the local strain field that gave rise to the hierarchical changes.
View Article and Find Full Text PDFPLoS One
June 2014
Minnesota Dental Research Center for Biomaterials and Biomechanics (MDRCBB) Department of Restorative Sciences, University of Minnesota School of Dentistry, Minneapolis, Minnesota, United States of America.
Biomineralization templated by organic molecules to produce inorganic-organic nanocomposites is a fascinating example of nature using bottom-up strategies at nanoscale to accomplish highly ordered multifunctional materials. One such nanocomposite is bone, composed primarily of hydroxyapatite (HA) nanocrystals that are embedded within collagen fibrils with their c-axes arranged roughly parallel to the long axis of the fibrils. Here we discern the ultra-structure of biomimetic mineralized collagen fibrils (MCFs) as consisting of bundles of subfibrils with approximately 10 nm diameter; each one with an organic-inorganic core-shell structure.
View Article and Find Full Text PDFConnect Tissue Res
May 2008
Department of Human Anatomical Sciences and Physiopathology of Locomotor Apparatus, University of Bologna, Italy.
Collagen fibril ultrastructure and course were examined in different connective tissues by PLM, SEM, TEM, and AFM. In tendons, collagen fibrils were large and heterogeneous with a straight subfibrillar arrangement. They ran densely packed, parallel, and straight changing their direction only in periodic crimps where fibrils showed a local deformation (fibrillar crimps).
View Article and Find Full Text PDFArch Histol Cytol
May 2000
Department of Anatomy and Histology, Faculty of Medicine, Niigata University, Japan.
The present study was designed to analyze the subfibrillar structure of corneal and scleral collagen fibrils by scanning electron microscopy (SEM) and atomic force microscopy (AFM). Isolated collagen fibrils of the bovine cornea and sclera were fixed with 1% OsO4, stained with phosphotungstic acid and uranyl acetate, dehydrated in ethanol, critical point-dried, metal-coated, and observed in an in-lens type field emission SEM. Some isolated collagen fibrils were fixed with 1% OsO4, dehydrated, critical point-dried and observed without metal-coating in an AFM.
View Article and Find Full Text PDFAnat Histol Embryol
August 1999
Department of Veterinary Anatomy, School of Veterinary Medicine, Rakuno Gakuen University, Hokkaido, Japan.
Light and electron microscopic studies were conducted on dermis samples taken from different regions of adult cows and pigs to determine whether there is a correlation between subfibrillar architecture and collagen fibril diameter in dermis tissue. Dermis thicknesses, collagen fibril diameters, subfibrillar architecture diameters, and angles of the helical arrangement of subfibrillar architectures were measured in all dermis samples. The results showed that the differences between subfibrillar architecture diameters in dermis samples from different regions of the same species were not significant and that the diameters of subfibrillar architectures in dermis samples were similar (22-28 nm) in the two species (cow and pig) examined in this study.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!