MOLECULAR-SIZE DISTRIBUTION ANALYSIS OF HUMAN GINGIVAL PROTEOGLYCANS AND GLYCOSAMINOGLYCANS IN SPECIFIC PERIODONTAL-DISEASES

In order to determine the molecular-size distribution of gingival prot eoglycans (PGs) and glycosaminoglycans (GAGs) both in periodontal heal th and disease states, gingival tissues were obtained from patients wi th early onset periodontitis (EOP) and adult periodontitis (AP) and al so from periodontally healthy subjects. Gel filtration chromatography of gingival PGs revealed different profiles for periodontally diseased and healthy gingiva. Healthy gingiva was mainly composed of high-mole cular size proteins and PGs, while diseased gingival tissue presented a decrease in high-molecular size PG forms and a shift towards low-mol ecular size proteins and PGs. This indicates the degradation of PG mac romolecules during periodontal disease activity. Furthermore, this shi ft towards low-molecular size forms was more intense in EOP patients w hen compared to AP patients. Gel filtration of gingival GAGs also demo nstrated depolymerization of GAGs, with low-molecular size GAGs being more intense in periodontally diseased gingiva, while healthy gingival GAGs profile was mainly composed of high-molecular size GAGs. Similar to the profile of gingival PGs, low-molecular size gingival GAGs were more prominent in gingival tissue from patients with EOP. These findi ngs suggest that both PGs and GAGs, essential components of the extrac ellular matrix (ECM), are depolymerized during periodontal disease act ivity, which is more prominent in EOP. Since the basic feature of peri odontal disease is matrix degradation, ECM components, more specifical ly PGs and GAGs, are likely to provide valuable information for a bett er understanding of periodontal disease activity.