Synthesis and intracellular transportation of type I procollagen during functional differentiation of odontoblasts

The expression of type I collagen, the most component of dentin extracellular matrix proteins (ECMs) in odontoblast is correlated with the activity of dentin formation. Since odontoblast possesses a distinct cellular process for protein transport into the dentinal tubule, it is important to examine...

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Veröffentlicht in:Histochemistry and cell biology 2009-05, Vol.131 (5), p.583-591
Hauptverfasser: Sato, Shigehisa, Tsuchiya, Masahiro, Komaki, Ken-ichiro, Kusunoki, Shin-ichiro, Tsuchiya, Shinobu, Haruyama, Naoto, Takahashi, Ichiro, Sasano, Yasuyuki, Watanabe, Makoto
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container_issue 5
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container_title Histochemistry and cell biology
container_volume 131
creator Sato, Shigehisa
Tsuchiya, Masahiro
Komaki, Ken-ichiro
Kusunoki, Shin-ichiro
Tsuchiya, Shinobu
Haruyama, Naoto
Takahashi, Ichiro
Sasano, Yasuyuki
Watanabe, Makoto
description The expression of type I collagen, the most component of dentin extracellular matrix proteins (ECMs) in odontoblast is correlated with the activity of dentin formation. Since odontoblast possesses a distinct cellular process for protein transport into the dentinal tubule, it is important to examine the intracellular protein localization. However, a study focusing on odontoblast processes has not been performed. Type I collagen is synthesized as procollagen, which is immediately converted to collagen upon secretion. After characterization of antiserum to rat type I procollagen, we investigated the intracellular localization of type I procollagen in odontoblasts during and after dentinogenesis, using immunohistochemistry and in situ hybridization. The level of mRNA expression decreased during dentinogenesis, whereas the intracellular localization of type I procollagen in odontoblast processes become more distinct. The percentage of dentinal tubules with type I procollagen increased significantly with aging. Odontoblasts in pulp horn, in particular, showed moderate expression of type I procollagen after dentinogenesis. Since loss of occlusion also caused a significant decrease in type I procollagen, we concluded that occlusal stimulation activated type I procollagen synthesis in odontoblasts. We also suggest that analysis of intracellular transport of type I procollagen via odontoblast processes may be a new approach to evaluation of odontoblast function.
doi_str_mv 10.1007/s00418-009-0556-6
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Since odontoblast possesses a distinct cellular process for protein transport into the dentinal tubule, it is important to examine the intracellular protein localization. However, a study focusing on odontoblast processes has not been performed. Type I collagen is synthesized as procollagen, which is immediately converted to collagen upon secretion. After characterization of antiserum to rat type I procollagen, we investigated the intracellular localization of type I procollagen in odontoblasts during and after dentinogenesis, using immunohistochemistry and in situ hybridization. The level of mRNA expression decreased during dentinogenesis, whereas the intracellular localization of type I procollagen in odontoblast processes become more distinct. The percentage of dentinal tubules with type I procollagen increased significantly with aging. Odontoblasts in pulp horn, in particular, showed moderate expression of type I procollagen after dentinogenesis. 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subjects Aging
Animals
Biochemistry
Biomedical and Life Sciences
Biomedicine
Cell Biology
Cellular biology
Collagen Type I - metabolism
Dentin - cytology
Dentin - metabolism
Dentinogenesis
Developmental Biology
Odontoblasts - cytology
Odontoblasts - metabolism
Original Paper
Osteopontin - metabolism
Protein Transport
Proteins
Rats
Rats, Wistar
Ribonucleic acid
RNA
Rodents
title Synthesis and intracellular transportation of type I procollagen during functional differentiation of odontoblasts
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