TY - JOUR
T1 - Co-distribution of cysteine cathepsins and matrix metalloproteases in human dentin
AU - Scaffa, Polliana Mendes Candia
AU - Breschi, Lorenzo
AU - Mazzoni, Annalisa
AU - Vidal, Cristina de Mattos Pimenta
AU - Curci, Rosa
AU - Apolonio, Fabianni
AU - Gobbi, Pietro
AU - Pashley, David
AU - Tjäderhane, Leo
AU - Tersariol, Ivarne Luis dos Santos
AU - Nascimento, Fábio Dupart
AU - Carrilho, Marcela Rocha
N1 - Funding Information:
The authors thank the funding agencies FAPESP (2016/07996-2 – P.I: M.R. Carrilho) and CNPq (312768/2013-3 – P.I: M.R. Carrilho), Brazil.
Publisher Copyright:
© 2016 Elsevier Ltd
PY - 2017/2/1
Y1 - 2017/2/1
N2 - It has been hypothesized that cysteine cathepsins (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.
AB - It has been hypothesized that cysteine cathepsins (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.
KW - Cysteine cathepsins
KW - Dentin
KW - Immunohistochemistry
KW - Matrix metalloproteases
KW - Proteolytic activity
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U2 - 10.1016/j.archoralbio.2016.11.011
DO - 10.1016/j.archoralbio.2016.11.011
M3 - Article
C2 - 27923176
AN - SCOPUS:85006974131
SN - 0003-9969
VL - 74
SP - 101
EP - 107
JO - Archives of Oral Biology
JF - Archives of Oral Biology
ER -