Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.17 (lysozyme)
21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Little information is available about the acquired pellicle layer that is formed on denture surfaces or its role in regulating microbial colonization of the prosthetic surface. Because denture-induced stomatitis is associated with increased numbers of Candida albicans and other microorganisms on the denture surface, the acquired denture pellicle (ADP) may play a role in modulating this colonization. This study examined and compared ADP from healthy patients and patients with stomatitis by chemical and immunochemical methods. The ADP was found to be composed of a selectively adsorbed layer containing salivary amylase, high molecular weight mucin (MG1), lysozyme, albumin, and sIgA. Salivary cystatins, proline-rich proteins, and low molecular weight mucin (MG2) were not detected. ADP amino acid composition was distinct from any of the ductal salivas, but had many similarities with enamel pellicle. Immunoblots of ADP from patients with stomatitis identified additional serum components, degradation products, and C. albicans cell components that were not detected in ADP from healthy patients. Quantification of these molecules in ADP could lead to a diagnostic test for oral mucosal disease underlying a denture base. Identification of specific molecules in denture pellicle that promote adhesion of C. albicans may elucidate a mechanism of fungal cell colonization on the denture surface. Future studies that chemically modify the denture acrylic resin surface to immobilize antimicrobial proteins may be a means of decreasing pathogenic plaque development.
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PMID:Characterization of acquired denture pellicle from healthy and stomatitis patients. 140 50

Wild type dihydrolipoyltransacetylase(E2p)-components from the pyruvate dehydrogenase complex of A. vinelandii or E. coli, and mutants of A. vinelandii E2p with stepwise deletions of the lipoyl domains or the alanine- and proline-rich region between the binding and the catalytic domain have been overexpressed in E. coli TG2. The high expression of A. vinelandii wild type E2p (20% of cellular protein) and of a mutant enzyme with two lipoyl domains changed the properties of the inner bacterial membrane. This resulted in a solubilization of A. vinelandii E2p after degradation of the outer membrane by lysozyme without any contamination by E. coli pyruvate dehydrogenase complex (PDC) or other high-molecular-weight contaminants. The same effect could be detected for A. vinelandii E2o, an E2 which contains only one lipoyl domain, whereas almost no solubilization of A. vinelandii E2p with one lipoyl domain or of E2p consisting only of the binding and catalytic domain was found. Partial or complete deletion of the alanine- and proline-rich sequence between the binding and the catalytic domain did also decrease the solubilization of the E2p-mutants after lysozyme treatment. Immunocytochemical experiments on E. coli TG2 cells expressing A. vinelandii wild type E2p indicated that the enzyme was present as a soluble protein in the cytoplasm. In contrast, overexpressed A. vinelandii E2p with deletion of all three lipoyl domains and E. coli wild type E2p aggregated intracellularly. The solubilization by lysozyme is therefore ascribed to excluded volume effects leading to changes in the properties of the inner bacterial membrane.
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PMID:Purification and cellular localization of wild type and mutated dihydrolipoyltransacetylases from Azotobacter vinelandii and Escherichia coli expressed in E. coli. 155 45

We cloned and sequenced the gene encoding the muramidase-released protein (MRP) of a pathogenic Streptococcus suis type 2 strain to determine whether its amino acid sequence resembles that of proteins with known functions and to determine its function in virulence. The complete nucleotide sequence composing the gene and the regions flanking it was determined. The deduced amino acid sequence revealed the presence of a signal peptide at the N terminus and a cell envelope anchor at the C terminus, both of which resembled similar regions in several other surface proteins from gram-positive bacteria. The processed form of MRP has a length of 1,209 amino acids and a calculated molecular weight of 131,094. A highly repetitive region preceded the envelope anchor. The repeated units were preceded by a proline-rich stretch of amino acids (26 of 86). No overall homologies were observed between the amino acid sequence of MRP and protein sequences in the EMBL data bank. A particular region within the amino acid sequence, however, showed some similarity with the fibronectin-binding protein of Staphylococcus aureus. Binding of MRP to human fibronectin, however, could not be confirmed.
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PMID:Cloning and nucleotide sequence of the gene encoding the 136-kilodalton surface protein (muramidase-released protein) of Streptococcus suis type 2. 158 2

