Colocalization of the collagen-binding proteoglycans decorin, biglycan, fibromodulin and lumican with different cells in human gingiva.
OBJECTIVE
Decorin, biglycan, fibromodulin and lumican are structurally related molecules that belong to the family of small leucine-rich proteoglycans (SLRPs). These SLRPs are secreted extracellular matrix molecules that interact with type I collagen and regulate collagen fibrillogenesis. They may also modulate cell functions that are important in maintenance of connective tissue structure. The aim of this study was to localize decorin, biglycan, fibromodulin and lumican in human gingiva.


METHODS
Localization of decorin and its proform (prodecorin), biglycan, fibromodulin and lumican and mature and proform of type I collagen was studied by immunohistochemical staining of frozen tissue sections from healthy human attached gingiva. Double immunostaining with anti-SLRP or anti-type I procollagen antibodies and specific markers for different connective tissue cells was used to study association of these molecules with cells.


RESULTS
The mature and proforms of decorin and collagen and biglycan, fibromodulin and lumican showed distinct localization in the extracellular matrix, where they associated with type I collagen fiber bundles. Prodecorin also localized to the epithelial basement membrane zone. Fibroblasts, myofibroblasts, endothelial cells and pericytes showed immunoreactivity for procollagen, prodecorin, biglycan and fibromodulin, whereas lumican associated with fibroblasts and myofibroblasts only. Biglycan and fibromodulin were also associated with macrophages. Basal epithelial cells of the gingival epithelium showed immunoreactivity for biglycan, fibromodulin and lumican.


CONCLUSIONS
Decorin, biglycan, fibromodulin and lumican associate with type I collagen and may collaborate to regulate collagen fibrillogenesis in human gingiva. Each of the SLRPs showed a distinct association with different connective tissue cells, suggesting that the cells produce these molecules and/or that the cells interact with them. Localization of biglycan, fibromodulin and lumican at the epithelial cells suggests novel functions for these SLRPs in human gingival epithelium.
Alimohamad
H
H
Department of Oral Biological and Medical Sciences, Laboratory of Periodontal Biology, Faculty of Dentistry, University of British Columbia, Vancouver, British Columbia, Canada.
Habijanac
T
T
Larjava
H
H
Häkkinen
L
L
D000328:Adult; D058578:Biglycan; D011508:Chondroitin Sulfate Proteoglycans / Q000032:analysis; D024042:Collagen Type I / Q000032:analysis*; D058575:Decorin; D005109:Extracellular Matrix / Q000737:chemistry; D016326:Extracellular Matrix Proteins / Q000032:analysis; D000071235:Fibromodulin; D005881:Gingiva / Q000737:chemistry*; D006801:Humans; D007632:Keratan Sulfate / Q000032:analysis; D000071234:Lumican; D011347:Procollagen / Q000032:analysis*; D011509:Proteoglycans / Q000032:analysis*; D013194:Staining and Labeling / Q000379:methods
C546884:BGN protein, human; D058578:Biglycan; D011508:Chondroitin Sulfate Proteoglycans; D024042:Collagen Type I; C546878:DCN protein, human; D058575:Decorin; D016326:Extracellular Matrix Proteins; C000604330:FMOD protein, human; C000604306:LUM protein, human; D000071234:Lumican; D011347:Procollagen; D011509:Proteoglycans; D000071235:Fibromodulin; D007632:Keratan Sulfate