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Dive into the research topics where Tchilalo Boukpessi is active.

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Featured researches published by Tchilalo Boukpessi.


Journal of Endodontics | 2009

Prevalence of Apical Periodontitis in Root Canal–Treated Teeth From an Urban French Population: Influence of the Quality of Root Canal Fillings and Coronal Restorations

Paula B.L. Tavares; Eric Bonte; Tchilalo Boukpessi; José F. Siqueira; Jean-Jacques Lasfargues

This cross-sectional study determined the prevalence of apical periodontitis in 1035 root canal-treated teeth from adult French patients and investigated the influence of the quality of canal fillings and coronal restorations on the periradicular status. Periapical radiographs were used for analyses, and teeth were classified as healthy or diseased according to the periapical index scoring system. Overall, the prevalence of apical periodontitis in root canal-treated teeth was 33%. Only 19% of the teeth had endodontic treatments rated as adequate. The success rate (number of healthy teeth) for cases with adequate endodontic treatment was 91%, which was significantly higher when compared with teeth with inadequate treatment (61%). Teeth with adequate restorations had significantly decreased prevalence of apical periodontitis (29%) as compared with teeth with inadequate restorations (41%). The combination of adequate endodontic treatment and adequate restorations yielded the highest success rate (93.5%). The quality of the endodontic treatment was the most important factor for success, although the quality of the coronal restoration also influenced the treatment outcome.


Biomaterials | 2008

The effect of stromelysin-1 (MMP-3) on non-collagenous extracellular matrix proteins of demineralized dentin and the adhesive properties of restorative resins

Tchilalo Boukpessi; S. Menashi; L. Camoin; J.M. TenCate; Michel Goldberg; C. Chaussain-Miller

Dentin non-collagenous matrix components (NCPs) are structural proteins involved in the formation, the architecture and the mineralization of the extracellular matrix (ECM). We investigated here how recombinant metalloproteinase stromelysin-1, also termed MMP-3, initiates the release of ECM molecules from artificially demineralized human dentin. Analysis of the supernatants by Western blotting reveals that MMP-3 extracts PGs (decorin, biglycan), and also a series of phosphorylated proteins: dentin sialoprotein (DSP), osteopontin (OPN), bone sialoprotein (BSP) and MEPE, but neither dentin matrix protein-1 (DMP1), another member of the SIBLING family, nor osteocalcin (OC), a non-phosphorylated matrix molecule. After treatment of dentin surfaces by MMP-3, scanning electron microscope (SEM) examination of resin replica shows an increased penetration of the resin into the dentin tubules when compared to surfaces only treated by demineralizing solutions. This preclinical investigation suggests that MMP-3 may be used to improve the adhesive properties of restorative materials.


Frontiers in Physiology | 2013

Dentin matrix degradation by host matrix metalloproteinases: inhibition and clinical perspectives toward regeneration

Catherine Chaussain; Tchilalo Boukpessi; Mayssam Khaddam; Leo Tjäderhane; Anne George; Suzanne Menashi

Bacterial enzymes have long been considered solely accountable for the degradation of the dentin matrix during the carious process. However, the emerging literature suggests that host-derived enzymes, and in particular the matrix metalloproteinases (MMPs) contained in dentin and saliva can play a major role in this process by their ability to degrade the dentin matrix from within. These findings are important since they open new therapeutic options for caries prevention and treatment. The possibility of using MMP inhibitors to interfere with dentin caries progression is discussed. Furthermore, the potential release of bioactive peptides by the enzymatic cleavage of dentin matrix proteins by MMPs during the carious process is discussed. These peptides, once identified, may constitute promising therapeutical tools for tooth and bone regeneration.


