Lack of cathelicidin processing in Papillon-Lefèvre syndrome patients reveals essential role of LL-37 in periodontal homeostasis
Identifieur interne : 001939 ( Main/Curation ); précédent : 001938; suivant : 001940Lack of cathelicidin processing in Papillon-Lefèvre syndrome patients reveals essential role of LL-37 in periodontal homeostasis
Auteurs : Sigrun Eick [Suisse] ; Magdalena Puklo [Pologne] ; Karina Adamowicz [Pologne] ; Tomasz Kantyka [Pologne] ; Pieter Hiemstra [Pays-Bas] ; Henning Stennicke [Danemark] ; Arndt Guentsch [Allemagne] ; Beate Schacher [Allemagne] ; Peter Eickholz [Allemagne] ; Jan Potempa [Pologne, États-Unis]Source :
- Orphanet Journal of Rare Diseases [ 1750-1172 ] ; 2014.
Abstract
Loss-of-function point mutations in the cathepsin C gene are the underlying genetic event in patients with Papillon-Lefèvre syndrome (PLS). PLS neutrophils lack serine protease activity essential for cathelicidin LL-37 generation from hCAP18 precursor.
We hypothesized that a local deficiency of LL-37 in the infected periodontium is mainly responsible for one of the clinical hallmark of PLS: severe periodontitis already in early childhood.
To confirm this effect, we compared the level of neutrophil-derived enzymes and antimicrobial peptides in gingival crevicular fluid (GCF) and saliva from PLS, aggressive and chronic periodontitis patients.
Although neutrophil numbers in GCF were present at the same level in all periodontitis groups, LL-37 was totally absent in GCF from PLS patients despite the large amounts of its precursor, hCAP18. The absence of LL-37 in PLS patients coincided with the deficiency of both cathepsin C and protease 3 activities. The presence of other neutrophilic anti-microbial peptides in GCF from PLS patients, such as alpha-defensins, were comparable to that found in chronic periodontitis. In PLS microbial analysis revealed a high prevalence of
Collectively, these findings imply that the lack of protease 3 activation by dysfunctional cathepsin C in PLS patients leads to the deficit of antimicrobial and immunomodulatory functions of LL-37 in the gingiva, allowing for infection with
The online version of this article (doi:10.1186/s13023-014-0148-y) contains supplementary material, which is available to authorized users.
Url:
DOI: 10.1186/s13023-014-0148-y
PubMed: 25260376
PubMed Central: 4181722
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PMC:4181722Le document en format XML
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<author><name sortKey="Potempa, Jan" sort="Potempa, Jan" uniqKey="Potempa J" first="Jan" last="Potempa">Jan Potempa</name>
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<affiliation wicri:level="2"><nlm:aff id="Aff7">Center of Oral Health and Systemic Diseases, University of Louisville School of Dentistry, Louisville, KY 40202 USA</nlm:aff>
<country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Kentucky</region>
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<front><div type="abstract" xml:lang="en"><sec><title>Background</title>
<p>Loss-of-function point mutations in the cathepsin C gene are the underlying genetic event in patients with Papillon-Lefèvre syndrome (PLS). PLS neutrophils lack serine protease activity essential for cathelicidin LL-37 generation from hCAP18 precursor.</p>
</sec>
<sec><title>Aim</title>
<p>We hypothesized that a local deficiency of LL-37 in the infected periodontium is mainly responsible for one of the clinical hallmark of PLS: severe periodontitis already in early childhood.</p>
</sec>
<sec><title>Methods</title>
<p>To confirm this effect, we compared the level of neutrophil-derived enzymes and antimicrobial peptides in gingival crevicular fluid (GCF) and saliva from PLS, aggressive and chronic periodontitis patients.</p>
</sec>
<sec><title>Results</title>
<p>Although neutrophil numbers in GCF were present at the same level in all periodontitis groups, LL-37 was totally absent in GCF from PLS patients despite the large amounts of its precursor, hCAP18. The absence of LL-37 in PLS patients coincided with the deficiency of both cathepsin C and protease 3 activities. The presence of other neutrophilic anti-microbial peptides in GCF from PLS patients, such as alpha-defensins, were comparable to that found in chronic periodontitis. In PLS microbial analysis revealed a high prevalence of <italic>Aggregatibacter actinomycetemcomitans</italic>
infection. Most strains were susceptible to killing by LL-37.</p>
</sec>
<sec><title>Conclusions</title>
<p>Collectively, these findings imply that the lack of protease 3 activation by dysfunctional cathepsin C in PLS patients leads to the deficit of antimicrobial and immunomodulatory functions of LL-37 in the gingiva, allowing for infection with <italic>A. actinomycetemcomitans</italic>
and the development of severe periodontal disease.</p>
</sec>
<sec><title>Electronic supplementary material</title>
<p>The online version of this article (doi:10.1186/s13023-014-0148-y) contains supplementary material, which is available to authorized users.</p>
</sec>
</div>
</front>
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