LL-37 in periodontal health and disease and its susceptibility to degradation by proteinases present in gingival crevicular fluid

Maeliosa T.C. McCrudden, David F. Orr, Yang Yu, Wilson A. Coulter, Gwen Manning, Chris R. Irwin, Fionnuala T. Lundy

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Aim

To determine the levels of LL-37 in and its susceptibility to degradation by components of gingival crevicular fluid (GCF) in periodontal health and disease.

Materials and Methods

Levels of LL-37 in GCF from periodontitis patients and periodontally healthy subjects were determined by ELISA. In addition, degradation of synthetic/exogenous LL-37 by components of GCF in the presence and absence of inhibitors was determined by matrix-assisted laser desorption/ionization time of flight mass spectrometry.

Results

The concentration of native LL-37 in GCF from Porphyromonas gingivalis positive (Pg+) and P. gingivalis negative (Pg-) sites in periodontitis patients was significantly higher than in GCF from healthy subjects. When synthetic LL-37 was added to healthy GCF, the peptide was not degraded. Conversely, GCF from Pg+ sites rapidly degraded synthetic LL-37 which was prevented in the presence of Arg− and Lys− gingipain inhibitors. Synthetic LL-37 was degraded more slowly by GCF from Pg− sites.

Conclusions

LL-37 is detectable in GCF in periodontal health and disease. The rapid degradation of synthetic LL-37 in periodontitis GCF, particularly in Pg+ sites, limits its role as a potential therapeutic in the gingival crevice. These results highlight the need to design stable peptide mimetics of LL-37 as future therapeutics in periodontitis.
Original languageEnglish
Pages (from-to)933-941
JournalJournal of Clinical Periodontology
Volume40
Issue number10
Early online date18 Aug 2013
DOIs
Publication statusPublished - Oct 2013

Keywords

  • antimicrobial peptide
  • cathelicidin
  • mass spectrometry
  • periodontitis
  • protease

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