Co-distribution of cysteine cathepsins and matrix metalloproteases in human dentin

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Candia Scaffa, Polliana Mendes ; Breschi, Lorenzo ; Mazzoni, Annalisa ; Pimenta Vidal, Cristina de Mattos ; Curci, Rosa ; Apolonio, Fabianni ; Gobbi, Pietro ; Pashley, David ; Tjaderhane, Leo ; dos Santos Tersariol, Ivarne Luis ; Nascimento, Fabio Dupart ; Carrilhon, Marcela Rocha

• Document type: Journal article
• Source: ARCHIVES OF ORAL BIOLOGY; v. 74, p. 101-107, FEB 2017.
• Web of Science Citations: 11

Abstract

It has been hypothesized that cysteine cathepsin's (CTs) along with matrix metalloproteases (MMPs) may work in conjunction in the proteolysis of mature dentin matrix. The aim of this study was to verify simultaneously the distribution and presence of cathepsins B (CT-B) and K (CT-K) in partially demineralized dentin; and further to evaluate the activity of CTs and MMPs in the same tissue. The distribution of CT-B and CT-K in sound human dentin was assessed by immunohistochemistry. A double-immunolabeling technique was used to identify, at once, the occurrence of those enzymes in dentin. Activities of CTs and MMPs in dentin extracts were evaluated spectrofluorometrically. In addition, in situ gelatinolytic activity of dentin was assayed by zymography. The results revealed the distribution of CT-B and CT-K along the dentin organic matrix and also indicated co-occurrence of MMPs and CTs in that tissue. The enzyme kinetics studies showed proteolytic activity in dentin extracts for both classes of proteases. Furthermore, it was observed that, at least for sound human dentin matrices, the activity of MMPs seems to be predominant over the CTs one. (C) 2016 Elsevier Ltd. All rights reserved. (AU)

• FAPESP's process: 09/14005-9 - Effect of protease inhibitors on the solubilization of demineralized dentin, preservation of mechanical properties of dentin matrix and durability of adhesive restorations.
• Grantee: Polliana Mendes Candia Scaffa
• Support Opportunities: Scholarships in Brazil - Doctorate