American Journal of Pathology | 2010

Abnormal Presence of the Matrix Extracellular Phosphoglycoprotein-Derived Acidic Serine- and Aspartate-Rich Motif Peptide in Human Hypophosphatemic Dentin

Tchilalo Boukpessi; C. Gaucher; Thibaut Léger; Benjamin Salmon; Julie Le Faouder; Cyril Willig; Peter S. N. Rowe; Michèle Garabédian; Olivier Meilhac; Catherine Chaussain

Severe dental troubles are associated with X-linked hypophosphatemic rickets and are mainly related to impaired dentin mineralization. In dentin matrix, matrix extracellular phosphoglycoprotein (MEPE) may be protected from proteolysis by a specific interaction with PHEX (phosphate regulating gene with homologies to endopeptidases on the X chromosome). The objective of our work was to determine whether PHEX impairment induces MEPE cleavage in dentin and the subsequent release of the C-terminal acidic serine- and aspartate-rich motif (ASARM) peptide, which is known to inhibit mineralization. By Western blot analysis, we explored dentin extracts from seven hypophosphatemic patients with mutations of the PHEX gene. A proteomic approach combining immunoprecipitation, surface-enhanced laser desorption/ionization-time of flight-mass spectrometry and matrix-assisted laser desorption ionization-time of flight analysis of the samples completed this exploration. This study shows a 4.1-kDa peptide containing the MEPE-derived ASARM peptide in hypophosphatemic samples. The presence of ASARM was less marked in patients treated with 1-hydroxylated vitamin D and phosphate during growth. Moreover, recombinant ASARM implanted in a rat pulp injury model disturbed the formation of the reparative dentin bridge. These results suggest that abnormal MEPE cleavage occurs when PHEX activity is deficient in humans, the ASARM peptide may be involved in the mineralization defects and the PHEX-MEPE interaction may be indirect, as ensuring a better phosphate and vitamin D environment to the mineralizing dentin prevents MEPE cleavage.


Cells Tissues Organs | 2009

Dentin noncollagenous matrix proteins in familial hypophosphatemic rickets.

C. Gaucher; Tchilalo Boukpessi; Dominique Septier; Frédéric Jehan; Peter S. N. Rowe; Michèle Garabédian; Michel Goldberg; Catherine Chaussain-Miller

Familial hypophosphatemic rickets is transmitted in most cases as an X-linked dominant trait and results from the mutation of the PHEX gene predominantly expressed in osteoblast and odontoblast. Patients with rickets have been reported to display important dentin defects. Our purpose was to explore the structure, composition and distribution of noncollagenous proteins (NCPs) of hypophosphatemic dentin. We collected teeth from 10 hypophosphatemic patients whose mineralization occurred either in a hypophosphatemic environment or in a corrected phosphate and vitamin environment. Teeth were examined by scanning electron microscopy, immunohistochemistry and Western blot analysis. An abnormal distribution (accumulation in interglobular spaces) and cleavage of the NCPs and particularly of matrix extracellular phosphoglycoprotein were observed in deciduous dentin. In contrast, it was close to normal in permanent dentin mineralized under corrected conditions. In conclusion, dentin mineralization in a corrected phosphate and vitamin D environment compensates the adverse effect of PHEX mutation.


Frontiers in Physiology | 2014

Grape seed extracts inhibit dentin matrix degradation by MMP-3

Mayssam Khaddam; Benjamin Salmon; Dominique Le Denmat; Leo Tjäderhane; Suzanne Menashi; Catherine Chaussain; Gaël Y. Rochefort; Tchilalo Boukpessi

