Prof. Roberto Di Lenarda
Department of Medicine, Surgery and Health Sciences, University of Trieste, 34127 Trieste, Italy
'%3e%3cpath%20d='M22.1642%2019.0924C21.7317%2018.068%2021.1041%2017.1375%2020.3163%2016.3527C19.5309%2015.5656%2018.6006%2014.9381%2017.5766%2014.5048C17.5674%2014.5002%2017.5582%2014.4979%2017.5491%2014.4933C18.9774%2013.4616%2019.9059%2011.7811%2019.9059%209.88504C19.9059%206.74408%2017.3611%204.19922%2014.2201%204.19922C11.0792%204.19922%208.53429%206.74408%208.53429%209.88504C8.53429%2011.7811%209.46282%2013.4616%2010.8912%2014.4956C10.882%2014.5002%2010.8728%2014.5025%2010.8636%2014.5071C9.83652%2014.9404%208.91487%2015.5617%208.1239%2016.355C7.33685%2017.1404%206.70933%2018.0707%206.276%2019.0947C5.85031%2020.0972%205.62072%2021.172%205.59967%2022.2609C5.59905%2022.2853%205.60335%2022.3097%205.61229%2022.3325C5.62123%2022.3553%205.63465%2022.376%205.65174%2022.3935C5.66883%2022.4111%205.68926%2022.425%205.71182%2022.4345C5.73437%2022.444%205.7586%2022.4489%205.78308%2022.4489H7.15868C7.25956%2022.4489%207.3398%2022.3686%207.3421%2022.2701C7.38795%2020.5001%208.09868%2018.8425%209.35506%2017.5861C10.655%2016.2862%2012.3814%2015.5709%2014.2201%2015.5709C16.0588%2015.5709%2017.7852%2016.2862%2019.0852%2017.5861C20.3415%2018.8425%2021.0523%2020.5001%2021.0981%2022.2701C21.1004%2022.3709%2021.1807%2022.4489%2021.2815%2022.4489H22.6571C22.6816%2022.4489%2022.7058%2022.444%2022.7284%2022.4345C22.751%2022.425%2022.7714%2022.4111%2022.7885%2022.3935C22.8056%2022.376%2022.819%2022.3553%2022.8279%2022.3325C22.8369%2022.3097%2022.8412%2022.2853%2022.8406%2022.2609C22.8176%2021.165%2022.5907%2020.0989%2022.1642%2019.0924ZM14.2201%2013.8284C13.1678%2013.8284%2012.1773%2013.418%2011.4322%2012.6729C10.6871%2011.9278%2010.2767%2010.9374%2010.2767%209.88504C10.2767%208.83271%2010.6871%207.84227%2011.4322%207.09715C12.1773%206.35204%2013.1678%205.94165%2014.2201%205.94165C15.2724%205.94165%2016.2629%206.35204%2017.008%207.09715C17.7531%207.84227%2018.1635%208.83271%2018.1635%209.88504C18.1635%2010.9374%2017.7531%2011.9278%2017.008%2012.6729C16.2629%2013.418%2015.2724%2013.8284%2014.2201%2013.8284Z'%20fill='%238590A2'/%3e%3c/g%3e%3c/svg%3e)
Co-authors
Following
Followers
Research Focus & Metrics
Explore full metrics on Scilit
Academic Career Length
31Years (1996-Present)
(Calculated once Scilit publication data is synced: current year − year of first publication + 1)
Representative Publications
View All Publications1 January 2008 in Dental Materials
Journal Article
Lorenzo BreschiAMAnnalisa Mazzoni
Annalisa Mazzoni
ARAlessandra Ruggeri
Alessandra Ruggeri
MCMilena Cadenaro
Milena CadenaroRoberto Di LenardaEDElettra De Stefano Dorigo
Elettra De Stefano Dorigo
28 November 2005 in European Journal of Oral Sciences
Journal Article
MCMilena Cadenaro
Milena CadenaroFAFrancesca Antoniolli
Francesca Antoniolli
Salvatore SauroFTFranklin R. Tay
Franklin R. Tay
Roberto Di LenardaLorenzo Breschi +3
1 May 2007 in Journal of Dental Research
Journal Article
AMA. Mazzoni
A. Mazzoni
Ferdinando MannelloFTF.R. Tay
F.R. Tay
GTG.A.M. Tonti
G.A.M. Tonti
SPS. Papa
S. Papa
Lorenzo Breschi +3
The role and function of dentin matrix metalloproteinases (MMPs) are not well-understood, but they may play a key role in dentinal caries and the degradation of resin-bonded dentin matrices. To test the null hypothesis that MMP-9 is not found in dentin matrix, we used gelatin zymography to extract and isolate all molecular forms of gelatinolytic MMPs in demineralized mature sound dentin powder obtained from extracted human molars, characterizing and identifying the enzymes by Western blotting. Gelatinolytic MMPs were detected in extracts of demineralized dentin matrix and identified as MMP-2 and MMP-9. Acidic extracts (pH 2.3) yielded 3–8 times more MMP activity than did EDTA (pH 7.4). Their activation may contribute to dentin matrix degradation, which occurs during caries progression and following resin bonding. Inhibition of MMP-2 and -9 proteolytic activity may slow caries progression and increase the durability of resin-dentin bonds.
