scholarly journals The effect of enamel proteins on erosion

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
T. Baumann ◽  
T. S. Carvalho ◽  
A. Lussi
Keyword(s):  
Enamel Proteins

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.

Ultrastructural studies and immunolocalization of enamel proteins in rodent secretory stage ameloblasts processed by various cryofixation methods

1994 ◽  
Vol 238 (4) ◽  
pp. 425-436 ◽  
Author(s):  
A. Nanci ◽  
H. Kawaguchi ◽  
Y. Kogaya
Keyword(s):  
Ultrastructural Studies ◽  
Enamel Proteins

Diffraction studies of enamel proteins and crystals: Their structural relations

Bone ◽  
1986 ◽  
Vol 7 (5) ◽  
pp. 394
Author(s):  
A. Jodaikin ◽  
W. Traub ◽  
S. Weiner ◽  
Y. Talmon ◽  
E. Grossman ◽  
...  
Keyword(s):  
Enamel Proteins ◽  
Structural Relations

The presence of protein phosphokinase in connective tissues and the phosphorylation of enamel proteins in vitro

1965 ◽  
Vol 97 (1) ◽  
pp. 77-87 ◽  
Author(s):  
Stephen M. Krane ◽  
Marcia J. Stone ◽  
Melvin J. Glimcher
Keyword(s):  
Connective Tissues ◽  
Enamel Proteins

Immunohistochemical demonstration of enamel proteins in odontogenic tumors

1992 ◽  
Vol 21 (3) ◽  
pp. 113-119 ◽  
Author(s):  
T. Saku ◽  
H. Okabe ◽  
H. Shimokawa
Keyword(s):  
Odontogenic Tumors ◽  
Immunohistochemical Demonstration ◽  
Enamel Proteins

scholarly journals Expression of Enamel Proteins in Rough Endoplasmic Reticulum and Golgi Complex in Human Dental Germs

2017 ◽  
Vol 35 (2) ◽  
pp. 435-441
Author(s):  
Francisco Javier Gutiérrez-Cantú ◽  
Alma Lilián Guerrero-Barrera ◽  
Wulfrano Sánchez Meraz ◽  
Amaury de Jesús Pozos-Guillen ◽  
Héctor Flores-Reyes ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Rough Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Enamel Proteins

Immunoblot detection and expression of enamel proteins at the apical portion of the forming root in porcine permanent incisor tooth germs

2001 ◽  
Vol 19 (4) ◽  
pp. 236-243 ◽  
Author(s):  
Makoto Fukae ◽  
Takako Tanabe ◽  
Yasuo Yamakoshi ◽  
Marie Yamada ◽  
Yuko Ujiie ◽  
...  
Keyword(s):  
Incisor Tooth ◽  
Apical Portion ◽  
Enamel Proteins ◽  
Tooth Germs

scholarly journals IMMUNOCHEMICAL AND IMMUNOCYTOCHEMICAL STUDY OF A 15 kDa NON-AMELOGENIN AND RELATED PROTEINS IN THE PORCINE IMMATURE ENAMEL: PROPOSAL OF A NEW GROUP OF ENAMEL PROTEINS ‘SHEATH PROTEINS’

1995 ◽  
Vol 16 (3) ◽  
pp. 131-140 ◽  
Author(s):  
TAKASHI UCHIDA ◽  
MAKOTO FUKAE ◽  
TAKAKO TANABE ◽  
YASUO YAMAKOSHI ◽  
TAKAHIRO SATODA ◽  
...  
Keyword(s):  
Immunocytochemical Study ◽  
Enamel Proteins ◽  
Related Proteins

Alteration of Enamel Proteins in Hypomaturation Amelogenesis Imperfecta

1989 ◽  
Vol 68 (9) ◽  
pp. 1328-1330 ◽  
Author(s):  
J.T. Wright ◽  
W.T. Butler
Keyword(s):  
Amino Acid ◽  
Autosomal Recessive ◽  
Amino Acid Profile ◽  
Amelogenesis Imperfecta ◽  
Healthy Controls ◽  
Diverse Group ◽  
Primary Defect ◽  
Autosomal Recessive Condition ◽  
Enamel Protein ◽  
Enamel Proteins

Amelogenesis imperfecta (AI) is a diverse group of disorders that affects primarily the enamel of teeth through a number of developmental processes. The purpose of this study was to characterize the enamel proteins in normal enamel and in hypomaturation AI enamel. Impacted teeth, which were at similar stages of development, were obtained for analysis from an individual with Al and from normal healthy controls. Evaluation of the amino acid profile and quantity of organic material collected showed that there was an excess of enamel protein material that had an amelogenin-like amino acid profile in mature hypomaturation AI enamel. The AI enamel protein content was 5%, while the control enamel had 0.1% protein (by weight). These findings indicate that the maturation process had been altered in this type of AI, and that maturation did not progress beyond the initial stages of secondary mineralization. Since this disorder is inherited as an autosomal recessive condition, it seems likely that the primary defect involves an abnormality in the mechanism for protein removal in enamel maturation.

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