Abstract
We studied the ultrastructural localization of three distantly related glycoproteins of the extracellular matrix, undulin, tenascin and fibronectin, in decalcified sections of human periodontal ligament (PL) and cementum. Undulin was associated with tightly packed major collagen fibrils and not with microfibrils, indicating that this protein may be involved in the supramolecular and functional organization of collagen fibrils into flexible bundles. Tenascin was found on globular masses between less densely packed collagen fibrils, thus displaying a pattern quite distinct from that of undulin. Fibronectin was noted in bulky material between the cross-striated fibrils, often surrounding individual fibrils like garlands, and in the microfibrillar meshwork extending from cross-striated fibrils. The three glycoproteins displayed a distinct and unique pattern of distribution in PL that can be correlated with their molecular structure and potential functions.