21 February 2012 in Journal of Dental Research
Journal Article
Annalisa Mazzoni
Fabio Dupart NascimentoMCM. Carrilho
M. Carrilho
ITIvarne L. S. Tersariol
Ivarne L. S. Tersariol
Veronica PapaLorenzo Breschi +4
Dentinal proteases are believed to play an important role in the degradation of hybrid layers (HL). This study investigated the HL gelatinolytic activity by in situ zymography and functional enzyme activity assay. The hypotheses were that HLs created by an etch-and-rinse adhesive exhibit active gelatinolytic activity, and MMP-2 and -9 activities in dentin increase during adhesive procedures. Etched-dentin specimens were bonded with Adper Scotchbond 1XT and restored with composite. Adhesive/dentin interface slices were placed on microscope slides, covered with fluorescein-conjugated gelatin, and observed with a multi-photon confocal microscope after 24 hrs. Human dentin powder aliquots were prepared and assigned to the following treatments: A, untreated; B, etched with 10% phosphoric acid; or C, etched with 10% phosphoric acid and mixed with Scotchbond 1XT. The MMP-2 and -9 activities of extracts of dentin powder were measured with functional enzyme assays. Intense and continuous enzyme activity was detected at the bottom of the HL, while that activity was more irregular in the upper HL. Both acid-etching and subsequent adhesive application significantly increased MMP-2 and -9 activities (p < 0.05). The results demonstrate, for the first time, intrinsic MMP activity in the HL, and intense activation of matrix-bound MMP activity with both etching and adhesive application.
1 July 2006 in Dentomaxillofacial Radiology
Journal Article
SCS Chiandussi
S ChiandussiMBM Biasotto
M BiasottoFDF Dore
F Dore
FCFabio Cavalli
Fabio CavalliMCMa Cova
Ma Cova
Roberto Di LenardaIt is important to recognize osteonecrosis of the jaws in patients treated with bisphosphonates because an early diagnosis can make a significant difference to the outcome of the disease. The aim of this study is to describe the radiological features of bisphosphonate osteonecrosis (BON) in order to aid its prompt recognition. A conventional radiograph, a computed tomograph (CT), a magnetic resonance image (MRI) and a 99Tc(m)-MDP 3-phase bone scan were carried out for 11 patients with BON. The main imaging findings of osteonecrosis are described. Conventional radiography and CT displayed osteolytic lesions with the involvement of cortical bone. MRI demonstrated the characteristic features of osteonecrosis and the oedema of soft tissues. Both CT and MRI were very useful in defining the extent of the lesions. 99Tc(m)-MDP three-phase bone scan was the most sensitive tool to detect the osteonecrosis at an early stage. 99Tc(m)-MDP three-phase bone scans who could be used as a screening test to detect subclinical osteonecrosis in patients who have received bisphosphonates. CT scans and MRI are useful in defining the features and extent of osteolytic lesions.
5 November 2012 in Journal of Dental Research
Journal Article
AMA. Mazzoni
A. Mazzoni
PSP. Scaffa
P. ScaffaMCM. Carrilho
M. Carrilho
LTL. Tjäderhane
L. TjäderhaneRoberto Di LenardaLorenzo Breschi +4
Auto-degradation of collagen matrices occurs within hybrid layers created by contemporary dentin bonding systems, by the slow action of host-derived matrix metalloproteinases (MMPs). This study tested the null hypothesis that there are no differences in the activities of MMP-2 and -9 after treatment with different etch-and-rinse or self-etch adhesives. Tested adhesives were: Adper Scotchbond 1XT (3M ESPE), PQ1 (Ultradent), Peak LC (Ultradent), Optibond Solo Plus (Kerr), Prime&Bond NT (Dentsply) (all 2-step etch-and-rinse adhesives), and Adper Easy Bond (3M ESPE), Tri-S (Kuraray), and Xeno-V (Dentsply) (1-step self-etch adhesives). MMP-2 and -9 activities were quantified in adhesive-treated dentin powder by means of an activity assay and gelatin zymography. MMP-2 and MMP-9 activities were found after treatment with all of the simplified etch-and-rinse and self-etch adhesives; however, the activation was adhesive-dependent. It is concluded that all two-step etch-and-rinse and the one-step self-etch adhesives tested can activate endogenous MMP-2 and MMP-9 in human dentin. These results support the role of endogenous MMPs in the degradation of hybrid layers created by these adhesives.
About Me
Roberto Di Lenarda is the Rector of the University of Trieste, Italy. He is a Full Professor in Odontostomatological Diseases. He is the Director of the Clinic of Maxillofacial Surgery and Odontostomatology; the Director of the Clinical Assistance Department of ASUGI Specialist Surgeries; the President of the College of University Teachers of Odontostomatological Disciplines; the Director of the Friuli Venezia Giulia Regional Committee of the AIRC 28/9/2016-today; the Former President of the Degree Course in Dental Hygiene and of the Master's Degree Course in Dentistry and Dental Prosthetics and the Former Director of DUC Biomedicine; Deputy Dean of the Faculty of Medicine and Surgery; and Director of the University Department of Medical, Surgical and Health Sciences. He was a Member of the Academic Senate of the University of Trieste from 2012 to 2018; the Secretary and Vice-President of the College of University Professors of Odontostomatological Disciplines (2008-2014) and later President-Elect (2015-2018) of the same. Since January 29, 2020, he has been a Representative of the Conference of Rectors of Italian Universities, serving as a link between the Ministry of Health and the Ministry of Universities at the permanent inter-ministerial table. His research focuses on the study and development of dental materials, pathology and oral medicine, orthodontics, periodontology, implantology, and regenerative oral surgery.