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)

The antigenic and allergenic epitope maps of the hen egg-white ovalbumin, ovomucoid, ovotransferrin and lysozyme were obtained using one-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis and two-dimensional sodium dodecyl sulfate gel electrophoresis following isoelectric focusing. The isoelectric points of egg-white proteins were assigned by the isoelectric focusing technique. Two-dimensional electrophoresis following isoelectric focusing provided further information regarding epitope mapping. Furthermore, electrophoretic transfer of the proteins to nitrocellulose and subsequent immunoautoradiography, clearly demonstrated the allergenicity of these proteins. An important benefit of these methods was confirming that lysozyme bound strongly to IgE in all the human sera from egg-allergic individuals and that lysozyme, in addition to ovalbumin, ovomucoid and ovotransferrin, was one of the major allergens of hen egg-white.
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PMID:Characterization of four major allergens of hen egg-white by IEF/SDS-PAGE combined with electrophoretic transfer and IgE-immunoautoradiography. 169 14

Immunologic defense factors in the human olfactory mucosa were localized immunohistochemically. Olfactory epithelium was identified with an antiserum to olfactory marker protein, specific for olfactory receptor neurons. Constituents of the secretory immune system, including IgA, IgM, secretory component, and J chain, were localized in the acinar and duct cells of Bowman's glands and in the mucociliary complex. In addition, B lymphocytes in the lamina propria near Bowman's glands displayed immunoreactivity for IgA, IgM, and J chain. Immunostaining also localized other humoral factors. Immunoreactivity for IgG was present throughout the stroma and in B lymphocytes in the lamina propria. Antibody to IgD stained numerous B lymphocytes clustered below the basement membrane. Antibody to IgE stained similarly distributed cells; toluidine blue staining demonstrated that many were mast cells. In addition, antibodies to IgD and IgE stained occasional intraepithelial B lymphocytes or mast cells. Two antimicrobial proteins, lactoferrin and lysozyme, were localized in Bowman's glands and the mucociliary complex. Thus, the human olfactory mucosa, which provides a direct neural route for pathogens to the brain, is a site for synthesis and secretion of immune and other defense factors.
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PMID:Characterization of the immune barrier in human olfactory mucosa. 173 51

Immunohistochemical techniques were used to investigate the cellular distribution of components of the secretory immune system, including secretory immunoglobulin, secretory piece, and J chain, as well as other immunoglobulins and nonspecific defense factors in the olfactory mucosae of salamanders and rats. In the salamander, secretory immunoglobulin M, and J chain were localized in duct and acinar cells of Bowman's glands, in B lymphocytes, and in sustentacular cells in immature regions of the olfactory mucosa. Lactoferrin and lysozyme were also present in Bowman's glands, in sustentacular cells in immature regions of the olfactory mucosa, and in blood cells in the lamina propria. Olfactory nerve section resulted in the presence of increased numbers of secretory immunoglobulin-immunoreactive B lymphocytes and in an altered distribution of IgM, secretory piece, and lactoferrin. In the rat, secretory immunoglobulin A and J chain were localized in duct and acinar cells of Bowman's glands and in B lymphocytes in the lamina propria. Secretory piece could be demonstrated in Bowman's glands only in rats that had a prior viral infection. Other defense factors, localized in the lamina propria, included IgG in the connective tissue stroma and in B lymphocytes, IgD-immunoreactive B lymphocytes, and IgE-immunoreactive cells that were identified as mucosal mast cells. Lactoferrin and lysozyme were present in serous acinar cells of Bowman's glands and in blood cells. These results demonstrate that the olfactory mucosa is protected from pathogenic invasion by the secretory immune system as well as other immunoglobulins, lactoferrin, and lysozyme.
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PMID:Immunohistochemical localization of components of the immune barrier in the olfactory mucosae of salamanders and rats. 176 18

Immunoglobulin-producing cells and epithelial expression of secretory component (SC), amylase, lysozyme (Ly) and lactoferrin (Lf) were studied by immunohistochemistry to obtain information about the development of mucosal immunity. Tissue specimens were obtained from 20 fetal and 40 postnatal parotid glands. (1) Fetal specimens. Occasional IgM- and IgA- but no IgD-, IgG- or IgE- producing cells were seen (ratios, IgM:IgA:IgD:IgG:IgE approximately 4:1:0:0:0). The IgAl subclass dominated (median 90%, range 50-95%) and these cells were mostly J-chain-positive (median 97%, range 94-98%). Only few IgA2-producing cells were seen (median 10%, range 5-50%) and they were also mostly J-chain-positive (median 99%, range 98-100%). Amylase, Ly and Lf were most prominent in early fetal life, while only small amounts of SC were present. (2) Postnatal specimens. Secretory component increased markedly along with a growing number of IgA- and IgD-producing cells (IgA:IgM:IgD:IgG:IgE approximately 4:2:1:1:0). The IgAl subclass remained predominant (median 65%, range 50-90%) although the proportion of IgA2-positive cells tended to be raised (median 35%, range 10-50%). Most IgAl (median 97%, range 67-100%) and IgA2 (median 94%, range 75-100%) cells were J-chain-positive. These features probably reflected local activation of the immune system in response to environmental factors. The amount of amylase, Ly and Lf decreased shortly after delivery, perhaps because the cellular stores were emptied by postnatal increase in secretory activity.
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PMID:Ontogenesis of the secretory immune system and innate defence factors in human parotid glands. 193 1

