Collagen distribution in the lamina cribrosa and the trabecular meshwork of the human eye

Br J Ophthalmol. 1987 Dec;71(12):886-92. doi: 10.1136/bjo.71.12.886.

Abstract

Tengroth and Ammitzböll found the collagen content of the optic disc in glaucoma to differ from that of normal eyes. A theory was advanced that a primary collagen disturbance might be involved in the pathogenesis of glaucoma. The connective tissue in the body has a supportive function in almost all the organs. The tensile strength and elasticity of connective tissue is mainly due to the presence of collagen fibres and elastic fibres, which also maintain the shape of the tissues. There are many different types of collagen, three of which are discussed in this paper. Type I collagen is found in tendons, skin, and numerous other organs, for example the eye. Type III is found mainly in the blood vessels but is also present in other tissues with a mesodermal origin, and type IV is found in the basement membranes. To elucidate the precise distribution of collagen types in the ocular structures an immunhistochemical study was undertaken in normal human eyes. The amino acids proline, hydroxyproline, and hydroxylysine, which are characteristic of collagen, were also analysed. Collagen types I, III, and IV were found in the lamina cribrosa, the trabecular meshwork, and the retrolaminary optic nerve. In contrast, only type I was found in the sclera.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Collagen / metabolism*
  • Humans
  • Hydroxylysine / metabolism
  • Hydroxyproline / metabolism
  • Middle Aged
  • Optic Nerve / metabolism
  • Proline / metabolism
  • Sclera / metabolism*
  • Trabecular Meshwork / metabolism*

Substances

  • Hydroxylysine
  • Collagen
  • Proline
  • Hydroxyproline