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

---

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.
...
PMID:Characterization of acquired denture pellicle from healthy and stomatitis patients. 140 50

Human saliva is secreted by the three pairs of major salivary glands (parotid, submandibular, and sublingual), and numerous minor ones, e.g. labial, buccal and (glosso)palatine glands. Using individually adapted collection devices, sublingual, submandibular, parotid and palatine secretions of five individuals were collected and analyzed. Electrophoretic analysis revealed that each type of saliva possesses characteristic features, despite interindividual variations. Parotid salivas are characterized by intensely staining amylase and proline-rich protein bands, but contain minute amounts of cystatins, lysozyme and the extra-parotid glycoprotein. Sublingual salivas are characterized by high concentrations of both types of salivary mucins, MG1 and MG2, and contain relatively high levels of lysozyme. Submandibular salivas contain highest concentration of salivary cystatin S. Palatine secretions contain high molecular weight mucins and a relatively high amylase concentration.
...
PMID:Human glandular salivas: their separate collection and analysis. 893 May 81

Mucins are high molecular-weight glycoproteins involved in the protection and lubrication of respiratory, gastrointestinal, and reproductive tracts. Hypersecretory diseases such as cystic fibrosis (CF), chronic bronchitis, and asthma result in dysregulated levels of mucin production stemming from increased abundance of mucin-secreting cell types in the surface airway epithelium and submucosal glands. The isolation of at least nine mucin genes has prompted studies to characterize the cellular expression patterns of these mucins in normal and diseased tissues. In the present study, in situ hybridization and immunocytochemical methods were used to determine the cellular distribution of MUC5B and MUC7 expression in CF and non-CF human bronchus. Our findings indicate that MUC5B and MUC7 have expression patterns in human bronchial airways that are limited exclusively to submucosal glands. Specifically, MUC5B expression was confined to all mucous tubules, whereas MUC7 expression was seen in a subset of lysozyme expressing serous tubules of submucosal glands. Interestingly, heterogeneity of MUC7 expression between glands of the same bronchus ranged from 0 to 93% of serous tubules, suggesting that functional diversity may exist between glands within the same bronchial sample. No remarkable differences were observed in the expression patterns of MUC5B or MUC7 between CF (n = 7) and non-CF (n = 10) bronchial samples. In conclusion, MUC5B and MUC7 expressions define different cellular compartments within submucosal glands of human bronchus and lend insight into the heterogeneity of mucin production in the lung.
...
PMID:MUC5B and MUC7 are differentially expressed in mucous and serous cells of submucosal glands in human bronchial airways. 965 Nov 78

The purpose of this study was to subculture normal human nasal epithelial (NHNE) cells without compromising their ability to differentiate into secretory and ciliated cells and to study the effect of retinoic acid on mucous and serous secretions in passaged cells and to compare the expression of mucin and lysozyme in cultured cells with those in in vivo nasal epithelium. The subcultured cells were tested after every passage for secretory differentiation in air-liquid interface cultures. The cultured NHNE cells secreted mucin and lysozyme. The cells became squamous and mucin secretion decreased when retinoic acid was deleted from the culture media. Cells from passage 1 through passage 2 remained able to differentiate into mucous or squamous cells. Mucin gene 4 (MUC4), MUC5AC, MUC7, MUC8, and lysozyme messenger RNAs were expressed in passage 2 NHNE cells. In conclusion, passage 2 NHNE cell cultures retain features of normal epithelium and are suitable for many studies of upper airway cell biology.
...
PMID:Secretory differentiation of serially passaged normal human nasal epithelial cells by retinoic acid: expression of mucin and lysozyme. 1085 73

