Self-Assembly of a Recombinant Amelogenin Protein Generates Supramolecular Structures

Fincham, Alan G.; Moradian‐Oldak, Janet; Simmer, James P.; Sarte, Patrick; Lau, Eduardo C.; Diekwisch, Thomas G.H.; Slavkin, Harold C.

doi:10.1006/jsbi.1994.1011

Cited by 243 publications

(201 citation statements)

References 0 publications

Supporting

Mentioning

186

Contrasting

Unclassified

Order By: Relevance

“…Roles in nucleation, growth, regulation of crystal size and shape, and control of crystal-crystal aggregation have been proposed [2][3][4][5]. Amelogenin is unique in that it self-assembles into nanospheres, supra-molecular structures observed in vitro [6][7][8] and in vivo [7,9] which are believed to be critical to the function of the protein. Several in vivo studies using antisense mice [10], knock out mice [11], transgenic mice [12], and hammerhead ribozymes [13] have investigated the role of amelogenin in regulating enamel nucleation and growth.…”

Section: Introductionmentioning

confidence: 99%

The nucleation and growth of calcium phosphate by amelogenin

Tarasevich

Howard

Larson

et al. 2007

Journal of Crystal Growth

View full text Add to dashboard Cite

The nucleation processes involved in calcium phosphate formation in tooth enamel are not well understood but are believed to involve proteins in the extracellular matrix. The ability of one enamel protein, amelogenin, to promote the nucleation and growth of calcium phosphate was studied in an in vitro system involving metastable supersaturated solutions. It was found that recombinant amelogenin (rM179 and rp(H)M180) promoted the nucleation of calcium phosphate compared to solutions without protein. The amount of calcium phosphate increased with increasing supersaturation of the solutions and increasing protein concentrations up to 6.5 μg/mL. At higher protein concentrations, the amount of calcium phosphate decreased. The kinetics of nucleation was studied in situ and in real time using a quartz crystal microbalance (QCM) and showed that the protein reduced the induction time for nucleation compared to solutions without protein. This work shows a nucleation role for amelogenin in vitro which may be promoted by the association of amelogenin into nanosphere templates, exposing charged functionality at the surface.

show abstract

Section: Introductionmentioning

confidence: 99%

The nucleation and growth of calcium phosphate by amelogenin

Tarasevich

Howard

Larson

et al. 2007

Journal of Crystal Growth

View full text Add to dashboard Cite

show abstract

“…Amelogenin protein is the major component of developing mammalian enamel, in which it represents approximately 90% of the protein content (Termine et al 1980;Fincham et al 1983Fincham et al , 1994Sasaki and Shimokawa 1995). Being such a predominant protein of the organic matrix, amelogenin plays essential roles in structuring developing enamel, but its organization and the exact contribution of its various residues to its function are still poorly understood.…”

Section: Introductionmentioning

confidence: 99%

Molecular Evolution of Amelogenin in Mammals

2005

View full text Add to dashboard Cite

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.

show abstract

“…They comprise 90% of the developing extracellular enamel matrix proteins (Termine et al, 1980) and play a major role in the biomineralization and structural organization of enamel (Robinson et al, 1998;Fincham et al, 1999). Amelogenins are hydrophobic molecules that self-assemble in vitro and in vivo into nanospheric structures, which regulate the oriented and elongated growth, shape, and size of the enamel mineral crystal (Fincham et al, 1994;Du et al, 2005). During enamel development and mineralization, the abundant secreted amelogenins in the extracellular enamel are sequentially and discretely degraded by specific proteases, the metalloprotease Enamelysin (MMP20) and the serine protease EMSP1 (KLK4) (Simmer and Hu, 2002).…”

mentioning

confidence: 99%

Amelogenin expression in long bone and cartilage cells and in bone marrow progenitor cells

Haze

Taylor

Blumenfeld

et al. 2007

The Anatomical Record

View full text Add to dashboard Cite

The amelogenin protein is considered as the major molecular marker of developing ectodermal enamel. Recent data suggest other roles for amelogenin beyond structural regulation of enamel mineral crystal growth. Here we describe our novel discovery of amelogenin expression in long bone cells, in cartilage cells, in cells of the epiphyseal growth plate, and in bone marrow stromal cells. Anat Rec, 290:455-460, 2007. 2007 Wiley-Liss, Inc.

show abstract

Self-Assembly of a Recombinant Amelogenin Protein Generates Supramolecular Structures

Cited by 243 publications

References 0 publications

The nucleation and growth of calcium phosphate by amelogenin

The nucleation and growth of calcium phosphate by amelogenin

Molecular Evolution of Amelogenin in Mammals

Amelogenin expression in long bone and cartilage cells and in bone marrow progenitor cells

Contact Info

Product

Resources

About