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)

Biochemical markers of kidney damage were examined in 52 male stainless steel welders (manual metal arc welding) exposed to chromium and nickel. No difference was found in the mean urinary excretion of total proteins, albumin, protein 1, transferrin, retinol-binding protein, lactate dehydrogenase, lysozyme, or beta-N-acetylglucosaminidase in a comparison with matched referents. Beta 2-microglobulin was slightly increased in those welders with a urinary chromium concentration of greater than 64.5 nmol.mmol-1 creatinine. The prevalences of abnormal values did not differ from those observed in the reference group. No correlation was found between the concentrations of chromium or nickel in urine and that of proteins or enzymes. No consistent or clinically significant renal impairment was revealed among the stainless steel welders exposed to a chromium air concentration slightly above the current threshold limit value of the American Conference of Governmental Industrial Hygienists for water-soluble hexavalent chromium compounds (50 micrograms.m-3).
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PMID:Lack of renal changes in stainless steel welders exposed to chromium and nickel. 141 68

Proteins and lipids synthesized by airway secretory cells or transudated are active components in the protection of respiratory epithelium. Proteins and ions are involved in the control of mucus hydration. Secretory proteins, such as secretory immunoglobulin A (IgA), transferrin and lysozyme, participate in the airway antibacterial defence. Other biochemical components found in secretions, such as anti-inflammatory and antioxidant agents as well as antiproteases, contribute significantly to the protection of the underlying epithelium.
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PMID:Functions of proteins and lipids in airway secretions. 157 48

Reduction of disulfide bonds is a key step in antigen processing both to allow the unfolding of protein antigens, increasing the access of proteolytic processing enzymes, and to expose free Cys residues within linear peptide epitopes recognized by T cells. We show here that reduction and alkylation of Ag (hen egg lysozyme and ribonuclease A) vastly increased their proteolysis (by specific enzymes or lysosomal fractions) and the production of specific immunogenic peptides that bound to class II MHC molecules recognized by T hybridoma cells. We also show that the lysosome is the vesicular compartment that mediates protein disulfide reduction. We coupled [125I]tyrosine to 131I-alpha 2-macroglobulin or [131I] transferrin via a reducible disulfide linker. Removal of [125I]tyrosine from the alpha 2-macroglobulin conjugate was initiated only after 15 to 20 min of uptake by macrophages, suggesting that reduction occurred late in the endocytic pathway. No reduction of transferrin conjugates was seen, indicating that early, recycling endosomes did not contain reducing activity. Subcellular fractionation showed that the disulfide bonds were reduced only in heavy density (lysosome) fractions and remained intact in fractions of light density (endosomes and plasma membrane). These results indicate the importance of lysosomes in the biochemical processing of protein Ag presented to T cells.
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PMID:Reduction of disulfide bonds within lysosomes is a key step in antigen processing. 172 38

Escherichia coli B/SM, strain 1-1, was killed dose dependently by human hereditary C9-deficient serum (C9DHS), which was shown to contain no C9 Ag by an ELISA method. On the other hand, human hereditary C7-deficient serum did not kill the bacteria under similar conditions. The bactericidal activity of C9DHS was inhibited by rabbit anti-C5 antibody but not by murine anti-C9 mAb. The anti-C9 antibody decreased the bactericidal activity of normal human serum (NHS) to the level of that with C9DHS. Sheep anti-human lysozyme antibody did not affect the bactericidal activity of C9DHS or NHS even when added at more than twice the concentration required to block the serum lysozyme activity on Micrococcus luteus. After treatment with C9DHS and washing, surviving Escherichia coli were killed by C9, but not by lysozyme, transferrin, or both. Other strains of E. coli (K12 W3110, C600, and NIHJ) and Salmonella typhimurium (strain NCTC 74), all maintained in the laboratory, were also killed by C9DHS. However, pathogenic strains recently isolated from patients with traveler's diarrhea and some strains of S. typhimurium were resistant to both C9DHS and NHS, at least at the serum concentration tested. A concentration of 0.1 M Tris did not increase the susceptibility of serum-resistant strains of bacteria to C9DHS, but made one strain of S. typhimurium tested susceptible to NHS, but not to C9DHS. These results clearly showed that C9DHS kills bacteria that are sensitive to NHS through activation of C up to the step of C8 in the same way that C9-deficient C serum lyzed sensitized erythrocytes.
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PMID:Bactericidal activity of C9-deficient human serum. 173 Aug 76

