Can quaternary ammonium methacrylates inhibit matrix MMPs and cathepsins?

Arzu Tezvergil-Mutluay, Kelli A. Agee, Annalisa Mazzoni, Ricardo M. Carvalho, Marcela Carrilho, Ivarne L. Tersariol, Fabio D. Nascimento, Satoshi Imazato, Leo Tjäderhane, Lorenzo Breschi, Franklin Chi Meng Tay, David Henry Pashley

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

Objective Dentin matrices release ICTP and CTX fragments during collagen degradation. ICTP fragments are known to be produced by MMPs. CTX fragments are thought to come from cathepsin K activity. The purpose of this study was to determine if quaternary methacrylates (QAMs) can inhibit matrix MMPs and cathepsins. Methods Dentin beams were demineralizated, and dried to constant weight. Beams were incubated with rh-cathepsin B, K, L or S for 24 h at pH 7.4 to identify which cathepsins release CTX at neutral pH. Beams were dipped in ATA, an antimicrobial QAM to determine if it can inhibit dentin matrix proteases. Other beams were dipped in another QAM (MDPB) to determine if it produced similar inhibition of dentin proteases. Results Only beams incubated with cathepsin K lost more dry mass than the controls and released CTX. Dentin beams dipped in ATA and incubated for 1 week at pH 7.4, showed a concentration-dependent reduction in weight-loss. There was no change in ICTP release from control values, meaning that ATA did not inhibit MMPs. Media concentrations of CTX fell significantly at 15 wt% ATA indicating that ATA inhibits capthesins. Beams dipped in increasing concentrations of MDPB lost progressively less mass, showing that MDPB is a protease-inhibitor. ICTP released from controls or beams exposed to low concentrations were the same, while 5 or 10% MDPB significantly lowered ICTP production. CTX levels were strongly inhibited by 2.5-10% MDPB, indicating that MDPB is a potent inhibitor of both MMPs and cathepsin K. Significance CTX seems to be released from dentin matrix only by cathepsin K. MMPs and cathepsin K and B may all contribute to matrix degradation.

Original languageEnglish (US)
Pages (from-to)e25-e32
JournalDental Materials
Volume31
Issue number2
DOIs
StatePublished - Feb 1 2015

Fingerprint

Cathepsin K
Cathepsins
Methacrylates
Dentin
Matrix Metalloproteinases
Ammonium Compounds
Cathepsin B
Peptide Hydrolases
Degradation
Matrix Metalloproteinase Inhibitors
Protease Inhibitors
Collagen
Weight Loss
Weights and Measures

Keywords

  • CTX
  • Cathepsins
  • Degradation of collagen
  • ICTP
  • MMPs
  • Quaternary ammonium compounds

ASJC Scopus subject areas

  • Materials Science(all)
  • Dentistry(all)
  • Mechanics of Materials

Cite this

Tezvergil-Mutluay, A., Agee, K. A., Mazzoni, A., Carvalho, R. M., Carrilho, M., Tersariol, I. L., ... Pashley, D. H. (2015). Can quaternary ammonium methacrylates inhibit matrix MMPs and cathepsins? Dental Materials, 31(2), e25-e32. https://doi.org/10.1016/j.dental.2014.10.006

Can quaternary ammonium methacrylates inhibit matrix MMPs and cathepsins? / Tezvergil-Mutluay, Arzu; Agee, Kelli A.; Mazzoni, Annalisa; Carvalho, Ricardo M.; Carrilho, Marcela; Tersariol, Ivarne L.; Nascimento, Fabio D.; Imazato, Satoshi; Tjäderhane, Leo; Breschi, Lorenzo; Tay, Franklin Chi Meng; Pashley, David Henry.

In: Dental Materials, Vol. 31, No. 2, 01.02.2015, p. e25-e32.

