The Enamel Protein Amelogenin Binds to the N-Acetyl-d-glucosamine-mimicking Peptide Motif of Cytokeratins*

@article{Ravindranath2000TheEP,
  title={The Enamel Protein Amelogenin Binds to the N-Acetyl-d-glucosamine-mimicking Peptide Motif of Cytokeratins*},
  author={R. Ravindranath and W. Y. Tam and P. Nguyen and A. Fincham},
  journal={The Journal of Biological Chemistry},
  year={2000},
  volume={275},
  pages={39654 - 39661}
}
Amelogenins bind to GlcNAc of the dentine-enamel matrix proteins (Ravindranath, R. M. H., Moradian-Oldak, J., Fincham, A. G. (1999) J. Biol. Chem. 274, 2464–2471). The hypothesis that amelogenins may interact with the peptides that mimic GlcNAc is tested. GlcNAc-mimicking peptide (SFGSGFGGGY) but not its variants with single amino acid substitution at serine, tyrosine, or phenylalanine residues inhibited hemagglutination of amelogenins and the terminal tyrosine-rich amelogenin polypeptide (TRAP… Expand
Amelogenin-Cytokeratin 14 Interaction in Ameloblasts during Enamel Formation*
TLDR
It is proposed that CK14 play a chaperon role for nascent amelogenin polypeptide during amelogenesis, and the dissociation of the co-assembly at the ameloblast Tomes' process is corroborated. Expand
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TLDR
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TLDR
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In a mouse model of amelogenesis imperfecta (Al), an amelogenin p.Y64H mutation was reported to cause the abnormal retention of amelogenin in the ameloblast secretory pathway. This was hypothesisedExpand
Enamel formation in vitro in mouse molar explants exposed to amelogenin polypeptides ATMP and LRAP on enamel development.
TLDR
Exogenous ATMP, T-ATMP and LRAP have divergent effects on developing enamel, which may play a role in the differentiation of ameloblasts, growth of enamel and formation of dentinal tubules. Expand
Amelogenins: Multi-Functional Enamel Matrix Proteins and Their Binding Partners.
Abstract Amelogenins are the most abundant extracellular matrix proteins secreted by ameloblasts during tooth development and are important for enamel formation. Recently, amelogenins have beenExpand
Molecular Evolution of Amelogenin in Mammals
TLDR
An evolutionary analysis of mammalian amelogenin, the major protein of forming enamel, was conducted by comparison of 26 sequences representative of the main mammalian lineages, finding that this region evolves more rapidly, and is less constrained, than the other well-conserved regions, which are subjected to strong constraints. Expand
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TLDR
The amelogenin tyrosyl motif peptide sequence showed a similarity to the secondary GlcNAc-binding site of wheat germ agglutinin, and this latter modification mimics a point mutation identified in a case of human X-linked amelogenesis imperfecta. Expand
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The overall results indicate that part of the heterogeneity found in porcine enamel proteins can be ascribed to variations of carbohydrate moieties attached to non-amelogenins. Expand
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TLDR
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TLDR
The Amino acid composition and mass spectrographic analyses established that, in both species, the carboxy-terminal sequences of the LRAP components are two residues longer than previously reported for bovine LRAP, and that both the TRAPs and LRAPs contained a single phosphorylated residue. Expand
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