Fresh samples of hydantoin induced hyperplastic, healthy and inflamed human gingiva were studied histochemically using various azo dyes for β‐glucuronidase (EC 3.2.1.31), for β‐ and β‐glucosidase (EC 3.2.1.20 and 3.2.1.21) as well as β‐galactosidase (EC 3.2.1.23) and for N‐acetylglucosaminidase (EC 3.2.1.30), in order to add support to the hypothesis that hydantoin induced hyperplasia is always connected with inflammation. Moderate β‐glucuronidase activity was observed in healthy, inflamed and hydantoinhyperplastic gingiva. The distribution of the enzyme activity was similar in all types of the tissue except the stratum corneum. The healthy gingiva did not reveal this activity whereas the inflamed and hydantoinhyperplastic gingiva did. The stratum basale and spinosum of the epithelium, the fibroblasts and the inflammatory cells, especially the macrophages, revealed enzyme activity in all types of tissues. In the healthy tissue only a few inflammatory cells were seen and thus the β‐glucuronidase activity was low when compared to inflamed or hyperplastic gingiva. Weak β‐galactosidase, N‐asetylglucosaminidase and β‐glucosidase activity was seen in all types of gingival samples. Enzyme activity was observed in the same structures as β‐glucuronidase with the exception of the stratum corneum, which revealed no activity. The relatively strong β‐glucuronidase activity in the keratinized cell layer of the epithelium of inflamed and hydantoinhyperplastic tissue may be due to the microbial enzyme diffusion into the keratinized cell layer of the injured tissue.
Arylaminopeptidase activity in hydantoin induced hyperplastic, inflamed and healthy human gingiva was studied using various N‐L‐aminoacyl‐2‐naphthylamines as substrates. The activity was seen to be located in the basal cell layer of the epithelium in the entire connective tissue, but it was strongest just below the epithelium in all tissues. High enzymic activity was also observed in the inflammatory cells as well as in the capillary walls of hydantoinhyperplastic and inflamed gingiva. Strong enzymic activity was obtained when N‐L‐alanyl‐, N‐L‐methionyl‐ and N‐L‐leacyl‐2‐naphthylamine were used as substrates. Moderate activity was observed with N‐L‐arginyl‐2‐naphthylamine and N‐Llysyl‐2‐naphthylamine in other tissues except in healthy gingiva where the enzymic activity was low or nil. To test the possible involvement of aminopeptidase B in the material the reactions were performed both in the presence and absence of 0.2 M sodium chloride, which specifically activates this enzyme. There was no observable enzymic activity in any slices when N‐L‐prolyl‐2‐naphthylamine was used as substrate. The role of different arylaminopeptidases in connection with gingival hyperplasia caused by diphenylhydantoin and the evident absence of enzymes specific to N‐L‐prolyl‐2‐naphthylamine are discussed.
Arylaminopeptidase and glycosidase activities were studied by histochemical staining methods in human tooth and supporting tissue ontogeny in order to demonstrate the possible metabolic differences in the differentiated and undifferentiated cells of the formation, modelling and re‐modelling metabolism of the tissue involved. The enzyme activities were studied using various N‐L‐ aminoacyl‐2‐naphthylamines and 1‐ and 2‐naphthol glycosides and ‐esters as substrates. The arylaminopeptidase activity (EC 3.4.11) was observed (1) in the basal cell layer of oral epithelium in the stomodeum, (2) in the subjacent mesoderm, (3) in the outer and (4) inner enamel epithelium, (5) in the dental papilla, (6) in the dental lamina, and (7) in the primordium of permanent tooth. No arylaminopeptidase activity could be observed in ameloblasts. odontoblasts. enamel, dentin, stellate reticulum and pulp, and the inner enamel epithelium also lost its activity during the stage of apposition. The following glycosidases were observed in the same structures as the arylaminopeptidases: β‐N‐acetylglucosaminidase (EC 3.2.1.30), β‐glucosidase (EC 3.2.1.21), β‐galactosidase (EC3.2.1.23). β‐glucuronidase (EC 3.2.1.31), as well as arylsulphatase (EC 3.1.6.1) The whole thickness of oral epithelium revealed β‐galactosidase and arylsulphatase activity, not only the basal cell layer. These observations were‐ thought to give support to the suggestions that differeniation is a stage of highly active metabolism and thus at the stage of apposition the cells of the outer enamel epithelium are actively differentiating.
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