4.6 Article

Optimizing dentin bond durability: Control of collagen degradation by matrix metalloproteinases and cysteine cathepsins

Journal

DENTAL MATERIALS
Volume 29, Issue 1, Pages 116-135

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.dental.2012.08.004

Keywords

Matrix metalloproteinase; Cysteine cathepsin; Dentin; Adhesive; Durability; Collagen; Degradation; Chlorhexidine; Composite resin; Tooth

Funding

  1. NIDCR [DE 015306]
  2. Academy of Finland
  3. NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH [R01DE015306] Funding Source: NIH RePORTER

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Objectives. Contemporary adhesives lose their bond strength to dentin regardless of the bonding system used. This loss relates to the hydrolysis of collagen matrix of the hybrid layers. The preservation of the collagen matrix integrity is a key issue in the attempts to improve the dentin bonding durability. Methods. Dentin contains collagenolytic enzymes, matrix metalloproteinases (MMPs) and cysteine cathepsins, which are responsible for the hydrolytic degradation of collagen matrix in the bonded interface. Results. The identities, roles and function of collagenolytic enzymes in mineralized dentin has been gathered only within last 15 years, but they have already been demonstrated to have an important role in dental hard tissue pathologies, including the degradation of the hybrid layer. Identifying responsible enzymes facilitates the development of new, more efficient methods to improve the stability of dentin-adhesive bond and durability of bond strength. Significance. Understanding the nature and role of proteolytic degradation of dentin-adhesive interfaces has improved immensely and has practically grown to a scientific field of its own within only 10 years, holding excellent promise that stable resin-dentin bonds will be routinely available in a daily clinical setting already in a near future. (c) 2012 Academy of Dental Materials. Published by Elsevier Ltd. All rights reserved.

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