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 interaction of human polymorphonuclear neutrophilic leukocytes (neutrophils) with interleukin-1 (IL-1) resulted in a time- and concentration-dependent, selective, release of azurophil (myeloperoxidase, lysozyme) and specific (lysozyme, vitamin B12-binding protein) granule constituents. Myeloperoxidase (MPO) and lysozyme secretion was markedly attenuated if neutrophils were not exposed to cytochalasin B (CB) prior to contact with IL-1. Degranulation was significantly enhanced in the presence of extracellular calcium. IL-1-elicited granule exocytosis was inhibited by the intracellular calcium antagonist, 8-(N,N-diethylamino)-octyl-(3,4,5-trimethoxy) benzoate hydrochloride (TMB-8), a calmodulin antagonist, trifluoperazine (TFP), and an anion channel blocker, 4,4'-diisothiocyano-2,2'-disulfonic acid stilbene (DIDS). An evaluation of the role of arachidonic acid metabolites in IL-1-induced neutrophil activation revealed a suppressive effect on enzyme release exerted by the lipoxygenase inhibitors, piriprost potassium (6,9,deepoxy-6,9-(phenylimino)-delta 6,8 -prostaglandin I1, U-60,257B) and NDGA (nordihydroguaiaretic acid), and a cyclooxygenase/lipoxygenase inhibitor, ETYA (5,8,11,14-eicosatetraynoic acid). These data describe the characteristics of IL-1 as a human neutrophil secretagogue, and enhance our insight into the mechanism of inflammatory cell activation with this monokine.
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PMID:Interleukin-1 stimulates granule exocytosis from human neutrophils. 242 Jul 32

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

To analyze the nature of cell-cell interactions in chondrogenesis, two cations that influence these interactions, calcium and poly-L-lysine (PL), were tested for their effects on chondrogenesis in vitro. High density cultures of chick limb bud mesenchyme (Hamilton-Hamburger stages 23/24), were exposed to culture media containing calcium (0.6-3.3 mM) or PL (1-10 micrograms/ml). Both cations stimulated chondrogenesis in a dose-dependent manner, and also promoted cartilage formation in normally non-chondrogenic, low cell density cultures. Chondrogenesis was assayed based on cartilage nodule number, [35S]sulfate incorporation, and expression of type II collagen as detected by immunohistochemistry. The calcium effect was not mimicked by other divalent cations (Cd, Co, Ni, Mg, Mn, and Sr). The effect of PL was dependent on its Mr (greater than or equal to 14K) and charge, and was mimicked by poly-D-lysine but not by lysine or other analogs of PL or lysine (epsilon-amino caproic acid, lysozyme, poly-L-arginine, and spermidine). Calcium and PL probably act by different mechanisms since their effects were additive, and required their presence on different days of culture: calcium acted on Day 1, and PL on Day 2. It is proposed that calcium may play a role in the cell aggregation phase of chondrogenesis whereas PL, or a naturally occurring polypeptide of similar nature, may promote chondrogenesis by crosslinking specific anionic components of the cell surface or extracellular matrix.
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PMID:Chondrogenesis of limb bud mesenchyme in vitro: stimulation by cations. 242 99

Protoplasts of S. michiganensis, S. chrysomallus and Streptomyces sp. 26-115, organisms producing actinomycins C and X form in hypertonic salt solution under the action of 3-4,5 mg/ml of lysozyme on the mycelium suspension. For protoplasting, the streptomycetes were grown on the soybean medium in the presence of 0.2-0.8 per cent of glycine. The mycelium of the streptomycete exponential growth phase was more favourable for protoplast formation. Protoplast regeneration was studied on the medium described by Okanishi et al. The quantitative composition of this medium was not optimal for regeneration of protoplasts of the above streptomycetes. The level of their regeneration depended to various extents on concentration of phosphate, magnesium and calcium ions and sucrose in the regeneration medium.
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PMID:[Isolation and regeneration of the protoplasts of the streptomycete producers of actinomycins C and X]. 243 May 19