Research output: Contribution to journalArticle

Tezvergil-Mutluay, A, Agee, KA, Mazzoni, A, Carvalho, RM, Carrilho, M, Tersariol, IL, Nascimento, FD, Imazato, S, Tjäderhane, L, Breschi, L, Tay, FCM & Pashley, DH 2015, 'Can quaternary ammonium methacrylates inhibit matrix MMPs and cathepsins?', Dental Materials, vol. 31, no. 2, pp. e25-e32. https://doi.org/10.1016/j.dental.2014.10.006
Tezvergil-Mutluay A, Agee KA, Mazzoni A, Carvalho RM, Carrilho M, Tersariol IL et al. Can quaternary ammonium methacrylates inhibit matrix MMPs and cathepsins? Dental Materials. 2015 Feb 1;31(2):e25-e32. https://doi.org/10.1016/j.dental.2014.10.006
Tezvergil-Mutluay, Arzu ; Agee, Kelli A. ; Mazzoni, Annalisa ; Carvalho, Ricardo M. ; Carrilho, Marcela ; Tersariol, Ivarne L. ; Nascimento, Fabio D. ; Imazato, Satoshi ; Tjäderhane, Leo ; Breschi, Lorenzo ; Tay, Franklin Chi Meng ; Pashley, David Henry. / Can quaternary ammonium methacrylates inhibit matrix MMPs and cathepsins?. In: Dental Materials. 2015 ; Vol. 31, No. 2. pp. e25-e32.
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abstract = "Objective Dentin matrices release ICTP and CTX fragments during collagen degradation. ICTP fragments are known to be produced by MMPs. CTX fragments are thought to come from cathepsin K activity. The purpose of this study was to determine if quaternary methacrylates (QAMs) can inhibit matrix MMPs and cathepsins. Methods Dentin beams were demineralizated, and dried to constant weight. Beams were incubated with rh-cathepsin B, K, L or S for 24 h at pH 7.4 to identify which cathepsins release CTX at neutral pH. Beams were dipped in ATA, an antimicrobial QAM to determine if it can inhibit dentin matrix proteases. Other beams were dipped in another QAM (MDPB) to determine if it produced similar inhibition of dentin proteases. Results Only beams incubated with cathepsin K lost more dry mass than the controls and released CTX. Dentin beams dipped in ATA and incubated for 1 week at pH 7.4, showed a concentration-dependent reduction in weight-loss. There was no change in ICTP release from control values, meaning that ATA did not inhibit MMPs. Media concentrations of CTX fell significantly at 15 wt{\%} ATA indicating that ATA inhibits capthesins. Beams dipped in increasing concentrations of MDPB lost progressively less mass, showing that MDPB is a protease-inhibitor. ICTP released from controls or beams exposed to low concentrations were the same, while 5 or 10{\%} MDPB significantly lowered ICTP production. CTX levels were strongly inhibited by 2.5-10{\%} MDPB, indicating that MDPB is a potent inhibitor of both MMPs and cathepsin K. Significance CTX seems to be released from dentin matrix only by cathepsin K. MMPs and cathepsin K and B may all contribute to matrix degradation.",
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AU - Carvalho, Ricardo M.

AU - Carrilho, Marcela

AU - Tersariol, Ivarne L.

AU - Nascimento, Fabio D.

AU - Imazato, Satoshi

AU - Tjäderhane, Leo

AU - Breschi, Lorenzo

AU - Tay, Franklin Chi Meng

AU - Pashley, David Henry

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N2 - Objective Dentin matrices release ICTP and CTX fragments during collagen degradation. ICTP fragments are known to be produced by MMPs. CTX fragments are thought to come from cathepsin K activity. The purpose of this study was to determine if quaternary methacrylates (QAMs) can inhibit matrix MMPs and cathepsins. Methods Dentin beams were demineralizated, and dried to constant weight. Beams were incubated with rh-cathepsin B, K, L or S for 24 h at pH 7.4 to identify which cathepsins release CTX at neutral pH. Beams were dipped in ATA, an antimicrobial QAM to determine if it can inhibit dentin matrix proteases. Other beams were dipped in another QAM (MDPB) to determine if it produced similar inhibition of dentin proteases. Results Only beams incubated with cathepsin K lost more dry mass than the controls and released CTX. Dentin beams dipped in ATA and incubated for 1 week at pH 7.4, showed a concentration-dependent reduction in weight-loss. There was no change in ICTP release from control values, meaning that ATA did not inhibit MMPs. Media concentrations of CTX fell significantly at 15 wt% ATA indicating that ATA inhibits capthesins. Beams dipped in increasing concentrations of MDPB lost progressively less mass, showing that MDPB is a protease-inhibitor. ICTP released from controls or beams exposed to low concentrations were the same, while 5 or 10% MDPB significantly lowered ICTP production. CTX levels were strongly inhibited by 2.5-10% MDPB, indicating that MDPB is a potent inhibitor of both MMPs and cathepsin K. Significance CTX seems to be released from dentin matrix only by cathepsin K. MMPs and cathepsin K and B may all contribute to matrix degradation.

AB - Objective Dentin matrices release ICTP and CTX fragments during collagen degradation. ICTP fragments are known to be produced by MMPs. CTX fragments are thought to come from cathepsin K activity. The purpose of this study was to determine if quaternary methacrylates (QAMs) can inhibit matrix MMPs and cathepsins. Methods Dentin beams were demineralizated, and dried to constant weight. Beams were incubated with rh-cathepsin B, K, L or S for 24 h at pH 7.4 to identify which cathepsins release CTX at neutral pH. Beams were dipped in ATA, an antimicrobial QAM to determine if it can inhibit dentin matrix proteases. Other beams were dipped in another QAM (MDPB) to determine if it produced similar inhibition of dentin proteases. Results Only beams incubated with cathepsin K lost more dry mass than the controls and released CTX. Dentin beams dipped in ATA and incubated for 1 week at pH 7.4, showed a concentration-dependent reduction in weight-loss. There was no change in ICTP release from control values, meaning that ATA did not inhibit MMPs. Media concentrations of CTX fell significantly at 15 wt% ATA indicating that ATA inhibits capthesins. Beams dipped in increasing concentrations of MDPB lost progressively less mass, showing that MDPB is a protease-inhibitor. ICTP released from controls or beams exposed to low concentrations were the same, while 5 or 10% MDPB significantly lowered ICTP production. CTX levels were strongly inhibited by 2.5-10% MDPB, indicating that MDPB is a potent inhibitor of both MMPs and cathepsin K. Significance CTX seems to be released from dentin matrix only by cathepsin K. MMPs and cathepsin K and B may all contribute to matrix degradation.

KW - CTX

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KW - MMPs

KW - Quaternary ammonium compounds

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