TY - JOUR
T1 - Synthesis and intracellular transportation of type i procollagen during functional differentiation of odontoblasts
AU - Sato, Shigehisa
AU - Tsuchiya, Masahiro
AU - Komaki, Ken Ichiro
AU - Kusunoki, Shin Ichiro
AU - Tsuchiya, Shinobu
AU - Haruyama, Naoto
AU - Takahashi, Ichiro
AU - Sasano, Yasuyuki
AU - Watanabe, Makoto
N1 - Funding Information:
Acknowledgments We wish to thank Dr. Yosuke Akiba (The Burke Medical Research Institute, White Plains, NY, USA) and other members in the Division of Aging and Geriatric Dentistry, Tohoku University Graduate School of Dentistry, for their excellent assistance with this study. This work was supported in part by grants-in-aid (19659500, 19791420) from the Ministry of Education, Science, Sports and Culture of Japan.
PY - 2009/5
Y1 - 2009/5
N2 - 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.
AB - 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.
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U2 - 10.1007/s00418-009-0556-6
DO - 10.1007/s00418-009-0556-6
M3 - Article
C2 - 19156436
AN - SCOPUS:63949088107
SN - 0948-6143
VL - 131
SP - 583
EP - 591
JO - Histochemistry and Cell Biology
JF - Histochemistry and Cell Biology
IS - 5
ER -