A comparison of cysteine and serine proteinases in human gingival crevicular fluid with tissue, saliva and bacterial enzymes by analytical isoelectric focusing

Gazi, M. I.; Cox, Susanne; Clark, Douglas; Eley, B M

doi:10.1016/0003-9969(96)00007-6

Cited by 13 publications

(21 citation statements)

References 22 publications

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“…Due to the fact that neutrophils are the main source of HNP1–3, 4 it was very interesting to find similar GCF HNP1–3 levels in all study groups. It was reported that defensins are substrates for some proteinases, which are derived from tissue and bacteria such as P. gingivalis 21 , 42 , 43 . It was demonstrated that P. gingivalis is a highly proteolytic organism that degraded a variety of antimicrobial peptides 21 .…”

Section: Discussionmentioning

confidence: 99%

Evaluation of Gingival Crevicular Fluid Adrenomedullin and Human Neutrophil Peptide 1–3 Levels of Patients With Different Periodontal Diseases

Türkoğlu

Emingil

Kütükçüler

et al. 2010

Journal of Periodontology

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Section: Discussionmentioning

confidence: 99%

Evaluation of Gingival Crevicular Fluid Adrenomedullin and Human Neutrophil Peptide 1–3 Levels of Patients With Different Periodontal Diseases

Türkoğlu

Emingil

Kütükçüler

et al. 2010

Journal of Periodontology

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“…Differences may be due to the different analytical methodologies used: mass spectroscopy analysis -technique used by Lundy et al (60) suggest that most a-defensins may be partially degraded in the periodontal pockets and may not account for their full activity. Accordingly, GCF has been shown to contain several tissue-derived and microorganism-derived proteases (61).…”

Section: Defensins Expression In Oral Tissuesmentioning

confidence: 99%

Defensins in the oral cavity: distribution and biological role

Gomes

Fernandes

2010

Journal of Oral Pathology &Amp; Medicine

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The oral cavity outreaches as a particular environment in which there is a continuous interplay between bacteria, fungi and viruses, and the epithelial barrier. Among the innate mechanisms that aim to establish a regulated equilibrium between health and disease, natural antimicrobial peptides, especially those part of the defensins' family, have emerged as fundamental mediators. Their biological role is emphasized by the large number of expressed genes, as well as the multiplicity of the individual molecules present on biological tissues and fluids, in physiological and pathological conditions. Furthermore, the direct antimicrobial action, defensins may play a pivotal role in the orchestration of the innate response and contribute to the interplay between the innate and adaptive immunity. This review focuses on the specificities of defensins' structure, expression and biological role in the oral environment, enlightening their relevance in physiological and pathological conditions.

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“…Bacterial cysteine proteinase activity has been demonstrated within diseased periodontal pockets (13,20), and epitopes of gingipains are detectable in clinical plaque samples from patients with adult periodontitis (unpublished data), so the gingipains are likely to be clinically relevant. The gingipains are expressed on the outer membrane of P. gingivalis and may also be released with vesicles or as soluble proteins (9,18,24).…”

mentioning

confidence: 98%

Porphyrin-Mediated Binding to Hemoglobin by the HA2 Domain of Cysteine Proteinases (Gingipains) and Hemagglutinins from the Periodontal PathogenPorphyromonas gingivalis

et al. 1999

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Heme binding and uptake are considered fundamental to the growth and virulence of the gram-negative periodontal pathogenPorphyromonas gingivalis. We therefore examined the potential role of the dominant P. gingivalis cysteine proteinases (gingipains) in the acquisition of heme from the environment. A recombinant hemoglobin-binding domain that is conserved between two predominant gingipains (domain HA2) demonstrated tight binding to hemin (Kd = 16 nM), and binding was inhibited by iron-free protoporphyrin IX (Ki = 2.5 μM). Hemoglobin binding to the gingipains and the recombinant HA2 (rHA2) domain (Kd = 2.1 nM) was also inhibited by protoporphyrin IX (Ki = 10 μM), demonstrating an essential interaction between the HA2 domain and the heme moiety in hemoglobin binding. Binding of rHA2 with either hemin, protoporphyrin IX, or hematoporphyrin was abolished by establishing covalent linkage of the protoporphyrin propionic acid side chains to fixed amines, demonstrating specific and directed binding of rHA2 to these protoporphyrins. A monoclonal antibody which recognizes a peptide epitope within the HA2 domain was employed to demonstrate that HA2-associated hemoglobin-binding activity was expressed and released by P. gingivalis cells in a batch culture, in parallel with proteinase activity. Cysteine proteinases from P. gingivalis appear to be multidomain proteins with functions for hemagglutination, erythrocyte lysis, proteolysis, and heme binding, as demonstrated here. Detailed understanding of the biochemical pathways for heme acquisition in P. gingivalis may allow precise targeting of this critical metabolic aspect for periodontal disease prevention.

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A comparison of cysteine and serine proteinases in human gingival crevicular fluid with tissue, saliva and bacterial enzymes by analytical isoelectric focusing

Cited by 13 publications

References 22 publications

Evaluation of Gingival Crevicular Fluid Adrenomedullin and Human Neutrophil Peptide 1–3 Levels of Patients With Different Periodontal Diseases

Evaluation of Gingival Crevicular Fluid Adrenomedullin and Human Neutrophil Peptide 1–3 Levels of Patients With Different Periodontal Diseases

Defensins in the oral cavity: distribution and biological role

Porphyrin-Mediated Binding to Hemoglobin by the HA2 Domain of Cysteine Proteinases (Gingipains) and Hemagglutinins from the Periodontal PathogenPorphyromonas gingivalis

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