A cross-sectional study was conducted to determine whether exposure to hydrocarbons in a shoe factory may produce renal effects that can be detected by determination of the urinary excretion of proteins and enzymes. The study population included 59 women who had been exposed to petroleum naphtha and toluene and 24 age-matched control women. The time-weighted average exposure to petroleum naphtha, toluene and ethylacetate was 1,619,81 and 160 mg/m3, respectively. The integrity of the renal structures or functions was assessed by measuring the urinary excretion of total protein, beta 2-microglobulin, retinol-binding protein, albumin, transferrin, lysozyme, lactate dehydrogenase and beta-N-acetylglucosaminidase (NAG). The only parameter that was significantly influenced by hydrocarbon exposure was the urinary activity of beta-N-acetylglucosaminidase. Although the health significance of this renal change, which was not accompanied by changes in the urinary excretion of low- or high-molecular-weight proteins, is unclear, the results of the present study are in agreement with our previous observations suggesting that long-term moderate exposure to solvents does not entail a significant risk for the development of nephrotoxicity.
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PMID:Urinary excretion of proteins and enzymes in workers exposed to hydrocarbons in a shoe factory. 176 14

Polymorphonuclear leukocytes (PMN) exposed to highly purified human lactoferrin (from colostrum) exhibit an increased random motility (at least 2.5-fold) and are primed to produce more superoxide [12.1 +/- 1.2 nmol O2-/min/10(6) PMN preincubated with lactoferrin (0.5 mg/ml) against 6.4 +/- 2.3 with cells without lactoferrin after FMLP stimulation]. The action of lactoferrin seemed to be specific, because it could be abolished by simultaneous addition of antilactoferrin antibody. Addition of transferrin and iron salts to PMN was without effect. Between iron-poor and iron-saturated lactoferrin there was no difference in influence on PMN function except for a higher FMLP stimulated superoxide production by iron-saturated lactoferrin. Aggregation, degranulation (beta-glucuronidase, lysozyme), and bacterial killing were not influenced by lactoferrin. Incubation of monocytes and monocyte-derived macrophages with lactoferrin did not alter their motility or their superoxide production rates. Our findings indicate that PMN become more effective after exposure to lactoferrin by having a greater motility and producing superoxide at a faster rate.
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PMID:Influence of lactoferrin on the function of human polymorphonuclear leukocytes and monocytes. 184 51

Antigen processing involves endocytosis, proteolysis and denaturation of antigens to generate peptides that bind to major histocompatibility complex class II molecules (Ia) in a complex recognized by CD4+ T cells. Ia and antigen are internalized and processed intracellularly, but the exact subcellular site of antigen degradation and formation of the Ia-peptide complex remains unclear. The present studies utilized low-temperature incubation in an attempt to functionally block certain steps in the processing of the antigen hen egg white lysozyme (HEL) by peritoneal exudate cells (PEC) and TA3 B lymphoma cells. Ia endocytosis and uptake of HEL by PEC persisted at 18 degrees C, albeit at somewhat slower rates, but delivery of ligands to lysosomes was blocked. Under these conditions HEL catabolism and antigen processing were effectively blocked, although enough catabolism and antigen processing were effectively blocked, although enough HEL was internalized at 18 degrees C to provide effective presentation during a subsequent incubation at 37 degrees C. In TA3 cells transferrin endocytosis and recycling were notably slowed at 18 degrees C, and iron uptake from transferrin by TA3 cells was completely blocked, indicating that certain specifically endosomal functions were inhibited at 18 degrees C. Thus, intracellular steps in antigen processing were blocked at 18 degrees C, corresponding to deficits in endosomal processing and targeting. These results demonstrate that antigen endocytosis and certain temperature-sensitive endosomal and lysosomal processes are essential for antigen processing.
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PMID:Low-temperature inhibition of antigen processing and iron uptake from transferrin: deficits in endosome functions at 18 degrees C. 196 38

