PubMed HealthSearch

PubMed · 283104

Proteolytic activity in developing bovine enamel.

Abstract

Partially mineralized enamel matrix removed from bovine incisor tooth germs contains proteolytic activity capable of completely degrading enamel matrix proteins at neutral and slightly alkaline pH. The protease activity also degrades common protease substrates such as casein and azocoll with optimal activity at pH 8-9. Inhibitor studies revealed that the enzyme involved is a serine protease of the chymotrypsin family.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

D Moe, H Birkedal-Hansen. 1979. Proteolytic activity in developing bovine enamel.. https://doi.org/10.1177/002203457905800207011

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Common epitopes of mammalian amelogenins at the C-terminus and possible functional roles of the corresponding domain in enamel mineralization.

The present studies were undertaken to investigate the presence of common epitopes of mammalian amelogenins at the C-terminus and the possible functional importance of the conserved C-terminal domain in enamel mineralization during mammalian amelogenesis. Enamel proteins, including the intact amelogenins and their degraded polypeptides, were isolated from the secretory enamel of pig, cow, rat, and rabbit incisors. Rabbit and rat antipeptide sera, as well as rat anti-25 kD and 20 kD pig amelogenin sera, were used to identify the amelogenins among the isolated matrix proteins of each of the animal species. The antipeptide sera were developed previously (Aoba et al. [19]) using as immunogens the two synthetic peptides, C13 and C25, which correspond to the last 12 (plus Cys for KLH-conjugation) and 25 amino acid residues of pig intact amelogenin, respectively. Reactivity of the enamel proteins with each antiserum was examined by Western blot analysis. The results of immunoblotting showed that a few enamel matrix proteins in each of the mammalian species were recognized by the anti-C13 serum, specifically, pig amelogenin at 25 kD (and trace components at 27, 22, and 18 kD), cow amelogenin at 28 kD (trace components at 26, 22, 19, and 14 kD), rat amelogenins at 28 and 26 kD (and a trace component at 20 kD), and rabbit amelogenins at 24 and 21 kD (and a trace at 13 kD). The anti-C25 serum reacted additionally with pig amelogenin at 23 kD, cow amelogenin at 27 kD (a major matrix constituent), and rabbit protein at 19 kD.(ABSTRACT TRUNCATED AT 250 WORDS)

Amelogenesis

Human amelogenesis. I: High resolution electron microscopy study of ribbon-like crystals.

Ribbon-like crystals, from developing enamel of human fetuses, were studied by high resolution electron microscopy. These crystals were classically described as the first organized mineral formed during amelogenesis. They were characterized by a mean width-to-thickness ratio (W.T-1) of 9.5, and 40% were bent. On lattice images we noted the presence of the central dark line (CDL) associated with white spots. Both structures were found in crystals with a minimum thickness of 8-10 nm. CDLs were localized in the center of the crystals and seemed to be linked to the initial growth process, but their exact structure and function were not fully determined. We were able to study the structure of the ribbon-like crystals with a Scherzer resolution close to 0.2 nm. The good correspondence between experimental and computed images showed that their structure was related to hydroxyapatite (HA). In addition, the presence of ionic substitutions and deficiencies were also compatible with HA. In this study, about 50% of the crystals showed structural defects. Screw dislocations were the most often noted defects and were observed within crystals aligned along five different zone axes. Low- and high-angle boundaries were also detected. Low-angle boundaries, found in the center of the crystals, could thus be related to CDLs and be implicated in the nucleation step of crystal formation, whereas high-angle boundaries could result from the fusion of ribbon-like crystals. Such mechanisms could induce an acceleration of the growth in thickness of the crystal observed during the maturation stage of amelogenesis.

Amelogenesis

Histogenetic aspects of the composition and structure of human ectopic enamel, studied by scanning electron microscopy.

This study was made on 12 enamel projections and 12 enamel pearls on human permanent molars to compare their structure and composition, which might elucidate possible histogenetic differences between these two forms of ectopic enamel. The enamel projections contained approx. 2 (weight)% less Ca and P than control occlusal and mid-coronal enamel. Their mineralization was less homogeneous and probably defective. Their enamel structure was markedly irregular in the prismatic as well as the aprismatic layer, but the composition and structure were very similar to those of the control enamel close to cervical border. The enamel of the pearls largely corresponded in composition and structure to the control occlusal and mid-coronal enamel. The enamel of large pearls also resembled coronal enamel in its compositional and structural variability in the occlusal-cervical direction. These findings suggest that amelogenesis in enamel projections is a continuation of amelogenesis in the cervical region. In contrast, amelogenesis in enamel pearls follows the same pattern as that in a dental crown, from the occlusal region to the cervical enamel border. Therefore, the enamel pearl may well be regarded as an attempt at new tooth formation.

Amelogenesis