aggressive periodontitis/protease

The purpose of this work was to study the elastase content of PMNs, the elastase alpha1-protease inhibitor complex, and the protease inhibitors in the plasma of patients with periodontal disease as compared with healthy subjects. We examined 11 patients with localized juvenile periodontitis (LJP),

The profile of salivary proteases and their cellular origin, with special reference to polymorphonuclear leukocytes and bacteria, was studied in localized juvenile periodontitis and compared with adult periodontitis and healthy controls. General proteolytic activity in saliva as well as collagenase,

In periodontitis, an effective host-response is primarily related to neutrophils loaded with serine proteases, including elastase (NE) and protease 3 (PR3), the extracellular activity of which is tightly controlled by endogenous inhibitors. In vitro these inhibitors are degraded by gingipains,

BACKGROUND Trappin-2 is one of the potent biologically active serine protease inhibitor with anti-inflammatory properties that has also been characterized as an "alarm anti-protease". Despite the importance of Trappin-2 in several chronic infections has been demonstrated, its potential involvement

alpha-1-Antitrypsin phenotypes and serum levels were determined in 19 patients with juvenile periodontitis in order to test whether reduced periodontal resistance in this disease is caused by decreased serum protease inhibitory capacity resulting from deficient alpha-1-antitrypsin phenotypes. The

Patients with juvenile periodontitis frequently have elevated levels of serum immunoglobulin A (IgA) antibodies to antigens of Actinobacillus actinomycetemcomitans. IgA occurs in two subclasses, IgA1 and IgA2, and in monomeric and polymeric forms. Because IgA1 is susceptible to cleavage by IgA1

Proteolytic tissue degradation is a typical phenomenon in inflammatory periodontal diseases. HtrA1 (High temperature requirement A 1) has a serine protease activity and is able to degrade fibronectin whose fragments induce the expression and secretion of several matrix metalloproteinases (MMPs). The

Cathepsin C (CatC) is a cysteine protease involved in a variety of immune and inflammatory pathways such as activation of cytotoxicity of various immune cells. Homozygous or compound heterozygous variants in the CatC coding gene CTSC cause different conditions that have in common severe

Salivary, serum matrix metalloproteinase-8 (MMP-8), tissue inhibitor of matrix metalloproteinases-1 (TIMP-1), neutrophil elastase (NE), and myeloperoxidase (MPO) levels were investigated in generalized chronic periodontitis (GCP), generalized aggressive periodontitis (GAgP), and healthy groups.

OBJECTIVE Matrix metalloproteinase (MMP)-8 is a protease that degrades numerous extracellular molecules and has been implicated in the pathogenesis of periodontitis. Polymorphism in the MMP-8 could affect the susceptibility to disease. Our aim was to evaluate the association between periodontitis

Previous reports have indicated the association of periodontal diseases with elevated levels of serum immunoglobulin G (IgG) antibodies to periodontally relevant bacteria. Recent results from this laboratory suggest that enzymes proteolytic for immunoglobulins are important virulence factors of

Porphyromonas gingivalis has been implicated as a contributing etiological agent of adult periodontitis and generalized forms of early-onset periodontitis. Proteases of P. gingivalis may contribute to its pathogenicity by destroying connective tissue as well as inactivating key plasma proteins that

Immunoglobulin A1 (IgA1) proteases secreted by oral Prevotella and Capnocytophaga species specifically cleave IgA1 at the same peptide bond in the hinge region, leaving intact monomeric Fab and Fc fragments. Assuming that Prevotella- and Capnocytophaga-induced Fab fragments of IgA1 expose a specific