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)

Little is known about the regulatory effects of cytokines on various nasal secretions in normal human nasal epithelial cells. The aim of this study was to examine whether TNF-alpha, IL-1beta or their combination can increase the secretion of mucin as an indicator of mucous secretion, the secretion of lysozyme as an indicator of serous secretion and the secretion of IL-6 and IL-8 as important cytokines. In addition, we wanted to examine their message levels in normal human nasal epithelium. On day 12 of culture, passage-2 normal human nasal epithelial cells were treated with 10 ng/ml TNF-alpha, 10 ng/ml IL-1beta and combinations of both. Twenty-four hours later, the apical secretions were collected. A mixture of TNF-alpha and IL-1beta synergistically increased secretion of mucin, IL-6 and IL-8, but did not increase secretion of lysozyme. A combination of TNF-alpha and IL-1beta showed a questionable increase of MUC2 mRNA levels. TNF-alpha, IL-1beta and a combination of both all significantly increased MUC8 mRNA levels. Neither TNF-alpha, IL-1beta nor a combination of both increased MUC5AC, MUC5B and lysozyme mRNA levels. IL-1beta alone or a combination of TNF-alpha and IL-1beta comparably increased IL-6 and IL-8 mRNA levels slightly. In conclusion, a mixture of inflammatory mediators can synergistically increase secretion of mucin, IL-6 and IL-8 in human nasal epithelium. Accordingly, nasal secretions may be under the control of an inflammatory mediator network.
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PMID:Effects of TNF-alpha and IL-1 beta on mucin, lysozyme, IL-6 and IL-8 in passage-2 normal human nasal epithelial cells. 1072 32

Class III mucin, identified by paradoxical concanavalin A staining, is confined to gastric gland mucous cells and is an essential component of the gastric surface mucous gel layer. The pretreatment required has hampered the application of this method to electron microscopic studies. Antibody HIK1083 reacts selectively with class III mucins. The present study was undertaken to explore, electron microscopically, the immunoreactivity of the human stomach to HIK1083. We examined normal mucosa from resected human stomachs (five cases; formalin-fixed, paraffin-embedded) and gastric biopsy specimens from patients with early gastric cancer [nine cases; glutaraldehyde- and osmium-fixed, epoxy-embedded (seven cases) and half-strength Karnovsky's solution-fixed, Lowicryl K4M-embedded (two cases)]. Immunostaining with HIK1083 and anti-lysozyme antibody was examined under light and electron microscopes. Gland mucous cells were labeled with HIK1083, and lysozyme was detected in some gland mucous cells and surface mucous cells. Electron microscopically, the secretory granules of gland mucous cells contained a single electron-dense core. HIK1083-positive mucins and lysozyme coexisted in the secretory granules of gastric gland mucous cells. HIK1083-reactive mucins and lysozyme were distributed in the matrix and in the dense core of these secretory granules, respectively. HIK1083 can be used for electron immunohistochemistry.
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PMID:Coexistence of gland mucous cell-type mucin and lysozyme in gastric gland mucous cells. 1076 61

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.
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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.
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PMID:Macromolecular organization of saliva: identification of 'insoluble' MUC5B assemblies and non-mucin proteins in the gel phase. 1102 28

Mucous hypersecretion is a major complication of otitis media and can prolong the disease course and increase morbidity. Mucin, a major component of mucus, is a macromolecular complex of glycoprotein and makes mucus viscous. Lysozyme is a secretory element of the middle ear mucosa. which has a non-specific and innate antibacterial function. We attempted to identify factors that regulate these secretory products and their morphological phenotype using cultured human middle ear epithelial cells. Cellular differentiation was induced by creating an air liquid interface on culture day 9 in serum-free conditioned media. Omission of retinoic acid (RA) caused decrease in the secretion of mucin and lysozyme, and in the cellular expression of MUC 2, MUC 5AC and MUC 5B mRNA. In contrast, removal of triiodothyronine (T3) caused an increase in the secretion of mucin and the level of MUC5AC mRNA. When hydrocortisone (HC) was removed from the media, the secretion of mucin was decreased with out an apparent change of message level. The expression of MUC 1 mRNA was not changed by the respective deficiency of RA. T3 or HC. The effect of T3 or HC on lysozyme was not significant. This study shows that RA, T3 and HC influence the morphological phenotype and the secretory function of mucin and lysozyme in cultured human middle ear epithelial cells. This culture system can serve as an in vitro model for study of the regulation of various cellular secretions in human middle ear epithelium.
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PMID:Effects of retinoic acid, triiodothyronine and hydrocortisone on mucin and lysozyme expression in cultured human middle ear epithelial cells. 1120 May 89

