Document Detail

Effect of phosphoric acid on the degradation of human dentin matrix.
MedLine Citation:
PMID:  23103634     Owner:  NLM     Status:  MEDLINE    
This study determined if dentin proteases are denatured by phosphoric acid (PA) used in etch-and-rinse dentin adhesives. Dentin beams were completely demineralized with EDTA for 30 days. We "acid-etched" experimental groups by exposing the demineralized dentin beams to 1, 10, or 37 mass% PA for 15 sec or 15 min. Control beams were not exposed to PA but were incubated in simulated body fluid for 3 days to assay their total endogenous telopeptidase activity, by their ability to solubilize C-terminal crosslinked telopeptides ICTP and CTX from insoluble dentin collagen. Control beams released 6.1 ± 0.8 ng ICTP and 0.6 ± 0.1 ng CTX/mg dry-wt/3 days. Positive control beams pre-incubated in p-aminophenylmercuric acetate, a compound known to activate proMMPs, released about the same amount of ICTP peptides, but released significantly less CTX. Beams immersed in 1, 10, or 37 mass% PA for 15 sec or 15 min released amounts of ICTP and CTX similar to that released by the controls (p > 0.05). Beams incubated in galardin, an MMP inhibitor, or E-64, a cathepsin inhibitor, blocked most of the release of ICTP and CTX, respectively. It is concluded that PA does not denature endogenous MMP and cathepsin activities of dentin matrices.
A Tezvergil-Mutluay; M Mutluay; R Seseogullari-Dirihan; K A Agee; W O Key; D L S Scheffel; L Breschi; A Mazzoni; L Tjäderhane; Y Nishitani; F R Tay; D H Pashley
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2012-10-26
Journal Detail:
Title:  Journal of dental research     Volume:  92     ISSN:  1544-0591     ISO Abbreviation:  J. Dent. Res.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2012-12-11     Completed Date:  2013-02-11     Revised Date:  2014-01-09    
Medline Journal Info:
Nlm Unique ID:  0354343     Medline TA:  J Dent Res     Country:  United States    
Other Details:
Languages:  eng     Pagination:  87-91     Citation Subset:  D; IM    
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MeSH Terms
Cathepsins / antagonists & inhibitors
Collagen Type I / analysis
Collagenases / drug effects
Cysteine Proteinase Inhibitors / pharmacology
Dentin / drug effects*,  enzymology
Dipeptides / pharmacology
Enzyme Activators / pharmacology
Enzyme Precursors / drug effects
Leucine / analogs & derivatives,  pharmacology
Materials Testing
Matrix Metalloproteinase Inhibitors / pharmacology
Matrix Metalloproteinases / drug effects
Peptide Hydrolases / drug effects
Peptides / analysis
Phenylmercuric Acetate / analogs & derivatives,  pharmacology
Phosphoric Acids / pharmacology*
Protein Denaturation
Sulfhydryl Reagents / pharmacology
Time Factors
Grant Support
Reg. No./Substance:
0/Collagen Type I; 0/Cysteine Proteinase Inhibitors; 0/Dipeptides; 0/Enzyme Activators; 0/Enzyme Precursors; 0/Matrix Metalloproteinase Inhibitors; 0/N-(2(R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl)-L-tryptophan methylamide; 0/Peptides; 0/Phosphoric Acids; 0/Sulfhydryl Reagents; 0/collagen type I trimeric cross-linked peptide; 6283-24-5/4-aminophenylmercuriacetate; 66701-25-5/E 64; E4GA8884NN/phosphoric acid; EC 3.4.-/Cathepsins; EC 3.4.-/Peptide Hydrolases; EC 3.4.24.-/Collagenases; EC 3.4.24.-/Matrix Metalloproteinases; GMW67QNF9C/Leucine; OSX88361UX/Phenylmercuric Acetate

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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