Since Matrix metalloproteinases (MMPs) have been suggested to contribute to dentin caries progression, the hypothesis that MMP inhibition would affect the progression of dentin caries is clinically relevant. Grape seed extracts (GSE) have been previously reported to be natural inhibitors of MMPs. Objective: To evaluate the capacity of a GSE mouthrinse to prevent the degradation of demineralized dentin matrix by MMP-3 (stromelysin-1). Materials and Methods: Standardized blocks of dentin obtained from sound permanent teeth extracted for orthodontic reasons were demineralized with Ethylenediaminetetraacetic acid (EDTA) and pretreated either with (A) GSE (0.2% w/v), (B) amine fluoride (AmF) (20% w/v), (C) a mouthrinse which contains both, (D) placebo, (E) sodium fluoride (0.15 mg.ml−1), (F) PBS, (G) Chlorhexidine digluconate (CHX), or (H) zinc chloride (ZnCl2). The dentin blocks were then incubated with activated recombinant MMP-3. The supernatants were analyzed by Western Blot for several dentin matrix proteins known to be MMP-3 substrate. In parallel, scanning electron microscopy (SEM) was performed on resin replica of the dentin blocks. Results: Western blot analysis of the supernatants revealed that MMP-3 released from the dentin matrix small proteoglycans (decorin and biglycan) and dentin sialoprotein (DSP) in the AmF, sodium fluoride, PBS and placebo pretreated groups, but not in the GSE and mouthrinse pretreated groups. SEM examination of resin replica showed that the mouthrinse and its active components not only had an anti-MMP action but also modified the dentin surface accessibility. Conclusion: This study shows that GSE either alone or combined with AmF as in the evaluated mouthrinse limits dentin matrix degradation. This association may be promising to prevent the progression of caries within dentin. However, the procedure should be adapted to clinically relevant durations.


Archive | 2017

Endogenous Enzymes in Root Caries

Tchilalo Boukpessi; Suzanne Menashi; Catherine Chaussain

Similar to coronal caries, root caries results from a disequilibrium of the de-remineralization balance in favor of the demineralization process. It mainly involves a bacterial shift in favor of an increase in the proportion of acidogenic and aciduric bacteria. This process permanently damages the dental mineralized tissues, namely the dental cementum and dentin. In addition to the demineralization and exposure of the dentin or the cementum organic matrix, acid production by cariogenic bacteria induces the activation of endogenous (host-derived) enzymes within the dentin and saliva. These enzymes include matrix metalloproteinases and cathepsins. Once activated, these potent proteolytic enzymes collectively have the capacity to degrade all the components of the exposed organic dentin and cementum matrices. In this chapter, the description of the healthy cement and dentin organic matrices and their endogenous proteases will be followed by the role of these proteases in the root caries process.


Dentistry 3000 | 2017

Endodontic Management of Patients With X Linked Hypophosphatemic Rickets:Case Series Report

Tchilalo Boukpessi; Mahdi Altabah; Catherine Chaussain; Agnès Linglart

Introduction: Familial hypophosphatemic rickets, the most common cause of inherited rickets, is in most cases transmitted as an X-linked dominant trait resulting from a mutation of the phosphate-regulating gene with homologies to endopeptidases on the X chromosome gene. This condition impairs bone, cement and dentin mineralization, resulting in skeletal and oral manifestations. Patients present spontaneous tooth abscesses that occur without any history of trauma or dental decay. Methods: Two XLH patients were referred to the endodontic department of Charles Foix Hospital. They reported history of multiple dental abscesses. The clinical and radiographic examination showed periapical lesions of central left mandibular incisor and first and second maxillary left molars. Furthermore, the radiographic examination showed enlarged pulp chambers, thin enamel and dentin. Conservative endodontic treatment was performed in the necrotic teeth. Results: The clinical and radiographic follow-up showed a bone healing in process in these two cases.


Clinical Oral Investigations | 2015

MTA versus Ca(OH)2 in apexification of non-vital immature permanent teeth: a randomized clinical trial comparison

Eric Bonte; Aurélie Beslot; Tchilalo Boukpessi; Jean-Jacques Lasfargues


Bone | 2010

Mepe-derived asarm peptide impairs dentin mineralization

Benjamin Salmon; C. Gaucher; Tchilalo Boukpessi; Thibaut Léger; Peter S. N. Rowe; Anne Poliard; Michèle Garabédian; Olivier Meilhac; Catherine Chaussain

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Benjamin Salmon

Paris Descartes University

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C. Gaucher

Paris Descartes University

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Eric Bonte

Paris Descartes University

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Mayssam Khaddam

Paris Descartes University

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Michel Goldberg

Paris Descartes University

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Olivier Meilhac

University of La Réunion

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