One hundred and forty five patients with different forms of dust-induced lung disease and 57 controls having no contacts with industrial aerosols were examined. It was ascertained that clinical and functional evidence cannot predict the course of the disease and the development of infectious complications (silicotuberculosis, mechanic bronchitis). Impaired humoral immunity and nonspecific resistance in dust-induced lung disease depend on the type of disease and predispose to infectious complications. Predisposition to occupational lung diseases (pneumoconioses, mechanical bronchitis) is associated with increases in the concentrations of plasma fibronectin and serum IgA and a decrease in serum mucin antigen levels. In chronic mechanical bronchitis, there were lower activities of lysozyme and complement and elevated serum IgM and IgG concentrations. Fibronectin, total IgE and the inflammatory marker the mucin antigen 3EG5 are involved in immunological inflammation in dust-induced lung disease. It is worth of determining the factors of humoral immunity and nonspecific resistance in workers contacting with high concentrations of industrial aerosols and in patients with dust-induced diseases to make a precise assessment of the time course of changes in a pathological process and to define a risk for infectious complications.
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PMID:[Immunological changes in dust-induced lung diseases]. 1131 68

Mucus hypersecretion is an important characteristic of many airway diseases. Mucin is the major component of mucus, and is secreted from surface goblet cells of the airway epithelium and mucous cells of submucosal glands. Lysozyme is an enzyme secreted by serous cells of airway submucosal glands. We hypothesized that secretagogues acting through different pathways would have different effects on tracheal mucin and lysozyme secretion. We used a sandwich enzyme-linked lectin assay (ELLA) to measure mucin-like glycoprotein secretion and a spectrophotometric method to measure lysozyme secretion from isolated ferret tracheal segments. We evaluated the secretory response to four secretagogues; prostaglandin F(2alpha) (PGF(2alpha)), adenosine triphosphate (ATP), methacholine (MCh), and human neutrophil elastase (HNE). Each agent stimulated mucin and lysozyme secretion. The relative potency was PGF(2alpha)< or =ATP<MCh<HNE for mucin and ATP< or =PGF(2alpha)<MCh<HNE for lysozyme secretion. We showed that there is an anatomic gradient for constitutive and stimulated mucin and lysozyme secretion with the distal tracheal segments secreting more mucin and lysozyme per gram of tissue than the proximal segments. This robust model system can be used to evaluate the regulation of airway mucous and serous cell secretion and to assess the effect of agents that might alter the secretory response. We confirm that on an equimolar basis, HNE is one of the most potent mucus secretagogues.
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PMID:Regulation of secretion from mucous and serous cells in the excised ferret trachea. 1134 43