Platelets, basophils and neutrophils from a patient with the Wiskott-Aldrich syndrome (WAS) were exposed to stimuli that activate specific membrane receptor or directly initiate biochemical events (e.g. the Ca2+ ionophore A23187 and ionomycin or arachidonic acid). Platelets from this patient did not aggregate in response to ADP, collagen, thrombin or adrenaline, which activate specific membrane receptors. Platelet aggregation, however, was normal in response to compound A23187, ionomycin or exogenous arachidonic acid. Histamine release from basophils of the WAS patient was normal in response to anti-IgE, a formylated peptide (f-met peptide), and to A23187. Similarly, the release of the lysosomal enzymes, beta-glucuronidase and lysozyme, from neutrophils of the WAS patient in response to serum treated zymosan (Zx), f-met peptide, and A23187 was not significantly different from that of his parents and 13 normal donors. These results suggest that the primary defect in WAS is selectively present in platelets and is located in a biochemical step between receptor activation and Ca2+ influx and/or initiation of arachidonate metabolism.
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PMID:The Wiskott-Aldrich syndrome: studies of platelets, basophils and polymorphonuclear leucocytes. 242 57

In autumn and spring a group of 132 ten-year-old school children (54.5% from families of smokers) were examined for blood content of immunoglobulins (IgG, IgA, (gM, in autumn including also IgE), lysozyme (LYS) and the so called acute reactants (alpha-1-antitrypsin = A1AT; alpha-2-macroglobulin = A2M; transferrin = TRF; ceruloplasmin = CPL); and for saliva sIgA and sLYS. Autumn examination detected significantly higher mean values of IgE in children from families of smokers, while other mean differences remained insignificant. Spring examination revealed significant differences in the means of IgA levels children from families of smokers (FS) had significantly lower levels of IgA while their saliva sIgA values were significantly higher. Mean spring CPL levels in FS were significantly higher. Analysis of distribution curves of autumn examination showed a significant shift of A1AT towards higher values in boys from FS. Girls from FS exhibited a shift of LYS towards lower values. Spring examination in boys FS evidenced a shift of CPL and sIgA values towards higher values; the curve of serum IgA levels split distinctly into two subgroups. In girls from FS the only change observed during the spring examination was a shift of A2M levels towards higher values with an indication of a split. To conclude, passive smoking in school children is responsible for a number of significant changes, the latter being more frequent and marked in spring when the children's organism is weakened by many other unfavourable circumstances. More significant changes were seen in boys.
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PMID:Humoral defending mechanisms in children of smoking parents. 244 22

Basophilic granulocytes were purified from the blood of normal individuals by successive isopyknic centrifugation and elutriation centrifugation. Starting with the leukocyte-rich fraction of 500 ml of blood, we recovered 31 to 80% (mean 51%, n = 20) of the basophils in 45 to 87% purity (mean 69%, n = 23). The contaminating cells were mainly lymphocytes. The basophils were greater than 98% vital (exclusion of ethidium bromide and hydrolysis of fluorescein diacetate). The histamine content of the basophils was 1.1 to 2 pg/cell (mean 1.6 pg/cell, n = 22). With anti-IgE, 30 to 50% of the histamine was released; with phorbol myristic acetate (PMA) or the calcium ionophore A23187, 70 to 100% of the histamine was released. Serum-opsonized zymosan (STZ) did not induce histamine release. Reactions with monoclonal antibodies revealed that the basophils expressed the C3bi receptor (CR3) and the leukocyte function-associated antigen 1 (LFA1), but not the gp 150,95 antigen, the C3b receptor (CR1), or the low avidity Fc gamma receptor. Basophils carry class I but not class II HLA antigens. During incubation of the basophils with serum-opsonized Staphylococcus aureus or Escherichia coli, these bacteria were neither phagocytized nor killed. STZ, PMA, A23187, or anti-IgE did not initiate an "oxidative burst" in the basophils. This was tested with oxygen consumption, cytochrome c reduction, NBT reduction, chemiluminescence, and release of hydrogen peroxide. Moreover, we did not detect cytochrome b558, superoxide dismutase, catalase, or peroxidase in the basophils. Of the typical granule-associated enzymes lysozyme, Vitamin B12-binding protein, and beta-glucuronidase, only beta-glucuronidase was present in the basophils in detectable amounts. This enzyme was released, together with histamine, on incubation of the cells with PMA, A23187, or anti-IgE, but not with STZ. We conclude that basophils from normal human blood are not phagocytes and are probably not involved in the oxidative defense of the host against foreign antigens.
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PMID:Metabolic comparison between basophils and other leukocytes from human blood. 300 19

