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proteinase/karies

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The secretion of aspartyl proteinase, a virulence enzyme, by isolates of Candida albicans from the oral cavity of HIV-infected subjects.

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Prevalence, serotype and in vitro secretion of aspartyl proteinase, a virulence enzyme, were studied in Candida isolates from the oral cavity of 337 HIV-infected subjects. Controls were 95 age-sex-matched HIV- (seronegative) subjects, belonging to either HIV-risk categories (47) or to the normal,

The relationship between the levels of SigA, lactoferrin and alpha(1) proteinase inhibitor in saliva and permanent dentition caries in 15-year-olds.

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A group of 15-year-olds were clinically examined for general state of dentition and level of dental caries. Unstimulated whole saliva from the subjects was laboratory tested to determine the levels of lactoferrin, Secretory IgA (SIgA) and alpha1 proteinase inhibitor. A significant relationship was

Binding of amino acid side chains to preformed cavities: interaction of serine proteinases with turkey ovomucoid third domains with coded and noncoded P1 residues.

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In the association of serine proteinases with their cognate substrates and inhibitors an important interaction is the fitting of the P1 side chain of the substrate or inhibitor into a preformed cavity of the enzyme called the S1 pocket. In turkey ovomucoid third domain, which is a canonical protein

[Proteinase activity in Candida albicans strains isolated from the oral cavity of immunocompromised patients, with oral candidiasis and in healthy subjects].

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BACKGROUND Candida albicans has a variety of virulence factors, including secreted aspartyl proteases, which are determinant factors in the pathogenesis of this yeast in immunocompromised patients. OBJECTIVE Proteinase activity was identified in C. albicans strains isolated from the oral cavity of

Changes in proteinase-activated receptor 2 expression in the human tooth pulp in relation to caries and pain.

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OBJECTIVE To investigate the presence of proteinase-activated receptor 2 (PAR2) in the human tooth pulp and to determine whether there are any changes in receptor expression with caries and pain. METHODS Forty-four mandibular first permanent molars were collected from children (n = 36, mean age 9.96

In vitro secreted aspartyl proteinase activity of Candida albicans isolated from oral diseases and healthy oral cavities.

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The in vitro secreted aspartyl proteinase (SAP) activity of Candida albicans isolated from a variety of oral conditions, including healthy oral cavities, was determined. SAP activity (units/10(6) cells/ml, +/-SD) was 0.28 +/- 0.33 for pseudomembranous candidosis isolates (n = 18), 0.35 +/- 0.46 for

Binding of amino acid side-chains to S1 cavities of serine proteinases.

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The P1 or primary specificity residue of standard mechanism canonical protein inhibitors of serine proteinases, inserts into the S1 primary specificity cavity of the cognate enzyme upon enzyme-inhibitor complex formation. Both natural evolution and protein engineering often change the P1 residue to
Isolates of Candida albicans from the oral cavities of subjects at different stages of human immunodeficiency virus (HIV) infection or uninfected controls were examined for (i) production of aspartic proteinase(s), a putative virulence-associated factor(s); (ii) the presence in the fungal genome of

Role of saliva proteinase 3 in dental caries.

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Salivary analysis can be used to assess the severity of caries. Of the known salivary proteins, a paucity of information exists concerning the role of proteinase 3 (PR3), a serine protease of the chymotrypsin family, in dental caries. Whole, unstimulated saliva was collected from children with

Mast cell tryptase induces eosinophil recruitment in the pleural cavity of mice via proteinase-activated receptor 2.

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Proteinase-activated receptor (PAR) 2 has been implicated in eosinophil migration. Mast cell (MC) tryptase has been similarly implicated in allergic diseases through the activation of PAR-2, but the role of this receptor in MC tryptase-induced inflammation is not well elucidated. This study aims to

Role of Candida albicans-secreted aspartyl proteinases (Saps) in severe early childhood caries.

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Candida albicans is strongly associated with severe early childhood caries (S-ECC). However, the roles of secreted aspartyl proteinases (Saps), an important virulence factor of C. albicans, in the progress of S-ECC are not clear. In our study, the Saps activities were evaluated by the yeast nitrogen

[Evalution of activity of acid aspartic proteinase in Candida strains isolated from oral cavity of patients with increased risk of mycosis].

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We have evaluated the activity of acid aspartic protease in 195 strains of Candida isolated from the oral cavity of three groups of patients. The first group comprised patients with cancer of the larynx qualified for surgery, the second- patients with neoplastic disease ( Hodgkin s disease,

Differential expression of secreted aspartyl proteinases in a model of human oral candidosis and in patient samples from the oral cavity.

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Candida albicans, an opportunistic pathogen in humans, secretes secretory aspartyl proteinases (Saps), which have been correlated with virulence. We examined the temporal regulation of the mRNA expression of seven known members of the SAP gene family by reverse transcription polymerase chain

Blockade of proteinase-activated receptor-4 inhibits the eosinophil recruitment induced by eotaxin-1 in the pleural cavity of mice.

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OBJECTIVE Although proteinase-activated receptor (PAR)-4 has been implicated in inflammation, its role in regulating eosinophil recruitment in response to chemoattractants has not yet been demonstrated. To investigate the contribution of proteinases and PAR-4 activation to eosinophil migration in

The catalytic site of serine proteinases as a specific binding cavity for xenon.

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BACKGROUND Under moderate pressure, xenon can bind to proteins and form weak but specific interactions. Such protein-xenon complexes can be used as isomorphous derivatives for phase determination in X-ray crystallography. RESULTS Investigation of the serine proteinase class of enzymes shows that the
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