Nom du corpus

Corpus Systématique Animale

Titre du document

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

Lien vers le document
Éditeur
Springer (journals)
Langue(s) du document
Anglais
Type de document
Research-article
Mots-clés d'auteur
  • Amelogenesis
  • Pig, cow, rat, rabbit amelogenins
  • Epitopes at the C-terminus
  • Adsorption
  • Enamel mineralization
Nom du fichier dans la ressource
Mammiferes_v2b_01811
Auteur(s)
  • T. Aoba 1
  • S. Shimoda 2
  • H. Shimokawa 3
  • T. Inage 4
Affiliation(s)
  • 1) Forsyth Dental Center, 140 Fenway, 02115, Boston, MA, USA
  • 2) Tsurumi University School of Dentistry, 230, Yokohama, Japan
  • 3) School of Dentistry, Tokyo Medical and Dental University, 113, Tokyo, Japan
  • 4) Nihon University School of Dentistry, 101, Tokyo, Japan
Résumé

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. The anti-pig 20 kD amelogenin (lacking the last 25 amino acid residues at the C-terminus) serum reacted with a large number of pig, cow, and rat amelogenins but, interestingly, with none of the rabbit enamel proteins. Probing of rat enamel proteins with Maclura pomifera lectin showed the heterogeneity of glycosylation of rat amelogenins, particularly between the 28 and 26 kD intact amelogenins. In parallel adsorption studies, part of the enamel protein samples isolated from each of the species was used as adsorbates to investigate the selective adsorption of amelogenins onto hydroxyapatite. Immunoblot analysis of the proteins adsorbed onto the crystals revealed that the mammalian amelogenins having the common epitopes at the C-terminus, in general, adsorb preferentially onto hydroxyapatite. The adsorption affinity of the degraded amelogenins decreased significantly with the loss of reactivity toward the anti-C13 serum. The overall results support the contention that the intact mammalian amelogenins, including rat and rabbit amelogenins, share common epitopes at the C-terminus and that the conserved C-terminal domain plays an important role in setting the molecular structures of the intact amelogenins so as to facilitate the protein-enamel mineral interaction.

Catégories Science-Metrix
  • 1 - health sciences
  • 2 - clinical medicine
  • 3 - endocrinology & metabolism
Catégories INIST
  • 1 - sciences appliquees, technologies et medecines
  • 2 - sciences biologiques et medicales
  • 3 - sciences biologiques fondamentales et appliquees. psychologie
Catégories Scopus
  • 1 - Life Sciences ; 2 - Biochemistry, Genetics and Molecular Biology ; 3 - Endocrinology
  • 1 - Health Sciences ; 2 - Medicine ; 3 - Orthopedics and Sports Medicine
  • 1 - Health Sciences ; 2 - Medicine ; 3 - Endocrinology, Diabetes and Metabolism
Catégories WoS
  • 1 - science ; 2 - endocrinology & metabolism
Identifiant ISTEX
39990A894BF8EBA52257E55CD4497FE12B8390F6
Revue

Calcified Tissue International

Année de publication
1992
Présence de XML structuré
Non
Version PDF
1.3
Score qualité du texte
10
Sous-corpus
  • Mammiferes
Type de publication
Journal
ark:/67375/1BB-K56WLZD7-R
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