Sections of primary lung carcinomas, lung metastases, mesotheliomas, and lung metastases of some rare mesenchymal tumors were incubated with different cytokeratin (CK), vimentin, desmin, and tissue polypeptide antigen (TPA) antibodies and with antibodies reactive with different hormones (ACTH, PTH, alpha-HCG, Calcitonin CT), CEA, carcinoma-associated antigen (CA1), secretory component (SC), neuron-specific enolase (NSE), alpha-1-antitrypsin (alpha-1-AT), lysozyme (lyso), and S-100 protein (S 100). CK antibodies derived from a 49 kD (reactive with simple epithelia [SE]) and a 67 kD CK polypeptide fraction (reaction with complex epithelia [CE] were useful differentiation markers for the four major groups of lung carcinomas. In one half of small cell carcinomas a positive reaction with NSE antibodies was found. S 100 and SC were good markers for papillary and bronchioloalveolar adenocarcinomas, whereas CEA was less important because of its reactivity with different types of lung carcinomas. To discern clear cell carcinomas of lung and renal origin a positive reaction with vimentin antibodies (some renal but not lung types) and with CA1 (no renal but all lung types) seemed to be useful. All hormone antibodies were of no importance as markers for difficult differential diagnosis, because positive reactivities were found in cases from every major carcinoma group. In addition, a Ca2+-activated adenosine triphosphatase (ATPase) was found in mesotheliomas but not in papillary adenocarcinomas.
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PMID:Immunohistochemical and histochemical markers of primary lung cancer, lung metastases, and pleural mesotheliomas. 243 80

The influence of proteins on phospholipase A2 was found to depend strongly on the enzyme assay system. We have used three different systems to measure phospholipase A2 which represent the different assay conditions used by a number of previous investigators. Two distinct stimulatory and two distinct inhibitory effects of proteins were observed. (1) A number of proteins - such as albumin, gamma-globulin and lysozyme - were found to inhibit phospholipase A2 activity only at very low substrate concentrations. This 'substrate depletion' was recently proposed as the mode of action for lipocortin. We therefore suggest that substrate depletion is not sufficiently specific to serve as a physiological regulatory mechanism and that the observed inhibition by lipocortin and other proteins more recently reported to mimic it are unlikely to be of physiological significance. (2) Use of liposomes at higher concentrations led to a nonlinear time-course. In this assay system, albumin (and other protein) stimulation can be accounted for as relief of product inhibition. (3) With high concentrations of phospholipids in the presence of cholate (mixed micelles), the behavior of proteins in the assay was complex. The assay time-course appeared linear in the absence of added protein, but at concentrations of added albumin up to 1 mg/ml, stimulation of phospholipase A2 activity was observed. Concentrations greater than this led to diminution of enzyme activity to the original activity. No effect whatever was observed when lysozyme was substituted for albumin. Since this biphasic result was not observed with liposomes, we suggest that the product whose inhibition is being relieved is the lysophosphatidylcholine, and not the free fatty acid. The inhibitory effect at high albumin concentrations is probably the result of removal of free fatty acids from the micelle: fatty acids are known to cause stimulation of phospholipase A2 by providing a negative charge to the lipid/water interface. (4) A different type of phospholipase A2 stimulation was apparent with melittin. This was found to be more specific than generally believed: we found no melittin stimulation of pancreatic phospholipase A2, yet confirmed a several-fold stimulation of bee venom phospholipase A2. We also found that high (millimolar) concentrations of calcium suppressed the melittin stimulation of bee venom phospholipase A2, and that a cationic detergent mimicked the stimulation by melittin. (5) We conclude that the effects of proteins on phospholipase A2 studied here can all be explained by proteins binding to substrate or product rather than enzyme-protein interactions.
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PMID:Mechanism for the inhibitory and stimulatory actions of proteins on the activity of phospholipase A2. 246 72

Stimulated parotid gland secretions collected from 16 patients with juvenile chronic arthritis (JCA) were analysed and the results compared with those obtained from 83 healthy sex-, age-, and socioeconomic status-matched children. Parotid salivary flow rate was measured and the saliva samples were assayed for calcium, phosphorus, potassium, chloride, sodium, urea, lysozyme, amylase and immunoglobulin levels (IgA, Ig, IgM). Our results showed that parotid flow rate (PFR) values in JCA patients were not statistically different from those in healthy controls. However, the mean salivary concentrations of calcium, phosphorus, potassium, lysozyme and IgA were significantly lower in the patients. These data could provide an explanation for the increased incidence of caries and gingivitis observed in JCA.
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PMID:Sialochemistry in juvenile chronic arthritis. 247 7

