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)

Total count of morbidity as well as prevalence of upper respiratory tract diseases (RTD) were followed in 210 miners working in shale mines with a low level of ionizing radiation regarding their smoking habits. After one and half year of observation were performed some tests of humoral immunity in the blood serum and saliva (immunoglobulins G, A, M and sIgA) as well as some tests of non-specific indices (alpha 2 macroglobulin -A 2M, transferrin -TRF, lysozyme -- LYS). The number of healthy non--smokers reached 41.3%, whereas the number of healthy smokers was only 26.5% (P less than 0.05). The greater was the number of diseases in single subjects, the greater was the difference between smokers and non-smokers (P less than 0.005). The difference between RTD morbidity of smokers and non-smokers was not significant in the subgroup of miners employed less than 10 years, but the length of employment it rose significantly (P less than 0.002) in disfavour of the smokers. The difference between smokers and non-smokers is emphasized by ageing. The mean levels of immunoglobulins (IgG, IgA, IgM) are significantly higher in healthy non-smokers in comparison with other miners; that is stressed also by distribution analysis. The distribution analysis. The distribution of A 2M values is also significantly different in the subgroup of healthy non-smokers compared with other miners. Highly significant differences were found between healthy non-smokers and other miners by discrimination analysis of coupled tests. The differences among the paired comperformed some tests of humoral immunity in the blood serum and saliva (immunoglobulins are apparently cooperative in the prevention of RTD. In contrast to that the level of A 2M are in reverse relationship to the levels of Ig; in the subgroup of healthy non-smokers low levels of A 2M are in connection with high levels of Ig of all three classes. The results are discussed from the point of view of the smoker's habits, the length of employment in mine's environment, the age of the miners and the supposed genetical factors.
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PMID:Morbidity and immunological test in miners working in mines with low ionizing radiation level. 620 25

Polymorphonuclear leukocytes (PMN) aggregate and avidly attach to endothelium in response to chemotactic agents. This response may be related in part to the release of the specific granule constituent lactoferrin (LF). We found by using immunohistology and biochemical and biophysical techniques that LF binds to the membrane and alters the surface properties of the PMN. Upon exposure of PMN treated with 5 micrograms/ml cytochalasin B to 2 x 10(-7) M formyl-methionine-leucine-phenylalanine for 5 min, the PMN mobilized LF to their surface as observed by immunoperoxidase staining for LF. At added LF levels ranging from 4 to 15 micrograms/10(7) PMN there was a dose-dependent reduction in PMN surface charge reaching 4 mV, when the partitioning into the membrane of a charged amphipathic nitroxide spin label was measured by electron spin resonance spectroscopy, whereas transferrin was without effect. When 125I-FeLF was added to human PMN in increasing amounts and the results corrected for the residual amount of free LF contaminating the cells, the PMN were saturated with LF at concentrations between 100 and 200 nM in the medium. Human PMN bound 1.35 x 10(6) molecules per cell and the calculated value for the association constant for these receptors was 5.2 x 10(6) M-1. Additionally, 6 micrograms/ml LF served as an opsonin for rabbit MN to promote PMN uptake by rabbit macrophages, when assessed by electron microscopy, but lysozyme did not. These studies indicate that LF can bind to the surface of the PMN and reduce its surface charge. This correlates with enhanced "stickiness" leading to a variety of cell-cell interactions.
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PMID:Membrane-bound lactoferrin alters the surface properties of polymorphonuclear leukocytes. 629 May 34

Twenty-one protein components were measured in urine specimens from 12 subjects with postural proteinuria in the recumbent posture and after a period of upright lordotic posture. The lordotic posture produced an increased urinary excretion of total protein and 19 protein components, particularly of albumin, IgG globulin, and transferrin (128, 68, and 167-fold, respectively). However, 90 min after the lordotic posture, most of the protein components returned to initial values, whereas albumin, IgG globulin, and transferrin remained high. beta 2-Microglobulin, retinol binding protein, and lysozyme showed the smallest increases after the lordotic posture. These findings suggest that proteinuria occurring after the lordotic posture may be characterized by an increased glomerular permeability.
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PMID:Quantitative determination of urinary protein components of children with postural proteinuria. 635 21

