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

Ravindranath, Rajeswari M.H.; Tam, Wai-Yin; Nguyen, Pauline; Fincham, Alan G.

doi:10.1074/jbc.m006471200

Cited by 35 publications

(43 citation statements)

References 44 publications

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“…Western Blot Analysis-K5 purified from HeLa cells and proteins isolated from ameloblast extracts during different developmental days (newborn to PN day 9) were resolved by gradient SDS-PAGE (4 -12%) and electrotransferred to polyvinylidene difluoride (PVDF) membranes (Immobilon-P Transfer Membrane, Millipore Corp.) at 100 mA for 35 min using a semi-dry transblot apparatus (Bio-Rad Scientific Instruments) (5,8). Protein transfer was assessed by staining the strips with 0.1% Fast Green (Sigma) in 40% methanol and 10% acetic acid (5,8).…”

Section: Methodsmentioning

confidence: 99%

“…Protein transfer was assessed by staining the strips with 0.1% Fast Green (Sigma) in 40% methanol and 10% acetic acid (5,8). The membranes were washed (five times) and blocked with PBS (pH 7.2) containing Ϫ1% HSA, and were overlaid with appropriate antibodies.…”

Section: Methodsmentioning

confidence: 99%

“…Analysis and Autoradiography-Purified K5 was resolved via SDS-PAGE and transferred to PVDF membranes at 100 mA for 35 min using a semi-dry transblot apparatus (Bio-Rad Scientific Instruments) (5,8). Protein transfer was assessed by staining the PVDF strips with 0.1% Fast Green as mentioned previously (5,8).…”

Section: Binding Of [ 3 H]atmp To K5 By Western Blotmentioning

confidence: 99%

“…The N-terminal 45 amino acid residues are referred to as tyrosine-rich amelogenin polypeptide (TRAP). 1 The C-terminal 13-amino acid sequence in the TRAP region called "amelogenin tyrosyl motif peptide" (ATMP: PYPSYGYEPMGGW) possesses unique ligand-binding properties, in that it binds specifically to N-acetylglucosamine (GlcNAc) (4) and GlcNAc-mimicking peptides (GMps) (5). Mutations in the ATMP sequence are observed in the human X-linked amelogenesis imperfecta (AI) (6).…”

mentioning

confidence: 99%

“…Mutations in the ATMP sequence are observed in the human X-linked amelogenesis imperfecta (AI) (6). The mutated forms of ATMP failed to bind with GlcNAc or the GMp (4,5). Lossof-function "mutations" of ATMP correlated well with the loss of amelogenin-ligand interaction.…”

mentioning

confidence: 99%

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Amelogenin Interacts with Cytokeratin-5 in Ameloblasts during Enamel Growth

Ravindranath

Basilrose

Ravindranath

et al. 2003

Journal of Biological Chemistry

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Binding Of [ 3 H]atmp To K5 By Western Blotmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Amelogenin Interacts with Cytokeratin-5 in Ameloblasts during Enamel Growth

Ravindranath

Basilrose

Ravindranath

et al. 2003

Journal of Biological Chemistry

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Structural and Functional Studies of Peptide–Carbohydrate Mimicry

Johnson

Pinto

2008

Topics in Current Chemistry

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Certain peptides act as molecular mimics of carbohydrates in that they are specifically recognizedby carbohydrate-binding proteins. Peptides that bind to anti-carbohydrate antibodies, carbohydrate-processingenzymes, and lectins have been identified. These peptides are potentially useful as vaccines andtherapeutics; for example, immunologically functional peptide molecular mimics (mimotopes) can strengthenor modify immune responses induced by carbohydrate antigens. However, peptides that bind specificallyto carbohydrate-binding proteins may not necessarily show the corresponding biological activity, andfurther selection based on biochemical studies is always required. The degree of structural mimicryrequired to generate the desired biological activity is therefore an interesting question. This reviewwill discuss recent structural studies of peptide-carbohydrate mimicry employing NMR spectroscopy,X-ray crystallography, and molecular modeling, as well as relevant biochemical data. These studiesprovide insights into the basis of mimicry at the molecular level. Comparisons with other carbohydrate-mimeticcompounds, namely proteins and glycopeptides, will be drawn. Finally, implications for the designof new therapeutic compounds will also be presented.

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Molecular Evolution of Amelogenin in Mammals

2005

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Abstract. An evolutionary analysis of mammalian amelogenin, the major protein of forming enamel, was conducted by comparison of 26 sequences (including 14 new ones) representative of the main mammalian lineages. Amelogenin shows highly conserved residues in the hydrophilic N-and C-terminal regions. The central hydrophobic region (most of exon 6) is more variable, but it has conserved a high amount of proline and glutamine located in triplets, PXQ, indicating that these residues play an important role. This region evolves more rapidly, and is less constrained, than the other well-conserved regions, which are subjected to strong constraints. The comparison of the substitution rates in relation to the CpG richness confirmed that the highly conserved regions are subjected to strong selective pressures. The amino acids located at important sites and the residues known to lead to amelogenesis imperfecta when substituted were present in all sequences examined. Evolutionary analysis of the variable region of exon 6 points to a particular zone, rich in either amino acid insertion or deletion. We consider this region a hot spot of mutation for the mammalian amelogenin. In this region, numerous triplet repeats (PXQ) have been inserted recently and independently in five lineages, while most of the hydrophobic exon 6 region probably had its origin in several rounds of triplet insertions, early in vertebrate evolution. The putative ancestral DNA sequence of the mammalian amelogenin was calculated using a maximum likelihood approach. The putative ancestral protein was composed of 177 residues. It already contained all important amino acid positions known to date, its hydrophobic variable region was rich in proline and glutamine, and it contained triplet repeats PXQ as in the modern sequences.

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

Cited by 35 publications

References 44 publications

Amelogenin Interacts with Cytokeratin-5 in Ameloblasts during Enamel Growth

Amelogenin Interacts with Cytokeratin-5 in Ameloblasts during Enamel Growth

Structural and Functional Studies of Peptide–Carbohydrate Mimicry

Molecular Evolution of Amelogenin in Mammals

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