Stimulated human submandibular/sublingual (HSMSL) and whole saliva were separated into sol and gel phases and mucins were isolated by density-gradient centrifugation in CsCl/4M guanidinium chloride. MUC5B and MUC7 were identified using anti-peptide antisera raised against sequences within the MUC5B and MUC7 apoproteins respectively. MUC7 was found mainly in the sol phase of both HSMSL and whole saliva, but some MUC7 was consistently present in the gel phase, suggesting that this mucin may interact with the salivary gel matrix. In HSMSL saliva, MUC5B was found in the gel phase; however, most of the material was 'insoluble' in guanidinium chloride and was only brought into solution by reduction. In whole saliva, the MUC5B mucin was present both in the sol and gel phases although some material was again 'insoluble'. Rate-zonal centrifugation of whole saliva showed that MUC5B mucins in the sol phase were smaller than those in the gel phase, suggesting differences in oligomerization and/or degradation. Antibodies against IgA, secretory component, lysozyme and lactoferrin were used to study the distribution of non-gel-forming proteins in the different phases of saliva. The majority of these proteins was found in the sol phase of both HSMSL and whole saliva. However, a significant fraction was present in the gel phase of whole saliva, suggesting a post-secretory interaction with the salivary gel matrix. A monoclonal antibody against a parotid salivary agglutinin was used to show that this protein is present mainly in the gel phase of both whole saliva and parotid secretion.
...
PMID:Macromolecular organization of saliva: identification of 'insoluble' MUC5B assemblies and non-mucin proteins in the gel phase. 1102 28

Goblet cells produce mainly MUC5AC, but also MUC5B and some MUC2 in apparently 'irritated' airways. MUC5B dominates in the submucosal glands although a little MUC5AC and MUC7 are usually present. MUC4 originates from the ciliated cells. After separation into a gel and a sol phase, lysozyme and lactoferrin are enriched in the salivary gel phase suggesting that mucus may act as a matrix for 'protective' proteins on the mucosal surface. A salivary MUC5B N-terminal fragment consistent with a cleavage event in the D' domain was detected with antibodies against various N-terminal peptide sequences suggesting that assembly of MUC5B occurs through a mechanism similar to that of the von Willebrand factor. Identification of additional cleavage sites C-terminal to the D' domain suggests that most of the N-terminal low-glycosylated part of MUC5B may be removed without affecting the oligomeric nature of the mucin. Possibly, the generation of mucins with different macromolecular properties through proteolytic 'processing' is one way of adapting the mucus polymer matrix to meet local physiological demands. Monomeric mucins that appear to turn over rapidly in the airway epithelium have been identified using radiolabelled mucin precursors. 'Shedding' of such mucins after microbe attachment may prevent colonization of epithelial surfaces.
...
PMID:Respiratory tract mucins: structure and expression patterns. 1256 89

Micelles represent macromolecular structures in saliva and the aim of this study was to identify salivary proteins that occur in these globular particles. Micelles were isolated from whole saliva (WS) collected from three individuals and analysed in different experiments. Samples were subjected to polyacrylamide gel electrophoreses, hydrolysed to determine their amino acid composition and total protein concentration, examined by scanning electron microscopy and examined on Western blots probed with a panel of antibodies directed against salivary proteins. On Coomassie Brilliant Blue stained gels, the banding pattern of whole saliva and micelles was similar but the intensity of bands was quite different. Amino acid analysis confirmed that the amino acid composition of micelles was distinct from that of whole saliva. Scanning electron microscopy showed that micelles exhibit a complex pattern consisting of individual particles or clusters of particles with different sizes and shapes. Micelles contain proteins with high (MG2 and secretory IgA), intermediate (lactoferrin, amylase and glycosylated proline-rich protein (PRP)) and low (lysozyme) molecular weight that were immuno-detected on blots probed with specific antibodies. Micelles represent particulate multicomponent structures in whole saliva that contain a subset of salivary proteins known to be important components of the innate immune system and are likely to play an important role in the maintenance of homeostasis in the oral environment.
...
PMID:Salivary micelles: identification of complexes containing MG2, sIgA, lactoferrin, amylase, glycosylated proline-rich protein and lysozyme. 1504 80