Human blood-borne monocytes were cultured for up to 22 days on disposable Teflon foils. Within 8 days, these monocytes developed into mature macrophages. At various stages of differentiation, the cells were recovered from the hydrophobic membrane and were assayed for typical monocyte-macrophage enzymes and morphology, binding of monoclonal antibodies (OKM1, OKla1), Fc and transferrin receptors, phagocytic activity, lysozyme production, and ability to inhibit the growth of an allogeneic tumor target cell line (U937). A significant antitumor activity of mature macrophages was found, which developed along with the differentiation of the monocyte precursor cells. In addition, cytotoxic effector macrophages could be activated by lymphokine-rich medium and synthetic alkyl-lysophospholipids. After density gradient separation, light cells (less than 1.05 and less than 1.06 g/ml) showed enhanced cytotoxicity, whereas cells from the dense fraction (greater than 1.06 g/ml) with low base-line activity could be best activated for cytotoxicity by lymphokines. If monocyte-macrophages are involved in a natural surveillance mechanism, our results may indicate the importance of unimpaired macrophage maturation to generate effective host defense against tumor development.
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PMID:Cytotoxic effector cell function at different stages of human monocyte-macrophage maturation. 635 33

Like all immunoglobulins (Ig), IgA has a double function: recognition of the antigen, situated in the Fab alpha fragments, and effector functions which allow elimination of the antigen (Ag), carried by the Fc alpha fragment. Secretory IgA ( IgAs ) is the principal Ig of external secretions and mucosae and has a different structure and composition from serum IgA. Its external function of protection against various forms of bacterial and viral aggression has been well established. Its general mechanism is "the immune exclusion of antigens" i.e. prevention of the penetration of the Ag into the organism by confining them to external secretions followed by elimination. The elimination of bacteria is facilitated by the immobilization and agglutination by IgA. Sometimes, with the aid of lysozyme, IgAs can be bacteriolytic. Antibacterial IgAs have a bacteriostatic function in synergy with lactoferrin and/or transferrin; they even reduce the bacterial production of siderophores. IgAs can inhibit bacterial adhesion to epithelial cells and can increase their adherence to mucus. The neutralization of viruses by IgA is due to inhibition of the first stage of infection, attachment and intracellular penetration of the virus. The same mechanism is involved in the neutralization of bacterial toxins. IgAs also decrease intestinal absorption of foreign proteins in the diet. It has been reported that antibacterial IgAs can cause certain bacteria to lose a plasmid which determines their infectivity. IgAs are able to protect themselves by neutralizing IgA1-proteases secreted by certain bacteria found on mucosal surfaces. Plasma IgA has a limited internal action compared to IgM or IgG. It is generally accepted that IgA barely activates complement (C) by the classical pathway and minimally opsonizes Ag for mono- and polymorphonuclear phagocytes. Antibacterial IgA are not bactericidal in the presence of complement and do not facilitate the phagocytosis of the bacteria to which they are attached. Certain unfavourable effector functions have even been described, such as a specific inhibition of complement fixation and bacterial lysis by IgM and IgG. Some IgA may non-specifically inhibit neutrophil chemotaxis as well as their bactericidal and phagocytic activities. It is difficult to believe that IgA, the second Ig (in quantity) in human serum, is simply useless or even harmful.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:[Effector mechanisms of IgA]. 637 72

Blood and saliva were collected in the autumn and spring from a group of schoolchildren (39 girls, 35 boys) with a mean age of 11.4 years. Serum immunoglobulin IgG, IgA, IgM and IgE, alpha 1-antitrypsin (A 1-AT), alpha 2 macroglobulin (A 2M), transferrin (TRF), ceruloplasmin (CPL), lysozyme (LYS) and pertussis (PE) antibody levels were determined. Calcium (Ca2+) and total serum protein levels were also determined. Secretory IgA (sIgA) and secretory lysozyme (sLYS) levels were assessed in the saliva. A highly significant drop in Ca2+ levels was found in the spring in boys, while in girls there was only a greater scatter of the values. Mean IgG, IgA and IgM values fell significantly in the spring in both sexes, but IgE levels fell significantly only in boys. PE levels rose significantly in the spring in girls. Among the other proteins, all the values rose in boys, except for TRF, whose levels fell. In girls, LYS and TRF levels rose, but all the other values fell. The coefficients of correlation between Ca2+ and the tested proteins showed a significant relationship only for A 2M and PE in girls and only for the total protein level in boys; in boys, the determination coefficient for sIgA and IgM was over 10%. The results do not testify to the existence of a close relationship between blood Ca2+ levels and Ig and other blood protein levels.
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PMID:Seasonal changes in the relationship of blood calcium levels to immunoglobulins and some of the blood proteins in schoolchildren. 650 75