The secretion of three antimicrobial proteins from the parotid glands of 82 generally healthy men and women, 22 to 81 years in age, was examined. No change was observed in the levels of secretory IgA, but statistically significant, modest elevations (approximately 50 to 100%) of lactoferrin, in both unstimulated and stimulated secretions, and lysozyme, in unstimulated secretions, were detected when results were expressed as mg antimicrobial protein/100 ml saliva. However, these alterations were not observed if data were expressed as mg antimicrobial protein/g total protein. Also, no change was detected in an acinar cell exocrine product, the anionic proline-rich proteins, as reported previously by our laboratory. The data are consistent with a maintenance of protective functions in parotid saliva during aging.
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PMID:Secretion of antimicrobial proteins from the parotid glands of different aged healthy persons. 362 4

The contribution of proteins from saliva and gingival crevicular fluid (GCF) to plaque was determined by comparing extracts of supragingival plaque of unknown age formed on normal teeth with plaque formed on artificial teeth in complete or partial dentures where crevicular fluid is absent. There was a total absence of albumin and a virtual absence of IgG from denture plaque samples, confirming their crevicular origin. The concentration of lactoferrin was much higher than that of lysozyme in all supragingival but not in the denture plaque samples, suggesting that GCF provided more lactoferrin than lysozyme to plaque. Amylase was a component in both denture and supragingival plaque, present in similar amounts in both deposits. Cysteine-containing phosphoproteins from saliva were in low concentration but present in all plaque samples; proline-rich proteins were virtually absent, reflecting the high vulnerability to proteolysis of these proteins. Salivary proteins in plaque extracts do not correspond with their relative concentrations in saliva.
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PMID:Immunochemical study of host proteins in human supragingival compared with denture plaque. 620 85

We present here the isolation and characterization of four antimicrobial peptides produced by a European bumblebee Bombus pascuorum. A 51-residue insect defensin was characterized which, like the Apis mellifera defensins, had a highly conserved 12-residue extension to its C-terminal compared to defensins from other insects. Monoisotopic mass analysis of the C-terminal of B. pascuorum defensin confirmed that this molecule was C-terminally amidated. This defensin showed strong anti-Gram-positive activity and some anti-fungal activity; also, in contrast to other insect defensins, it showed anti-Gram-negative activity. A 17-residue apidaecin was characterized, showing anti-Gram-negative activity, and differing by a single amino acid substitution from the A. mellifera apidaecin. A 39-residue abaecin was isolated, the largest proline-rich antimicrobial peptide characterized to date, which showed activity against both Gram-negative and Gram-positive bacteria. Finally, we isolated an N-terminally blocked molecule, with a molecular mass of 10,122 Da, which showed activity against Gram-negative bacteria only. These characteristics are reminiscent of hymenoptaecin from the honeybee A. mellifera, but a definitive characterization of this molecule awaits further work. No evidence of lysozyme activity was found in the haemolymph of challenged or naive B. pascuorum.
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PMID:Novel antibacterial peptides isolated from a European bumblebee, Bombus pascuorum (Hymenoptera, Apoidea). 921 67

Cyclic antidepressants are still a dominating group of psychotherapeutic drugs used in the treatment of depression. One of their major side effect is salivary gland dysfunction (oral dryness, xerostomia), leading in humans to increased oral disease and dysfunction of speech, chewing, swallowing and taste. The purpose of this study was to assess the effects of the long-term administration of the tricyclic antidepressant desipramine and the reversibility of this treatment following a 15 d washout period on specific salivary proteins, composition of oral microbiota, and oral health (gingivitis) of aging female F344 rats. Total salivary proteins showed decreased concentrations with age and desipramine. Similar SDS/PAGE protein profiles appeared in all phases but in different relative amounts with age and treatment. While certain proteins maintained steady levels (lactoferrin) or decreased with age and treatment (amylase), the synthesis of proline-rich proteins, high molecular weight mucin-type glycoproteins, and lysozyme was induced with desipramine and age. The oral microbiota was significantly changed with age and the administration of the antidepressant. The incidence of gingivitis with desipramine was highest in the oldest animals, For the different parameters measured, recovery was delayed with age. These data indicate, that desipramine has profound effects on salivary protein secretion. This may partially explain the changes in microbiota and the increased incidence of gingivitis.
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PMID:Desipramine induced changes in salivary proteins, cultivable oral microbiota and gingival health in aging female NIA Fischer 344 rats. 1120 93

