Connective tissue alteration in abdominal wall hernia

Br J Surg. 2011 Feb;98(2):210-9. doi: 10.1002/bjs.7339.

Abstract

Background: The aetiology and pathogenesis of abdominal wall hernia formation is complex. Optimal treatment of hernias depends on a full understanding of the pathophysiological mechanisms involved in their formation. The aim of this study was to review the literature on specific collagen alterations in abdominal wall hernia formation.

Methods: A computer-assisted search of the medical databases PubMed and Embase was performed, together with a cross-reference search of eligible papers.

Results: Fifty-two papers were included. Collagen alteration depended on the type of hernia; there were more pronounced changes in patients with a direct inguinal hernia than in those with an indirect inguinal hernia, recurrent inguinal hernia or incisional hernia. A consistent finding was a significant increase in immature type III collagen relative to the stronger type I collagen in patients with a hernia. This resulted in thinner collagen fibres with a correspondingly diminished biomechanical strength. It has been suggested that these alterations are due to variation in the synthesis, maturation or degradation of collagen by matrix metalloproteinases, in combination or alone.

Conclusion: Hernia formation and recurrence is associated with altered collagen metabolism manifested by a decreased type I:III collagen ratio.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Abdominal Wall
  • Collagen Type I / metabolism*
  • Collagen Type I / ultrastructure
  • Collagen Type III / metabolism*
  • Collagen Type III / ultrastructure
  • Connective Tissue / metabolism*
  • Connective Tissue / ultrastructure
  • Extracellular Matrix Proteins / metabolism
  • Hernia, Abdominal / etiology*
  • Hernia, Abdominal / metabolism
  • Humans
  • Matrix Metalloproteinases / physiology
  • Microscopy, Electron
  • Recurrence

Substances

  • Collagen Type I
  • Collagen Type III
  • Extracellular Matrix Proteins
  • Matrix Metalloproteinases