Chrysotile asbestos permeabilizes the plasma membrane of rabbit polymorphonuclear leukocytes (PMNs) which is evident from the release of the cytoplasmic enzyme lactate dehydrogenase (LDH) from the cell. When Ca2+ is present in the medium exocytosis is observed, evident from the release of the granule associated enzyme lysozyme which is not liberated in the absence of Ca2+. Asbestos-induced enzyme release is inhibited by polyanions or by removal of positive charges on asbestos, and resembles enzyme release induced by synthetic polycations. Pretreatment of PMNs with neuraminidase does not affect the ability of asbestos to induce enzyme release from these cells. Asbestos induces release of glucose from glucose-loaded liposomes, and this effect can be inhibited by the polyanion poly-D-glutamic acid. The results are compatible with the view that positive charges play a decisive role in the interaction between PMNs and asbestos, and that the primary target of asbestos could be the lipid bilayer of the membrane. The interaction results in a permeabilized plasma membrane. When Ca2+ is present in the medium it moves into the cell and causes exocytosis of the granule enzyme lysozyme. Inhibition of cytotoxicity by polyanion may cause a diminished Ca2+-influx and hence inhibition of lysozyme release.
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PMID:The involvement of ionic interactions during asbestos-induced enzyme release from polymorphonuclear leukocytes. 247 90

Two unusual characteristics of some outer membrane proteins of Rhizobium leguminosarum are described. First, most of the major outer membrane proteins could only be visualized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis after lysozyme treatment of the isolated cell envelopes, suggesting a very strong, possibly covalent, interaction of these proteins with the peptidoglycan. These peptidoglycan-associated outer membrane proteins belonged to two distinct groups of immunologically related proteins, groups II and III, as defined by typing with monoclonal antibodies. As members of both groups of proteins could be radioactively labeled by growing cells in the presence of N-[3H]acetylglucosamine, we propose that variation in the apparent molecular weight of the antigens within each group is caused by varying numbers of peptidoglycan subunit residues on only two or three different outer membrane proteins. Second, group III outer membrane proteins, with masses of 35 to 46 kilodaltons, formed oligomers stabilized by divalent cations which resisted complete denaturation in 2% sodium dodecyl sulfate at 100 degrees C. Reconstitution experiments showed that of the divalent cations tested, Ca2+ and, to a lesser extent, Mn2+ and Sr2+ were the best stabilizers.
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PMID:Evidence for divalent cation (Ca2+)-stabilized oligomeric proteins and covalently bound protein-peptidoglycan complexes in the outer membrane of Rhizobium leguminosarum. 250 Apr 20

Treatment of rabbit polymorphonuclear leukocytes (PMNs) with 20 mM sodium fluoride for 10 min, followed by removal of fluoride and addition of Ca2+ results in extensive exocytosis. This is apparent from a strong lysozyme release, together with a slight LDH release. During fluoride-activated Ca2+-dependent exocytosis an increase of indo fluorescence and a strong association of 45Ca with the cells occurs. Different inhibitors inhibit both 45Ca association and lysozyme release. Pretreatment of PMNs with pertussis toxin, or the presence of AI3+ in the medium has little effect on fluoride-activated Ca2+-dependent exocytosis. During pretreatment with fluoride, the ATP level strongly decreases. Exocytosis nevertheless occurs upon addition of Ca2+, indicating that a normal ATP level is not required for exocytosis. The glycogen content of the cell strongly decreases during exposure to Ca2+ after pretreatment with fluoride, but not during pretreatment with fluoride. Breakdown of glycogen and accumulation of 3-phosphoglycerate suggest that glycolysis is blocked at the enolase step, but proceeds as far as that step.
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PMID:Exocytotic enzyme release from rabbit polymorphonuclear leukocytes after treatment with fluoride and calcium. 250 51


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