Teneurin-2 presence in rat and human odontoblasts.

K R Torres-Da-Silva,C A Dias,I Z Guiati,D A Lovejoy,G W L Tessarin,A Gonçalves,E Ervolino,C A Casatti,I M Beneti

doi:10.1371/journal.pone.0184794

K R Torres-Da-Silva, C A Dias + Show 7 more

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https://doi.org/10.1371/journal.pone.0184794

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Abstract

Teneurins are transmembrane proteins consisting of four paralogues (Ten-1-4), notably expressed in the central nervous system during development. All teneurins contain a bioactive peptide in their carboxyl terminal named teneurin C-terminal associated peptide (TCAP). The present study analyzed the detailed distribution of teneurin-2-like immunoreactive (Ten-2-LI) cells in developing and mature rat molar teeth, as well as in mature human dental pulps. Ten-2 and TCAP-2 genic expressions were also evaluated in rat and human dental pulps. Finally, Ten-2-LI cells were analyzed during the repair process after dentin-pulp complex injury in rat lower molar teeth. For this, histological sections of rat molar teeth and human dental pulps were submitted to immunohistochemical techniques, while total RNA from developing rat teeth and mature human dental pulps were submitted to conventional RT-PCR. Ten-2-LI cells were evident in the initial bell stage of rat molar teeth development, especially in ectomesenchymal cells of the dental papilla. Ten-2-LI odontoblasts showed strong immunoreactivity in rat and human mature teeth. Ten-2 and TCAP-2 genic expressions were confirmed in rat and human dental pulps. Dentin-pulp complex injury resulted in a decrease of Ten-2-LI odontoblasts after traumatic injury. Interestingly, Ten-2-LI cells were also evident in the pulp cell-rich zone in all postoperative days. In conclusion, Ten-2-LI presence in rat and human odontoblasts was demonstrated for the first time and Ten-2/TCAP-2 genic expressions were confirmed in rat and human dental pulps. Furthermore, it was revealed that Ten-2-LI rat odontoblasts can be modulated during the regenerative process.

Highlights

Teneurins represent a type II transmembrane glycoprotein with approximately 2800 amino acids, composed of four paralogues (Ten-1-4) and consisting of a number of splice variants in vertebrates [1,2]
Teneurins are mainly expressed during development of the central nervous system (CNS) in rodents and chicken, their expression pattern persists in certain regions during adulthood
Ten-2 and teneurin C-terminal associated peptide-2 (TCAP-2) genic expressions were evaluated in rat and human dental pulps by conventional room temperature (RT)-polymerase chain reaction (PCR) technique

Summary

Introduction

Teneurins represent a type II transmembrane glycoprotein with approximately 2800 amino acids, composed of four paralogues (Ten-1-4) and consisting of a number of splice variants in vertebrates [1,2]. This protein was initially isolated and characterized in Drosophila melanogaster as a tenascin-like molecule accessory (ten-a) during studies in search of orthologous tenascins (TN), a family of cell-adhesion molecules from the extracellular matrix [1,2]. Teneurins were characterized in several invertebrates (tenascin-like molecule major, ten-m) and vertebrates (odz; Ten1-4) showing considerable structural conservation among species [1,2]. The carboxyl terminal of the teneurins contain a bioactive peptide sequence (40–41 amino acids) with structural similarity to the corticotrophin releasing factor (CRF) named teneurin C-terminal associated peptides (TCAP), related to stress modulation, neuroprotection, among other functions [4,5,6,7,8]

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