Lathyrogens and the role of collagen in the eruption of rat incisors.

Collagen fibres in the periodontal ligament may have two functions: to resist displacing forces and to cause the tooth to erupt. Their function was examined in the continuously-erupting incisor of the rat using various concentrations and types of lathyrogens. Lathyrogens retarded tooth eruption and increased the quantity of salt-soluble collagen in the ligament, indicating inhibition of the maturation of salt-soluble (young) collagen into salt-insoluble (old) collagen, which would lead to reduction in the tensile strength of the fibres and decrease resistance to occlusal forces. The easy extractability of the teeth is explained by the greater susceptibility to lathyrogens of the fibres in the alveolar-related part of the periodontal ligament, compared with those in the other parts.

The concentration, extractability and characterization of collagen in human dental pulp.

Premolar and third molar dental pulps were studied. The amount of collagen in the dried pulps was 25.7 per cent in premolars and 31.9 per cent in third molars. These percentages are much higher than those reported for pulps in other species. Significant differences were further found in the collagen content and cell distribution (DNA) of the coronal, middle and apical parts of the pulp. Collagen content was the lowest in the coronal part, while the cell content was the lowest in the middle part. The extractability of collagen in a neutral salt solution or 0.5 M acetic acid was found to be extremely low (less than 1 per cent). Pretreatment of the pulp with hyaluronidase in order to remove proteoglycans had no effect on the solubility. It is concluded that human pulp collagen is highly cross-linked and cannot be considered as immature. Characterization of collagen was performed by methods in which limited pepsin digestion or CNBr cleavage was used. The digests were analysed by means of quantitative electrophoresis which revealed an amount of 42.6 per cent type III of the total collagen. Because of the large differences between dental pulps from man and experimental animals, extreme caution should be exercised in drawing conclusions from data of other species to explain phenomena observed in human teeth.

Immunofluorescent localization and extractability of fibronectin in human dental pulp.

Fibronectin, visualized in premolar pulps by indirect immunofluorescence, was abundant in the odontoblast layer, around blood vessels and in the core of the pulp. Similarity of alignment of fibronectin with the argyrophilic fibres and von Korff fibres was evident. Fibronectin was extracted from pulps after first removing blood by washing with water, confirmed by eventual negative reaction on alpha 2-macroglobulin. Extraction of fibronectin from this remaining tissue was most effectively achieved by treatment with collagenase or hyaluronidase, though in all cases some fibronectin remained, indicating that fibronectin in pulp is not exclusively associated with collagen and/or proteoglycans. The fibronectin quantified by electro-immunoassay and expressed as percentage of dry weight was 0.030 per cent in the water extract, 0.094 per cent in the collagenase extract and 0.109 per cent in the hyaluronidase extract. Twice as much fibronectin was extracted from the apical pulp as from the coronal and middle parts, in accord with earlier findings of a higher collagen content in the radicular part. It is suggested that with the loss of collagen type III during odontoblast differentiation and its reappearance with advancing vascularization of the dental papilla, the amount of fibronectin is similarly altered.