Collagenase in Sjögren's syndrome

Ann Rheum Dis. 1994 Dec;53(12):836-9. doi: 10.1136/ard.53.12.836.

Abstract

Objective: To study collagenase production in labial salivary glands in patients with Sjögren's syndrome (SS).

Methods: Collagenases were localised in labial salivary glands by immunohistochemistry. Collagenase activity against triple helical type I collagen monomers in stimulated saliva was measured using sodium dodecyl sulphate polyacrylamide gel electrophoresis and laser densitometry; tissue inhibitor metalloproteinase (TIMP) was measured by enzyme linked immunosorbent assay.

Results: Cells containing collagenase of matrix metalloproteinase (MMP)-1 type were more frequent and more intensely staining in SS than in healthy glands. Only SS saliva contained functional enzyme (11.7 (6.8) x 10(-6) IU/1). Cells containing MMP-8 type neutrophil collagenase were not found in situ, which was in accordance with sialochemical findings/doxycycline inhibition studies. TIMP was found in both SS and normal saliva.

Conclusions: Fibroblast, but not neutrophil type, collagenase is synthesised, secreted, and subsequently activated, but is not inhibited by TIMP in labial salivary glands or saliva in SS. Collagenase may destroy glandular and salivary duct tissue and perturb factors influencing the morphogenetic extracellular matrix.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Collagenases / metabolism*
  • Glycoproteins / metabolism
  • Humans
  • Immunohistochemistry
  • Matrix Metalloproteinase 1
  • Matrix Metalloproteinase Inhibitors
  • Saliva / enzymology
  • Salivary Glands / enzymology*
  • Sjogren's Syndrome / enzymology*
  • Tissue Inhibitor of Metalloproteinases

Substances

  • Glycoproteins
  • Matrix Metalloproteinase Inhibitors
  • Tissue Inhibitor of Metalloproteinases
  • Collagenases
  • Matrix Metalloproteinase 1