amelogenesis imperfecta/proline

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Canine models of human amelogenesis imperfecta: identification of novel recessive ENAM and ACP4 variants.

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Identifikohuni Regjistrohu

Amelogenesis imperfecta (AI) refers to a genetically and clinically heterogeneous group of inherited disorders affecting the structure, composition, and quantity of tooth enamel. Both non-syndromic and syndromic forms of AI have been described and several genes affecting various aspects of the

Reduced amelogenin-MMP20 interactions in amelogenesis imperfecta.

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Amelogenin with a proline 41 to threonine mutation (P41T) is hydrolyzed at a lower rate by matrix metalloproteinase 20 (MMP20), resulting in an inherited tooth enamel defect, amelogenesis imperfecta (AI). The aim of this study was to elucidate the effect of P41T on the interactions between

Reduced hydrolysis of amelogenin may result in X-linked amelogenesis imperfecta.

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Amelogenesis imperfecta (AI) is a group of inherited disorders with defective tooth enamel formation caused by various gene mutations. One of the mutations substitutes a cytidine to adenine in exon 6 of the X-chromosomal amelogenin gene, which results in a proline to threonine change in the

Characterisation of the biochemical and cellular roles of native and pathogenic amelogenesis imperfecta mutants of FAM83H.

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The majority of mutations identified in patients with amelogenesis imperfecta have been mapped to FAM83H. As FAM83H expression is not limited to the enamel, how FAM83H contributes to amelogenesis is still largely unknown. We previously reported that members of the FAM83 family of proteins interact

X-linked amelogenesis imperfecta may result from decreased formation of tyrosine rich amelogenin peptide (TRAP).

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Identifikohuni Regjistrohu

Amelogenesis imperfecta (AI) is a group of inherited disorders with defective tooth enamel formation caused by various gene mutations. One of the mutations substitutes a cytidine for an adenine in exon 6 of the X-chromosomal amelogenin gene, which results in a proline to threonine change in the

The enamel proteins in human amelogenesis imperfecta.

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Identifikohuni Regjistrohu

Amelogenesis imperfecta comprises a unique group of hereditary conditions that result in abnormal enamel development. The purpose of this study was to characterize the enamel proteins in different amelogenesis imperfecta types and to determine if amelogenin, the principal matrix protein in normal

An amelogenin gene defect associated with human X-linked amelogenesis imperfecta.

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Identifikohuni Regjistrohu

Dental enamel is a product of ameloblast cells, which secrete a mineralizing organic matrix, composed primarily of amelogenin proteins. The amelogenins are thought to be crucial for development of normal, highly mineralized enamel. The X-chromosomal amelogenin gene is a candidate gene for those

A missense mutation of Leu74Pro of OGR1 found in familial amelogenesis imperfecta actually causes the loss of the pH-sensing mechanism.

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Ovarian cancer G protein-coupled receptor 1 (OGR1), also known as GPR68, is a proton-sensing G protein-coupled receptor (GPCR) coupling to G_q/11/phospholipase C/Cap>2+p> signaling pathways. The specific histidine residues at the extracellular surface of OGR1 are suggested to be

Altered self-assembly and apatite binding of amelogenin induced by N-terminal proline mutation.

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OBJECTIVE A single Pro-70 to Thr (p.P70T) mutation of amelogenin is known to result in hypomineralised amelogenesis imperfecta (AI). This study aims to test the hypothesis that the given mutation affects the self-assembly of amelogenin molecules and impairs their ability to conduct the growth of

Evolutionary analysis of selective constraints identifies ameloblastin (AMBN) as a potential candidate for amelogenesis imperfecta.

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Identifikohuni Regjistrohu

BACKGROUND Ameloblastin (AMBN) is a phosphorylated, proline/glutamine-rich protein secreted during enamel formation. Previous studies have revealed that this enamel matrix protein was present early in vertebrate evolution and certainly plays important roles during enamel formation although its

Transgenic mice that express normal and mutated amelogenins.

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Identifikohuni Regjistrohu

Amelogenin proteins are secreted by ameloblasts within the enamel organ during tooth development. To better understand the function of the 180-amino-acid amelogenin (M180), and to test the hypothesis that a single proline-to-threonine (P70T) change would lead to an enamel defect similar to

Molecular evolution of amelogenin in mammals.

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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

Specialized biology from tandem beta-turns.

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Diverse forms of pathologies can be derived from the lack of flexibility in tissues and the absence of required concentrations of certain types of proteins (e.g., amelogenesis imperfecta). beta-spirals using canonical proline-nucleated beta-turns in diverse proteins allow for vital functions

The enamel protein amelogenin binds to the N-acetyl-D-glucosamine-mimicking peptide motif of cytokeratins.

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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

Amelogenin-cytokeratin 14 interaction in ameloblasts during enamel formation.

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The enamel protein amelogenin binds to the GlcNAc-mimicking peptide (GMp) (Ravindranath, R. M. H., Tam, W., Nguyen, P., and Fincham, A. G. (2000) J. Biol. Chem. 275, 39654-39661). The GMp motif is found in the N-terminal region of CK14, a differentiation marker for ameloblasts. The binding affinity

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