Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.17 (lysozyme)
 21,489 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Salivary proteins adsorbed to powdered enamel and cementum from parotid and submandibular saliva (1:1) of caries-resistant (CR) and caries-susceptible (CS) subjects were examined qualitatively by polyacrylamide disc electrophoresis and quantitatively by immunochemical procedures. The electrophoretic patterns showed no consistent difference between enamel and cementum or between CR and CS samples. Quantitatively, there were no significant differences between CR and CS samples, but significant differences between enamel and cementum. On the basis of ng/mm2, enamel adsorbed five times as much acidic proline-rich protein and cysteine-containing protein as cementum and nearly twice as much lysozyme. There were no significant differences in adsorption of albumin and lactoferrin. The lack of difference in the concentration of pellicle proteins in CR and CS subjects may be related to similar findings with parotid and submandibular saliva. The influence of the major differences in surface pellicle proteins between enamel and cementum on the properties of their respective pellicles is uncertain.
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PMID:Quantitative immunochemistry of salivary proteins adsorbed in vitro to enamel and cementum from caries-resistant and caries-susceptible human adults. 346 84

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.
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PMID:Human glandular salivas: their separate collection and analysis. 893 May 81

New cysteine protease inhibitors in human tears and milk and their medical significance are reviewed in this paper. As protective components against bacterial infection in the eyes, we detected four kinds of anti-bacterial proteins in normal human tears including lysozyme and three kinds of cysteine protease inhibitors. Using our reverse zymography of normal tears, three kinds of cysteine protease inhibitors were found to be 78kDa, 20kDa and 15kDa and were determined to be lactoferrin, Von Ebner's Gland (VEG) protein and cystatin S, respectively. All of them belong to the cystatin super family and VEG protein and cystatin S are well known cysteine protease inhibitors. The C-terminus area 17mer peptide, Y679-K695, of lactoferrin showed strong homology with a common active domain of the cystatin family and the synthesized peptide showed inhibition of cysteine proteases. Not only were disease-specific changes found in these inhibitor profiles, but also disease-specific new inhibitors in patients tears with certain autoimmune diseases. A 35kDa inhibitor, which was detected specifically in tears with Behcet's disease, an typical autoimmune disease, was determined to be a lacrimal acidic proline-rich protein based on the N-terminus sequence analysis. A 65kDa inhibitor of tears with Harada's autoimmune disease was determined to be an Ig heavy chain V-III region. In addition, lactoferrin content in Harada's disease was very low. We found two cathepsin inhibitors in bovine milk using reverse zymography, namely lactoferrin and beta-casein. The L133-Q151, in the human beta-casein molecule is the active inhibitory domain. They may play an important role in antiseptic and anti-infectious functions.
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PMID:Medical significance of cysteine protease inhibitors in mammalian secretory fluids. 1367 84

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.
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PMID:Salivary micelles: identification of complexes containing MG2, sIgA, lactoferrin, amylase, glycosylated proline-rich protein and lysozyme. 1504 80

We created hybrid proteins to study the functions of TonB. We first fused the portion of Escherichia coli tonB that encodes the C-terminal 69 amino acids (amino acids 170 to 239) of TonB downstream from E. coli malE (MalE-TonB69C). Production of MalE-TonB69C in tonB(+) bacteria inhibited siderophore transport. After overexpression and purification of the fusion protein on an amylose column, we proteolytically released the TonB C terminus and characterized it. Fluorescence spectra positioned its sole tryptophan (W213) in a weakly polar site in the protein interior, shielded from quenchers. Affinity chromatography showed the binding of the TonB C-domain to other proteins: immobilized TonB-dependent (FepA and colicin B) and TonB-independent (FepADelta3-17, OmpA, and lysozyme) proteins adsorbed MalE-TonB69C, revealing a general affinity of the C terminus for other proteins. Additional constructions fused full-length TonB upstream or downstream of green fluorescent protein (GFP). TonB-GFP constructs had partial functionality but no fluorescence; GFP-TonB fusion proteins were functional and fluorescent. The activity of the latter constructs, which localized GFP in the cytoplasm and TonB in the cell envelope, indicate that the TonB N terminus remains in the inner membrane during its biological function. Finally, sequence analyses revealed homology in the TonB C terminus to E. coli YcfS, a proline-rich protein that contains the lysin (LysM) peptidoglycan-binding motif. LysM structural mimicry occurs in two positions of the dimeric TonB C-domain, and experiments confirmed that it physically binds to the murein sacculus. Together, these findings infer that the TonB N terminus remains associated with the inner membrane, while the downstream region bridges the cell envelope from the affinity of the C terminus for peptidoglycan. This architecture suggests a membrane surveillance model of action, in which TonB finds occupied receptor proteins by surveying the underside of peptidoglycan-associated outer membrane proteins.
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PMID:Insight from TonB hybrid proteins into the mechanism of iron transport through the outer membrane. 1839 Jun 58

In-depth studies on the proteome of reflex tears are still inadequate. Hence, further studies on this subject will unravel the key proteins which are conjectured to possess vital functions in the protection of the ocular surface. Therefore, this study investigated the differences in the expression levels in proteome of reflex compared to basal tears. Basal (n = 10) and reflex (n = 10) tear samples from healthy subjects were collected employing the capillary method, subsequently pooled and the proteomes were characterized employing 1DE combined with LC-ESI-MS/MS strategy for label-free quantitative (LFQ) analysis. The differentially expressed proteins were validated by 2DE combined with LC-ESI-MS/MS and targeted-MS approach called accurate inclusion mass screening (AIMS) strategies. The analysis of the reflex tear proteome demonstrated increased abundance in proline-rich protein 4 (PRR4) and zymogen granule protein 16 homolog B (ZG16B) for the first time. Other abundant lacrimal proteins, e.g. lactotransferrin and lysozyme remained constant. Predominantly, the lacrimal gland-specific PRR4 represents the major increased protein in reflex tears in an attempt to wash out irritants that come into contact with the eye. Conversely, decreased abundance in Ig alpha-1 chain C, polymeric immunoglobulin receptor, cystatin S/SN, clusterin and mammaglobin were observed. This study had further unraveled the intricate proteome regulation during reflex tearing, especially the potential role of PRR4, which may be the key player in the protection and maintenance of dynamic balance of the ocular surface.
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PMID:Characterization of human reflex tear proteome reveals high expression of lacrimal proline-rich protein 4 (PRR4). 2617 77

A cross-sectional observational study was conducted to evaluate the inter-individual variation in the MALDI-TOF MS peptide profiles of unstimulated whole saliva in a population of 268 systemically healthy adults aged 18-30 yr (150 males and 118 females) with no apparent caries lesions or periodontal disease. Using Spectral Clustering, four subgroups of individuals were identified within the study population. These subgroups were delimited by the pattern of variation in 9 peaks detected in the 2-15 kDa m/z range. An Unsupervised Feature Selection algorithm showed that P-C peptide, a 44 residue-long salivary acidic proline-rich protein, and three of its fragments (Fr. 1-25, Fr. 15-35 and Fr. 15-44) play a central role in delimiting the subgroups. Significant differences were found in the salivary biochemistry of the subgroups with regard to lysozyme and chitinase, two enzymes that are part of the salivary innate defense system (p < 0.001). These results suggest that MALDI-TOF MS salivary peptide profiles may relate information on the underlying state of the oral ecosystem and may provide a useful reference for salivary disease biomarker discovery studies.
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PMID:A Study of the Variation in the Salivary Peptide Profiles of Young Healthy Adults Acquired Using MALDI-TOF MS. 2725 23