Objective-To study collagenase production in labial salivary glands in
patients with Sjogren's syndrome (SS). Methods-Collagenases were loca
lised in labial salivary glands by immunohistochemistry. Collagenase a
ctivity against triple helical type I collagen monomers in stimulated
saliva was measured using sodium dodecyl sulphate polyacrylamide gel e
lectrophoresis and laser densitometry; tissue inhibitor metalloprotein
ase (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 g
lands. Only SS saliva contained functional enzyme (11.7 (6.8) x 10(-6)
IU/1). Cells containing MMP-8 type neutrophil collagenase were not fo
und in situ, which was in accordance with sialochemical findings/doxyc
ycline inhibition studies. TIMP was found in both SS and normal saliva
. Conclusions-Fibroblast, but not neutrophil type, collagenase is synt
hesised, secreted, and subsequently activated, but is not inhibited by
TIMP in labial salivary glands or saliva in SS. Collagenase may destr
oy glandular and salivary duct tissue and perturb factors influencing
the morphogenetic extracellular matrix.