The radioallergosorbent test (RAST) and RAST inhibition test were used to examine cross-allergenicity amongst the major hen's egg-white and egg-yolk proteins. Using ovalbumin as a reference allergen to compare cross-reactivity, it was apparent that the proteins conalbumin, ovomucoid and lysozyme substantially inhibited binding to ovalbumin discs of IgE in the sera of patients clinically hypersensitive to egg. The converse situation with conalbumin, ovomucoid and lysozyme on the discs and ovalbumin as the inhibitor also resulted in significantly decreased levels of IgE binding to the proteins on the discs. It was also demonstrated that cross-reactions occurred between ovalbumin and the yolk protein, apovitellenin I. Cross-reaction was also observed surprisingly when egg lysozyme was on the disc and the milk protein allergen alpha-lactalbumin was used as the inhibitor. The demonstration of cross-reaction between all of these proteins may signify that there are a number of common allergenic determinants on these egg proteins, thus providing a molecular basis for the phenomenon of cross-reactivity.
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PMID:Allergenic cross-reactivity of egg-white and egg-yolk proteins. An in vitro study. 365 6

Twenty-five workers in an egg-processing factory were evaluated for respiratory sensitization to inhaled egg proteins by a physician evaluation, serial peak expiratory flow rate (PEFR) measurements for a 1-week period, and immunologic tests. Immunologic studies included skin prick tests, serum-specific IgE (RAST), and specific IgG (ELISA) to solutions prepared from commercial food allergens: factory-powdered egg white and yolk products and purified egg white fractions, including ovalbumin, ovomucoid, lysozyme, and conalbumin. Six workers had significant daily PEFR lability (greater than 20%) of whom five had associated cutaneous reactivity to at least one egg allergen. A diagnosis of "definite asthma" was established in five workers suspected by the physician of having asthma. These five workers exhibited significant decrements in daily PEFR that were accompanied by bronchial symptoms. Occupational asthma was diagnosed by the physician in four of the five latter workers. Definite asthma was significantly associated with both cutaneous reactivity to egg allergens (p less than 0.01) and RAST binding (p less than 0.01). Of eight workers with cutaneous reactivity to at least one egg reagent, four workers (50%) were positive to only purified egg white fractions. The highest levels of RAST binding were detected in four workers, and the best binding activity was to ovomucoid and ovalbumin fractions. Elevated specific IgG responses were significantly higher in egg-factory workers to whole egg (p less than 0.005), lysozyme (p less than 0.002), and conalbumin (p less than 0.002) allergens compared to responses of nonexposed control subjects. However, no differences in specific IgG were detected between symptomatic and asymptomatic workers.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Clinical and immunologic studies among egg-processing workers with occupational asthma. 369 57

Thirty-eight production workers exposed to Ni and 35 exposed to Co were examined for the content of Ni and Co in hair, the serum concentration levels of immunoglobulins, IgG, IgA, IgM, and IgE, and serum proteins, alpha 2-macroglobulin (A2M), transferrin (TRF), alpha 1-antitrypsin (A1AT), ceruloplasmin (CPL), lysozyme (LYS), and alpha 1-glycoprotein (A1GP). Atomic absorption analysis of hair revealed that the respective geometric mean values of Ni and Co in Ni-exposed workers were 216.75 and 3.31 micrograms X g-1 and in Co-exposed workers 34.5 and 96.81 micrograms X g-1. These values were significantly higher than respective control values found in nonexposed individuals matched by age (Ni: 3.31 and Co: 0.38 micrograms X g-1). These findings suggest that hair analysis is a suitable method for the biological monitoring of exposure to these two metals. Tests for serum proteins revealed that nickel workers differed from controls by exhibiting significantly elevated IgG, IgA, and IgM levels; cobalt workers by a significant elevation of IgA level; and both exposed groups by a significant drop in the IgE level. A significant rise in the concentration (P less than 0.001-P less than 0.005) was also recorded in the case of A1AT, A2M, CPL, and LYS. The possible biomedical implications of these immunobiochemical findings are critically analyzed.
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PMID:Human exposure to nickel and cobalt: biological monitoring and immunobiochemical response. 373 11


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