We have provided evidence that hen egg white lysozyme (HEWL) existed in alpha helical and beta structure dominated molten globule (MG) states at high pH and in the presence of tertiary butanol, respectively. Circular dichroism (CD), intrinsic fluorescence, ANS binding and acrylamide-induced fluorescence quenching techniques have been used to investigate alkali-induced unfolding of HEWL and the effect of tertiary butanol on the alkaline-induced state. At pH 12.75, HEWL existed as molten globule like intermediate. The observed MG-like intermediate was characterized by (i) retention of 77% of the native secondary structure, (ii) enhanced binding of ANS (approximately 5 times) compared to native and completely unfolded state, (iii) loss of the tertiary structure as indicated by the tertiary structural probes (near-UV, CD and Intrinsic fluorescence) and (iv) acrylamide quenching studies showed that MG state has compactness intermediate between native and completely unfolded states. Moreover, structural properties of the protein at isoelectric point (pI) and denatured states have also been described. We have also shown that in the presence of 45% tertiary butanol (t-butanol), HEWL at pH 7.0 and 11.0 (pI 11.0) existed in helical structure without much affecting tertiary structure. Interestingly, MG state of HEWL at pH 12.7 transformed into another MG state (MG2) at 20% t-butanol (v/v), in which secondary structure is mainly beta sheets. On further increasing the t-butanol concentration alpha helix was found to reform. We have proposed that formation of both alpha helical and beta sheet dominated intermediate may be possible in the folding pathway of alpha + beta protein.
...
PMID:Different molten globule-like folding intermediates of hen egg white lysozyme induced by high pH and tertiary butanol. 1730 93

In this research, we investigated the interaction occurring between oil-in-water emulsion droplets, stabilized by different emulsifiers, i.e. lysozyme and beta-lactoglobulin (beta-lg), and salivary proteins (SPs) with a molecular mass (M(r)) above about 10kDa. Different techniques, i.e. infrared spectroscopy, Western blotting, PAS staining and SDS-PAGE coupled to MS, were employed for this purpose. This study demonstrated the interaction between several salivary proteins and the emulsifiers at the oil-water interfaces. In particular, results show that the high M(r) mucin MUC5B was strongly bound to lysozyme stabilized emulsions, whereas beta-lg stabilized emulsions associated with MUC7 and, moderately, with MUC5B. Furthermore, we observed that salivary proteins in the range M(r) 10-100kDa associated differently with emulsion droplets. A large majority of SPs was found to interact with lysozyme stabilized emulsion droplets whilst in case of beta-lg stabilized emulsions, the SPs distribute more evenly between the fraction associated and non-associated with the droplets. A clear example is alpha-amylase (M(r) approximately 55kDa) which predominantly associates with lysozyme stabilized emulsion droplets, but not with beta-lg emulsion droplets. To conclude, our findings indicate that adsorption/association of salivary protein components onto the emulsion droplets is related to the type of emulsifying proteins at the oil-water interfaces and it is probably driven by the overall net charge at the droplet's oil-water interfaces, i.e. positive for lysozyme stabilized emulsions and negative for beta-lactoglobulin stabilized emulsion at neutral pH.
...
PMID:Identification of salivary proteins at oil-water interfaces stabilized by lysozyme and beta-lactoglobulin. 2019 85

Both the major and minor salivary glands are the sources of saliva, a fluid vital for the maintenance of a healthy oral cavity. Here, the expression profiles of human submandibular (SMG) and labial glands (LG) were compared by RT-PCR analysis of laser microdissected mucous and serous cells, respectively. The focus was on trefoil factor family (TFF) genes, but also other genes encoding secretory proteins (mucins, lysozyme, amylase, statherin, and histatins) or aquaporin 5 were included. Immunofluorescence studies concerning TFF1-3, FCGBP, amylase, and lysozyme are also presented. It was shown that LGs clearly contain serous cells and that these cells differ in their expression profiles from serous SMG cells. Furthermore, all three TFF peptides, together with MUC5B, MUC7, MUC19, and FCGBP, were clearly detectable in mucous acini of both LGs and SMGs. In contrast, lysozyme was differentially expressed in LGs and SMGs. It can be expected that labial saliva may play a particularly important role for protecting the teeth.
...
PMID:Expression analysis of human salivary glands by laser microdissection: differences between submandibular and labial glands. 2079 22


1 2 Next >>

---