1. A comparison is made of gel electrophoretic patterns of the "whey" proteins of the milk of red (Macropus rufus) and eastern grey (Macropus giganteus) kangaroos at various stages of lactation. Qualitative and quantitative changes occur with time during the mature phase of lactation of both types. Their onset is related solely to the stage of lactation. "Whey" proteins are isolated and characterised and the nature of protein changes determined for the first time. 2. The anodic electrophoretic pattern is divided into 6 main zones (designated A F in order of decreasing mobility) and 2 cathodic zones (G and H) that are only detected in the milk of M. giganteus. 3. Zones A, B and C are milk specific. Zone B is present throughout lactation in both species and is an alpha-lactalbumin. Zones A and C are present only in late lactation, zone C, usually, but not always, appearing first. Zone A is an alpha-lactalbumin in M. giganteus, but is not an alpha-lactalbumin in M. rufus. Zone C appears to be the same protein in both species and is possibly a beta-lactoglobulin. 4. Zone D is kangaroo serum albumin and zone E is possibly a beta 2-microglobulin. Zone F contains three main iron (III) binding bands whose relative intensity varies with stage of lactation. Their intensity differs from the corresponding blood serum transferrin bands. 5. Zone H of Macropus giganteus is a lysozyme. 6. Lactose is present in the milk, but is not the principal sugar. 7. The significance of the results is discussed.
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PMID:"Whey" proteins of milk of the red (Macropus rufus) and eastern grey (Macropus giganteus) kangaroo. 660 Sep 92

Immune reactions elicited in the sera of individuals exposed to nickel and cobalt were assessed by changes in the concentration of serum immunoglobulins IgG, IgA and IgM and serum proteins alpha 2 macroglobulin (A2M), transferrin (TRF), alpha 1-antitrypsin (A1AT), ceruloplasmin (CPL) and lysozyme (LYS). Examinations were carried out in workers occupationally exposed to Ni (38 individuals) or Co (35 individuals) and in groups of non-occupationally exposed children living in areas with a different degree of air pollution from a nearby source of Ni and Co emissions (one group was made up of 54 exposed children, the other one of 64 "less exposed" children of the same age). Groups of non-exposed controls were represented by a group of 42 male adults matched by age and by a group of 48 children from a non-polluted area. Significantly increased average values were obtained for IgG, IgA and IgM in group of workers exposed to Ni, for IgA in workers exposed to Co and for A1AT, A2M, CPL and LYS in both groups of occupationally exposed adults (p less than 0.001 - p less than 0.005). Among non-occupationally exposed children the group of the most exposed had significantly elevated average values for A2M and A1AT which were higher than those recorded in groups of "less exposed" and control children (p less than 0.02 and p less than 0.05, respectively). The biomedical importance of these findings is discussed in detail.
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PMID:Immuno-biochemical findings in groups of individuals occupationally and non-occupationally exposed to emissions containing nickel and cobalt. 666 71

Selected proteins were quantitated after collecting samples of the tears by using two sampling techniques. Tears from the same individual were collected via absorption by Schirmer filter paper strip from the unanesthetized, inferior, conjunctival sac and were compared with tears collected by a capillary tube (taking care not to touch the conjunctiva), after stimulation of tearing by irritation of the nasal mucosa with ammonia vapor. Tear samples were quantitated immunochemically for two typical lacrimal proteins, lysozyme and lactoferrin, and three typical serum proteins, albumin, transferrin, and IgG. Tear analysis of all constituents were performed on a single sample of tears collected by each method from the same individual. Normal subjects without ocular pain or discomfort comprised a sample of 12 subjects ranging in age from 19 to 57 years and consisting of 9 men and 3 women. Concentrations of lysozyme and lactoferrin in samples collected by either method were not significantly different. In contrast, the concentration of albumin, IgG and transferrin collected by Schirmer filter paper technique was significantly higher (P less than 0.01) than the concentration in tears collected by the capillary tube technique. A highly significant increase in serum proteins was seen when the Schirmer filter paper strip was used to collect tears compared to tears collected without mechanical stimulation of the conjunctiva.
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PMID:The effect of collection technique on tear composition. 669 55

Antisera to aldehyde reductase from fruit-fly (Drosophila melanogaster) and chicken were cross-reacted with aldehyde reductase from several species of insects and birds using the technique of microcomplement fixation. Large differences in immunological distances are evident between species of the Class Insecta and of the Class Aves indicating considerable differences in the amino acid sequences of the aldehyde reductase of these species. Immunological distances for aldehyde reductase between pairs of insect species or bird species when plotted against the immunological distances for transferrin, albumin, lysozyme and alpha-glycerophosphate dehydrogenase for the same pairs of species gave a linear relationship in each case. From these relationships the rate of evolution of aldehyde reductase in terms of a unit evolutionary period (UEP) was calculated to be 12 which agreed favorably with the value previously obtained from compositional comparisons. A UEP of 12 is approximately half that of lactate dehydrogenase and shows that aldehyde reductase is evolving at twice the rate of glycolytic enzymes. This may indicate a relatively non-essential metabolism role for the enzyme.
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PMID:Evolution of aldehyde reductase: an immunological approach to the relatedness of aldehyde reductase from different species. 677 12


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