Enamel Protein Amelotin-Coated Nano Hydroxyapatite for Accelerated Dentin Remineralization

2020 ◽  
Author(s):  
Mehrnoosh Neshatian ◽  
James Holcroft ◽  
Anil Kishen ◽  
Bernhard Ganss
Keyword(s):  
Enamel Protein

Relative Levels of mRNA Encoding Enamel Proteins in Enamel Organ Epithelia and Odontoblasts

2003 ◽  
Vol 82 (12) ◽  
pp. 982-986 ◽  
Author(s):  
T. Nagano ◽  
S. Oida ◽  
H. Ando ◽  
K. Gomi ◽  
T. Arai ◽  
...  
Keyword(s):  
Tooth Enamel ◽  
Structural Proteins ◽  
Enamel Organ ◽  
Maturation Stage ◽  
Mrna Levels ◽  
Rt Pcr ◽  
Enamel Protein ◽  
Enamel Proteins ◽  
Enamel Layer

Amelogenin, enamelin, sheathlin (ameloblastin/ amelin), enamelysin (MMP-20), and KLK4 (EMSP-1) are the major structural proteins and proteinases in developing tooth enamel. Recently, odontoblasts were reported to express amelogenin, the most abundant enamel protein. In this study, we hypothesized that odontoblasts express all enamel proteins and proteases, and we measured their relative mRNA levels in enamel organ epithelia and odontoblasts associated with porcine secretory- and maturation-stage enamel by RT-PCR, using a LightCycler instrument. The results showed that amelogenin mRNA in secretory-stage EOE is 320-fold higher than in odontoblasts beneath secretory-stage enamel, and over 20,000-fold higher than in odontoblasts under maturation-stage enamel. Similar results were obtained for enamelin and sheathlin. Enamelysin mRNA levels were equivalent in these two tissues, while KLK4 mRNA was higher in odontoblasts than in secretory-stage EOE. These results support the conclusion that odontoblasts are involved in the formation of the enamel layer adjacent to enamel-dentin junction.

scholarly journals Functions of KLK4 and MMP-20 in dental enamel formation

2008 ◽  
Vol 389 (6) ◽  
Author(s):  
Yuhe Lu ◽  
Petros Papagerakis ◽  
Yasuo Yamakoshi ◽  
Jan C.-C. Hu ◽  
John D. Bartlett ◽  
...  
Keyword(s):  
Autosomal Recessive ◽  
Dental Enamel ◽  
Organic Matrix ◽  
Maturation Stage ◽  
Protein Cleavage ◽  
Enamel Formation ◽  
Residual Protein ◽  
Kallikrein 4 ◽  
Enamel Protein ◽  
Enamel Proteins

Abstract Two proteases are secreted into the enamel matrix of developing teeth. The early protease is enamelysin (MMP-20). The late protease is kallikrein 4 (KLK4). Mutations in MMP20 and KLK4 both cause autosomal recessive amelogenesis imperfecta, a condition featuring soft, porous enamel containing residual protein. MMP-20 is secreted along with enamel proteins by secretory-stage ameloblasts. Enamel protein-cleavage products accumulate in the space between the crystal ribbons, helping to support them. MMP-20 steadily cleaves accumulated enamel proteins, so their concentration decreases with depth. KLK4 is secreted by transition- and maturation-stage ameloblasts. KLK4 aggressively degrades the retained organic matrix following the termination of enamel protein secretion. The principle functions of MMP-20 and KLK4 in dental enamel formation are to facilitate the orderly replacement of organic matrix with mineral, generating an enamel layer that is harder, less porous, and unstained by retained enamel proteins.

Normal Mature Human Enamel Protein

1979 ◽  
Vol 58 (2_suppl) ◽  
pp. 986-987 ◽  
Author(s):  
A. Belcourt
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Gel Electrophoresis ◽  
Protein Concentration ◽  
Polyacrylamide Gel Electrophoresis ◽  
Organic Matrix ◽  
Low Molecular Weight ◽  
Human Enamel ◽  
Weak Density ◽  
Enamel Protein

Pure enamel was prepared using an original microdissection technic. Protein concentration was 375 μg per gram of enamel. Polyacrylamide gel electrophoresis showed a single fast-migrating zone containing a thin double band. Ultracentrifugation studies suggested that the proteins were of low molecular weight or of weak density. Absorption spectra showed a strong absorbance at 260nm. Amino acid analyses yielded a composition of 25% Gly, 13.5% Glu, 11% Ser, 11% Pro, 2% Cys and 2% Hyp. A glucidic content of 15% was estimated and glucose, galactose, mannose and fucose were identified. The organic matrix of enamel seemed to be constituted of two major glycoproteins probably fibrous but different from keratin.

