Potential of Treated Dentin Matrix Xenograft for Dentin-Pulp Tissue Engineering

Hengameh Bakhtiar; Amir Mazidi; Saeed Mohammadi-Asl; Sadegh Hasannia; Mohammad Reza Ellini; Mohammad Pezeshki-Modaress; Seyed Naser Ostad; Kerstin Galler; Amir Azarpazhooh; Anil Kishen

doi:10.1016/j.joen.2019.10.005

Potential of Treated Dentin Matrix Xenograft for Dentin-Pulp Tissue Engineering

J Endod. 2020 Jan;46(1):57-64.e1. doi: 10.1016/j.joen.2019.10.005. Epub 2019 Nov 20.

Affiliations

¹ Department of Endodontics, Faculty of Dentistry, Tehran Medical Sciences, Islamic Azad University, Tehran, Iran; Faculty of Dentistry, University of Toronto, Toronto, Ontario, Canada; Stem Cell Research Center, Tissue Engineering and Regenerative Medicine Institute, Tehran Central Branch, Islamic Azad University, Tehran, Iran.
² Student Research Committee, Faculty of Dentistry, Tehran Medical Sciences, Islamic Azad University, Tehran, Iran.
³ Department of Clinical Biochemistry, Tarbiat Modarres University, Tehran, Iran.
⁴ Burn Research Center, Iran University of Medical Sciences, Tehran, Iran.
⁵ Department of Toxicology-Pharmacology, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran.
⁶ Department of Conservative Dentistry and Periodontology, University Hospital Regensburg, Regensburg, Germany.
⁷ Faculty of Dentistry, University of Toronto, Toronto, Ontario, Canada; Department of Dentistry, Mount Sinai Hospital, Toronto, Ontario, Canada; Clinical Epidemiology and Health Care Research, Institute of Health Policy, Management and Evaluation, University of Toronto, Toronto, Ontario, Canada.
⁸ Faculty of Dentistry, University of Toronto, Toronto, Ontario, Canada; Department of Dentistry, Mount Sinai Hospital, Toronto, Ontario, Canada. Electronic address: Anil.Kishen@dentistry.utoronto.ca.

PMID: 31759677
DOI: 10.1016/j.joen.2019.10.005

Abstract

Introduction: This study aims to develop and characterize the regenerative potential of an atelopeptidized treated dentin matrix xenograft using in vitro and in vivo models.

Methods: Freshly extracted bovine dentin was pulverized into 250- to 500-μm particles and demineralized with 17% EDTA for 1, 7, and 13 days. The samples were atelopeptidized with pepsin. The degree of demineralization and the effect of atelopeptidization were assessed using field emission scanning electron microscopy combined with energy-dispersive X-ray spectroscopy and Fourier transform infrared spectroscopy, respectively. The expression of dentin matrix acidic phosphoprotein 1, dentin sialophosphoprotein, and osteopontin was evaluated in dental pulp stem cells using quantitative real-time polymerase chain reaction. The samples were then implanted intramuscularly in rats for 30 days, and the inflammatory cells were quantified histologically.

Results: Field emission scanning electron microscopy combined with energy-dispersive X-ray spectroscopy revealed an exposed tubular structure of dentin after 1 and 7 days of demineralization. Fourier transform infrared spectroscopy confirmed the absence of amide peaks at 1260 to 1640/cm after atelopeptidization. The dental pulp stem cell expression of dentin matrix acidic phosphoprotein 1 and dentin sialophosphoprotein increased in all compared with the untreated control group (P < .05). The maximum expression rates were observed for the 1-day demineralized and atelopeptidized group. The 1-day demineralized group elicited the highest inflammatory response compared with the 7- or 13-day demineralized groups (P < .001). Atelopeptidization significantly decreased the inflammatory response only in the 1-day demineralized dentin group (P < .05).

Conclusions: Atelopeptidization of 1-day demineralized dentin xenograft preserved the collagen structure, minimized the immune reaction, and provided sufficient regenerative potential.

Keywords: Atelopeptidization; demineralization; dentin-pulp complex; regeneration; treated dentin matrix; xenograft.

MeSH terms

Animals
Cattle
Dental Pulp*
Dentin* / transplantation
Heterografts*
Microscopy, Electron, Scanning
Peptides
Rats
Tissue Engineering*

Substances

Peptides