Relatively little is known about the formation of the acquired enamel pellicle other than that it involves the selective adsorption of specific proteins from oral fluids. Previous studies on the identification of pellicle components have relied largely on immunological or enzymatic detection and have been hampered by the fact that only minute quantities of pellicle can be removed from tooth surfaces. The present work describes an improved method of harvesting pellicle that combines mechanical and chemical removal; this approach was used to investigate systematically the desorption of in vitro pellicle components with different solutions. Eleven major in vitro pellicle proteins were identified by using a combination of electrophoretic separation and matrix-assisted laser desorption/ionization-reflectron time-of-flight mass spectrometry. A similar analysis of in vivo-formed pellicle revealed the presence of intact statherin, lysozyme, albumin and amylase. Further analysis of in vivo pellicle by liquid chromatography-electrospray ionization mass spectrometry suggested the presence of numerous low molecular-weight fragments of precursor proteins. The protein composition of in vitro whole-salivary pellicle adsorbed to hydroxyapatite and that of in vivo enamel pellicle differed for proline, the result of a reduction in the content of acidic proline-rich proteins in the in vivo samples. Unique features of the oral environment such as enzymatic activities or mineral surface properties may account for these differences between in vivo and in vitro pellicle formation.
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PMID:Compositional analysis of human acquired enamel pellicle by mass spectrometry. 1126 63

Human acquired enamel pellicle is formed by molecules selectively adsorbed onto tooth surfaces. The present work describes the use of monoclonal antibody (mAb) technology as a novel approach to identify micro amounts of components present in pellicle. MAbs were obtained with reactivities against statherin, histatin, mucous glycoprotein 1(MGI), albumin, amylase and human immunoglobulins (Igs), indicating that these are pellicle components, which was further confirmed by immunoblotting. No mAbs against proline-rich proteins (PRPs), lysozyme, mucous glycoprotein 2 (MG2), carbonic anhydrase, lactoferrin or peroxidase were obtained, suggesting that these components are absent, present in low amounts, or exhibit low antigenicity. Further characterization of the binding epitopes of some of th e obtained anti-MGO, anti-statherin and anti-histatin mAbs were carried out and the biological relevance is discussed. The results open up the possibility that immunization with human pellicle and mAbs production can be employed to identify hitherto unknown constituents of pellicle.
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PMID:Characterization of the immunologic responses to human in vivo acquired enamel pellicle as a novel means to investigate its composition. 1275 71

Human acquired enamel pellicle is composed of molecules that selectively adsorb from saliva onto tooth surfaces and provides a protective interface between the tooth enamel and the oral environment. To identify the micro-amounts of components present in pellicle, we immunized mice with in vivo-formed human acquired enamel pellicle and analyzed the serum immune responses. Selective reactivities of the serum (OD > 1.0 above background) against albumin, amylase, carbonic anhydrase II, sIgA, IgG, IgM, lactoferrin, lysozyme, proline-rich proteins, statherin, histatin 1, and mucous glycoprotein 1 were observed. We further confirmed the presence of proline-rich proteins, lactoferrin, lysozyme, and carbonic anhydrase II by probing in vivo pellicle with specific polyclonal anti-sera. The polyclonal antibody approach provided a powerful method for the identification of various pellicle proteins, including some which show mineral homeostasis or antimicrobial activity.
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PMID:Identification of in vivo pellicle constituents by analysis of serum immune responses. 1469 Nov 15


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