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Journal of Dental Research, Vol 68, 20-25, Copyright © 1989 by International & American Associations for Dental Research Online Journals
ARTICLES |
H. Larjava, J. Heino, V. M. Kahari, T. Krusius and E. Vuorio
Departments of Periodontology, University of Turku, Finland.
Human granulation-tissue fibroblasts were cultured from oral chronic inflammatory lesions and compared with fibroblasts of healthy gingival connective tissue with respect to cell-surface sialoglycoproteins, and the synthesis of extracellular matrix components. Granulation-tissue fibroblasts exhibited a slower growth rate and larger size than their controls. Their cell-surface sialoglycoproteins resembled those of the control cells, except that the relative amount of glycoproteins in the 140-kd region was lower. The ratio of mRNAs for pro alpha l (I) and pro alpha l (III) collagen chains was decreased in granulation-tissue fibroblasts, although electrophoretic fractionation of the proteins did not reveal consistent differences in type I/type III collagen ratio. Granulation-tissue fibroblasts secreted into the culture medium a dermatan sulfate proteoglycan with a lower molecular weight. After digestion with chondroitinase ABC, the molecular weight of the core protein appeared to be identical with that of the control fibroblasts, suggesting a difference in the glycosylation of the core protein. These results support the theory that granulation-tissue fibroblasts represent a distinct phenotype of fibroblastic cells.
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