Equine sarcoid: In situ demonstration of matrix metalloproteinase expression

Vet J. 2014 Nov;202(2):279-85. doi: 10.1016/j.tvjl.2014.07.026. Epub 2014 Aug 28.

Abstract

Sarcoids are the most prevalent equine skin tumours and remain a therapeutic challenge due to their differing clinical morphology, local aggressive behaviour, and high recurrence following surgical treatment. In vitro, sarcoid derived fibroblasts are invasive and express matrix metalloproteinase (MMP) -1, -2 and -9. It was hypothesised that the MMPs produced by neoplastic cells play a role in both their local invasiveness and interaction with the overlying epidermis (picket fence formation). The objective of this morphological study was to investigate the local behaviour and in situ MMP expression pattern in sarcoids of different clinical types. A total of 43 surgically excised sarcoids were examined by histology, immunohistology for the expression of MMP-1, -2 and -9, and transmission electron microscopy. Regardless of the clinical type, sarcoids showed local invasion of the dermis and damage to the basement membrane in areas of interaction with the epidermis. This was associated with MMP-1 expression in both neoplastic cells and epidermis. The results suggest a link between MMP-1 expression and the local aggressiveness of sarcoids regardless of the clinical type.

Keywords: Basement membrane; Dermal invasion; Equine sarcoid; Matrix metalloproteinases; Picket fence formation.

MeSH terms

  • Animals
  • Female
  • Gene Expression Regulation, Neoplastic*
  • Histology
  • Horse Diseases / genetics*
  • Horses
  • Male
  • Matrix Metalloproteinase 1 / genetics*
  • Matrix Metalloproteinase 1 / metabolism
  • Matrix Metalloproteinase 2 / genetics*
  • Matrix Metalloproteinase 2 / metabolism
  • Matrix Metalloproteinase 9 / genetics*
  • Matrix Metalloproteinase 9 / metabolism
  • Microscopy, Electron, Transmission / veterinary
  • Sarcoidosis / genetics
  • Sarcoidosis / veterinary*
  • Skin Neoplasms / genetics
  • Skin Neoplasms / veterinary*

Substances

  • Matrix Metalloproteinase 2
  • Matrix Metalloproteinase 9
  • Matrix Metalloproteinase 1