Not only tendons: The other architecture of collagen fibrils

Int J Biol Macromol. 2018 Feb;107(Pt B):1668-1674. doi: 10.1016/j.ijbiomac.2017.10.037. Epub 2017 Oct 10.

Abstract

For many decades the fibrillar collagens have been the subject of a remarkable body of ultrastructural research. The vast majority of the studies, however, were carried out on tendon or on tendon-derived material. For many reasons this reflects an obvious choice but at the same time it also is an unfortunate circumstance, because this flooding of tendon-related data can easily encourage the false confidence that all connective tissues are similar. The reality is quite the opposite, and a different fibrillar structure has been long time observed on collagen fibrils from different tissues, the most notable example being offered by corneal fibrils. The same architecture can be found in a number of disparate tissues and may actually be the prevalent one on a whole-body scale. Although these fibrils diverge from those of tendon in their architecture, size, D-period, composition, cross-linking and fibrillogenesis mechanism, their structure was the subject of rather sparse ultrastructural studies and even today their mere existence is often overlooked or ignored. This paper summarizes the main aspects of the structural biology of these forgotten fibrils.

Keywords: Collagen; Extracellular matrix; Fibrillogenesis.

Publication types

  • Review

MeSH terms

  • Animals
  • Collagen / chemistry*
  • Cross-Linking Reagents / pharmacology
  • Humans
  • Tendons / anatomy & histology*

Substances

  • Cross-Linking Reagents
  • Collagen