Tear samples were collected from 1 eye of each of 40 cows, 27 sheep, 5 goats, and 5 human beings. Additionally, 10 bovine tear samples were pooled and concentrated. Spectrophotometric assays, using Micrococcus lysodeikticus, were performed on each sample to detect lysozyme activity expressed in hen egg lysozyme (HEL) equivalents. Lysozyme activity was not detected in tears of cows, but 158.8 +/- 159.3 mg of HEL/ml was detected in tears of sheep, 220.7 +/- 37.5 mg of HEL/ml in tears of goats, and 216.3 +/- 86.2 mg of HEL/ml in tears of human beings. In pooled bovine tear samples, lysozyme activity was not detected on plate assay and lysozyme protein was not detected on polyacrylamide gel electrophoresis, column chromatography, or immunoelectrophoresis with rabbit anti-bovine tear antibodies. On the basis of these observations, we concluded that the basic ocular protective mechanism in bovine tears is not lysozyme. Other anti-bacterial proteins such as lactoferrin, transferrin, complement, or beta-lysin may, therefore, be of primary importance in protecting the bovine eye.
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PMID:Lysozyme concentrations in the tears of cattle, goats, and sheep. 202 Dec 61

The levels of 13 proteins were measured in six tear samples collected atraumatically at progressively increasing flow rate from nonstimulated (less than 0.5 microliter/min) to highly stimulated (greater than 50 microliters/min) in ten subjects. Tears were fractionated initially by size-exclusion high-performance liquid chromatography (SE-HPLC). Enzyme-linked immunosorbent assays and kinetic assays were then applied to relevant SE-HPLC fractions to determine specific protein levels. Nine of the 13 proteins assayed showed significantly higher concentrations in nonstimulated tears than in any other tear sample. Immunoglobulin (Ig) M, secretory IgA, polymeric IgA1, and polymeric IgA2 all decreased progressively in concentration from nonstimulated tears to the higher flow-rate stimulated samples. The level of IgG, albumin, and transferrin showed a large drop in concentration between nonstimulated tears and the first (lowest flow-rate) stimulated sample, with relatively little decrease for any subsequent sample. Levels of lactoferrin, tear-specific prealbumin, lysozyme, and peroxidase were relatively constant throughout the series of tear samples. These results indicate that the mechanisms responsible for changes in concentration of constitutive, serum-derived, and regulated tear proteins with stimulus can be studied successfully using noninvasive methods to collect human tears. They also show that simply distinguishing between nonstimulated and stimulated tears is not sufficient to completely characterize the effect of stimulus conditions on tear protein composition.
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PMID:Changes in human tear protein levels with progressively increasing stimulus. 207 41

Histochemical and immunohistochemical studies have been reported in only a few cases of sinus histiocytosis with massive lymphadenopathy (SHML) to date. These indicate that SHML cells belong to the macrophage/histiocyte family, but their exact origin is still unknown. We determined the antigenic phenotype of SHML cells in sections from 20 cases of routinely fixed, paraffin-embedded tissue and from two cases of fresh frozen tissue using a broad panel of antibodies to macrophage/histocyte, B-, and T-cell antigens. SHML cells expressed the following: (1) S-100 protein, (2) "pan-macrophage" antigens such as EBM11, HAM 56, and Leu-M3, (3) antigens functionally associated with phagocytosis (Fc receptor for IgG, complement receptor 3), and lysosomal activity (lysozyme, alpha 1-antichymotrypsin, and alpha 1-antitrypsyn), (4) antigens associated with early inflammation (Mac-387, 27E10), (5) antigens commonly found on monocytes, but not tissue macrophages (OKM5, Leu-M1), and (6) "activation" antigens (Ki-1 and receptors for transferrin and interleukin 2). These data suggest that SHML cells are true functionally activated macrophages that may be recently derived from circulating monocytes.
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PMID:Immunophenotypic characterization of sinus histiocytosis with massive lymphadenopathy (Rosai-Dorfman disease). 218 14


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