An adhesion-promoting protein involved in the binding of Lactobacillus fermentum strain 104R to small intestinal mucus from piglets and to partially purified gastric mucin was isolated and characterized. Spent culture supernatant fluid and bacterial cell wall extracts were fractionated by ammonium sulfate precipitation and gel filtration. The active fraction was purified by affinity chromatography. The adhesion-promoting protein was detected in the fractions by adhesion inhibition and dot blot assays and visualized by polyacrylamide gel electrophoresis (PAGE), sodium dodecyl sulfate-PAGE, and Western blotting with horseradish peroxidase-labeled mucus and mucin. The active fraction was characterized by estimating the relative molecular weight and by assessing the presence of carbohydrates in, and heat sensitivity of, the active region of the adhesion-promoting protein. The purified protein was digested with porcine trypsin, and the peptides were purified in a SMART system. The peptides were tested for adhesion to horseradish peroxidase-labeled mucin by using the dot blot adhesion assay. Peptides which bound mucin were sequenced. It was shown that the purified adhesion-promoting protein on the cell surface of L. fermentum 104R is extractable with 1 M LiCl and low concentrations of lysozyme but not with 0.2 M glycine. The protein could be released to the culture supernatant fluid after 24 h of growth and had affinity for both small intestinal mucus and gastric mucin. In the native state this protein was variable in size, and it had a molecular mass of 29 kDa when denatured. The denatured protein did not contain carbohydrate moieties and was not heat sensitive. Alignment of amino acids of the adhering peptides with sequences deposited in the EMBL data library showed poor homology with previously published sequences. The protein represents an important molecule for development of probiotics.
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PMID:Purification and characterization of a surface protein from Lactobacillus fermentum 104R that binds to porcine small intestinal mucus and gastric mucin. 1197 5

Muciphages are mucin-rich phagocytes believed to evolve as a result of the disruption of colorectal crypts. In a previous work we found, in rectal biopsies from patients with chronic ulcerative colitis, muciphages having not only mucin but also lysozyme, an enzyme with a potent antimicrobial activity. Recently we detected lysozyme-rich muciphages in the normal mucosa of the stalk of colonic adenomas. Filed hematoxylin and eosin (H&E)-stained sections from 30 consecutive colorectal adenomas with a stalk (lined by normal colorectal mucosa) were stained with PAS (for mucopolysaccharides), with CD68 (to label macrophages) and with lysozyme (Muramidase). Of the 30 adenomas, 16 (40%) showed muciphages in the mucosa of the stalk. Those muciphages were PAS- CD68- and lysozyme-positive. Although the significance of these findings remains elusive, it is conceivable that lysozyme-rich muciphages mirror increased cell destruction in colorectal adenomas with a high cell turnover. The possibility that lysozyme-rich muciphages surrounding adenomas are instrumental in a novel molecular mechanism of host defense, effective at the early stages of colorectal carcinogenesis, was also entertained. Such a mechanism would prevent the lateral expansion of the dysplastic epithelium of the adenoma into the surrounding normal mucosa of the stalk.
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PMID:Lysozyme-rich muciphages surrounding colorectal adenomas. 1201 65

Recent technical advances now permit the serial culture of normal human middle ear epithelial (NHMEE) cells. However, the ciliary differentiation of these cells has not been achieved. The purpose of this study was to establish a culture system in order to differentiate serially cultured NHMEE cells into ciliated cells. If ciliated cells developed, the percentages of ciliated cells and secretory cells were measured throughout the duration of culture. We also examined the levels of mucin and lysozyme secretion and their mRNAs in a time-dependent manner. Human middle ear mucosa with a normal appearance was harvested and serially cultured after enzymatic disaggregation. These cells were cultured in an air-liquid interface (ALI) culture system for 2, 7, 14, 21 and 28 days after confluence. Ciliogenesis usually began 16-18 days after confluence. The percentage of ciliated cells detected by means of immunohistochemical staining increased over time up to a maximum of 10.6% but the percentage of secretory cells remained stable at approximately 40% throughout the duration of culture. By Day 14 after confluence, the amounts of mucin and lysozyme secretion, as measured by dot-blotting analysis, had increased significantly and then remained stable. The expression levels of mucin gene 5B (MUC5B), MUC8 and lysozyme increased with the duration of culture. MUC8 in particular showed a dramatic increase on Day 28 after confluence. In contrast, the level of MUC5AC mRNA peaked on Day 14 after confluence, and then decreased. In conclusion, ciliary differentiation of NHMEE cells can be induced using an ALI culture system. Our study also suggests that secretory function develops earlier than ciliogenesis, and that the expressions of MUC5B and MUC8 mRNAs increase as a function of differentiation.
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PMID:Ciliary and secretory differentiation of normal human middle ear epithelial cells. 1203 May 73


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