Epigenetic Regulation of Enamel Protein Synthesis during Epithelial-Mesenchymal Interactions

1977 ◽  
pp. 209-226 ◽  
Author(s):  
HAROLD C. SLAVKIN ◽  
GARY N. TRUMP ◽  
STEVEN SCHONFELD ◽  
ANNA BROWNELL ◽  
NINO SORGENTE ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Epigenetic Regulation ◽  
Enamel Protein

scholarly journals Enamel Protein

1939 ◽  
Vol 32 (5) ◽  
pp. 513-518 ◽  
Author(s):  
Paul Pincus
Keyword(s):  
Enamel Protein

scholarly journals Controls of nature: Secondary, tertiary, and quaternary structure of the enamel protein amelogenin in solution and on hydroxyapatite

2020 ◽  
Vol 212 (3) ◽  
pp. 107630
Author(s):  
Wendy J. Shaw ◽  
Barbara J. Tarasevich ◽  
Garry W. Buchko ◽  
Rajith M.J. Arachchige ◽  
Sarah D. Burton
Keyword(s):  
Quaternary Structure ◽  
Enamel Protein

Amino Acid Sequence of a Major Human Amelogenin Protein Employing Edman Degradation and cDNA Sequencing

1993 ◽  
Vol 72 (12) ◽  
pp. 1566-1572 ◽  
Author(s):  
J. Catalano-Sherman ◽  
A. Palmon ◽  
Y. Burstein ◽  
D. Deutsch
Keyword(s):  
Present Report ◽  
Complete Sequence ◽  
Edman Degradation ◽  
Cdna Sequencing ◽  
Cdna Sequences ◽  
Coding Regions ◽  
Major Class ◽  
Human Enamel ◽  
Sequencing Studies ◽  
Enamel Protein

The abundant hydrophobic, proline-glutamine, and histidine-rich (over 90%) amelogenins constitute the major class of proteins in forming extracellular enamel matrix. These are thought to play a major role in the structural organization and mineralization of developing enamel. The present report describes the successful sequencing of the major human amelogenin protein, by use of both Edman degradation and cDNA sequencing. When Edman degradation was used, over 75% of the primary structure of the protein was determined. This sequence was supplemented with cDNA sequencing studies, which revealed the predicted sequence of this protein. Together, they provide the complete sequence of an important human enamel protein. The information complements recent studies on bovine and human amelogenin genes. A comparison between the present results and the protein sequences predicted from the corresponding human amelogenin genomic coding regions and that of cDNA sequences of other species is described.

"Proenamel → Enamel → Polypeptides": A Concept

1979 ◽  
Vol 58 (2_suppl) ◽  
pp. 988-990 ◽  
Author(s):  
J. Chrispens ◽  
B. Weliky ◽  
P. Bringas ◽  
H. Slavkin
Keyword(s):  
New Zealand ◽  
Developmental Stage ◽  
Protein Gene ◽  
Protein S ◽  
Molar Tooth ◽  
Matrix Proteins ◽  
Gene Products ◽  
Enamel Matrix ◽  
Enamel Matrix Proteins ◽  
Enamel Protein

Our laboratory is interested in determining the number of enamel protein gene products which characterize the ameloblast phenotype, and to what extent these proteins are degraded as a function of enamel maturation. Many investigators have reported a large number of heterogeneous proteins within the enamel matrix (Eggert, Allen and Burgess, 1973; Weidmann and Eyre, 1971). One explanation for this apparent heterogeneity may be the uncertain age of the analyzed enamel matrix; specimens may have undergone degradative processes associated with enamel maturation. To overcome this difficulty, our laboratory selected 26-day embryonic New Zealand White (NZW) rabbit incisor and molar tooth organs to isolate enamel protein(s). At this developmental stage it is possible to identify newly-secreted enamel matrix proteins.

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