Amelogenins: assembly, processing and control of crystal morphology

Moradian‐Oldak, Janet

doi:10.1016/s0945-053x(01)00154-8

Cited by 198 publications

(235 citation statements)

References 54 publications

Supporting

Mentioning

226

Contrasting

Unclassified

Order By: Relevance

“…Amelogenin was identified as the main enamel matrix protein comprising 80 -90% that of the total enamel protein (23). Crystal pattern organization and regulation of enamel thickness were suggested to be the functions of amelogenin (23,34). It was shown that the CCAAT/enhancer-binding protein ␣ (C/EBP␣) activated amelogenin expression, and Msx2 functions as a transcriptional repressor of amelogenin expression …”

Section: Discussionmentioning

confidence: 99%

Hierarchical Interactions of Homeodomain and Forkhead Transcription Factors in Regulating Odontogenic Gene Expression

Venugopalan¹,

Li²,

Amen

et al. 2011

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

Section: Discussionmentioning

confidence: 99%

Hierarchical Interactions of Homeodomain and Forkhead Transcription Factors in Regulating Odontogenic Gene Expression

Venugopalan¹,

Li²,

Amen

et al. 2011

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Amelogenin proteins self-assemble into nanospheres and coils which serve as an enamel scaffold. 20 These transient self-assemblies run throughout the enamel layer and guide apatite crystal formation and growth. 21,22 Amelogenin null mice show a significant reduction of enamel thickness which is in addition devoid of prismatic pattern.…”

Section: Msx2mentioning

confidence: 99%

Enamel Protein Regulation and Dental and Periodontal Physiopathology in Msx2 Mutant Mice

Molla

Descroix

Aïoub

et al. 2010

The American Journal of Pathology

View full text Add to dashboard Cite

Signaling pathways that underlie postnatal dental and periodontal physiopathology are less studied than those of early tooth development. Members of the muscle segment homeobox gene (Msx) family encode homeoproteins that show functional redundancy during development and are known to be involved in epithelial-mesenchymal interactions that lead to crown morphogenesis and ameloblast cell differentiation. This study analyzed the MSX2 protein during mouse postnatal growth as well as in the adult. The analysis focused on enamel and periodontal defects and enamel proteins in Msx2-null mutant mice. In the epithelial lifecycle, the levels of MSX2 expression and enamel protein secretion were inversely related. Msx2؉/؊ mice showed increased amelogenin expression, enamel thickness, and rod size. Msx2 ؊/؊ mice displayed compound phenotypic characteristics of enamel defects, related to both enamel-specific gene mutations (amelogenin and enamelin) in isolated amelogenesis imperfecta, and cell-cell junction elements (laminin 5 and cytokeratin 5) in other syndromes. These effects were also related to ameloblast disappearance, which differed between incisors and molars. In Msx2 ؊/؊ roots, Malassez cells formed giant islands that overexpressed amelogenin and ameloblastin that grew over months. Aberrant expression of enamel proteins is proposed to underlie the regional osteopetrosis and hyperproduction of cellular cementum. These enamel and periodontal phenotypes of Msx2 mutants constitute the first case report of structural and signaling defects associated with enamel protein overexpression in a postnatal context.

show abstract

“…Amelogenins are a family of hydrophobic proteins derivable from a single gene by alternative splicing and controlled post secretory processing. The C-terminal region of the protein is composed of a sequence of hydrophilic and charged amino acids [4]. Amelogenin protein interacts, at the extra-cellular level, with calcium and phosphate ions to control the nucleation, growth and organization of the apatite crystals of tooth enamel [1].…”

Section: Introductionmentioning

confidence: 99%

Unbinding Process of Amelogenin and Fibrinogen Adsorbed on Different Solid Surfaces Using AFM

Richert¹,

Boukari²,

Berner³

et al. 2011

JBNB

View full text Add to dashboard Cite

The interaction of proteins with solid surfaces is a fundamental phenomenon in the biomaterials field. We investigated, using atomic force microscopy (AFM), the interactions of a recombinant amelogenin with titanium, a biphasic calcium phosphate (BCP) and mica. The unbinding processes were compared to those of an earlier studied protein, namely fibrinogen. Force spectroscopy (AFM) experiments were carried out at 0 ms, 10 2 ms, 10 3 ms and 10 4 ms of contact time. In general, the rupture forces increased as a function of interaction time. The unbinding forces of amelogenin interacting with the BCP surface were always stronger than those of the amelogenin-titanium system. The unbinding forces of fibrinogen interacting with the BCP surface were always much stronger than those of the fibrinogen-titanium system.For the most part, this study provides direct evidence that recombinant amelogenin binds more strongly than fibrinogen on the studied substrates.

show abstract

Amelogenins: assembly, processing and control of crystal morphology

Cited by 198 publications

References 54 publications

Hierarchical Interactions of Homeodomain and Forkhead Transcription Factors in Regulating Odontogenic Gene Expression

Hierarchical Interactions of Homeodomain and Forkhead Transcription Factors in Regulating Odontogenic Gene Expression

Enamel Protein Regulation and Dental and Periodontal Physiopathology in Msx2 Mutant Mice

Unbinding Process of Amelogenin and Fibrinogen Adsorbed on Different Solid Surfaces Using AFM

Contact Info

Product

Resources

About