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)

The activities of elastase, cathepsin G, lysozyme and myeloperoxidase of polymorphonuclear leukocytes were determined by spectrophotometry in thirty-six patients with psoriatic lesions, twelve symptom-free patients with psoriasis and fifteen normal controls. The mean activities of cathepsin G, elastase and lysozyme were found to be increased by 55 to 70% in patients with actively spreading plaque lesions compared with healthy controls (P less than 0.01). Most patients with guttate lesions had total enzyme activities within the normal range. Those with stationary plaque psoriasis had activities of both neutral proteinases (cathepsin G and elastase) which were about 40% lower than normal controls (P less than 0.05). In the lesion-free psoriatics, the activities of neutral proteinases were about 70% of control values. Our findings emphasize the importance of assessment of disease activity in this sort of investigation. The present data may help to resolve much of the confusion regarding PMN function in psoriasis.
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PMID:Neutral proteinases and other neutrophil enzymes in psoriasis, and their relation to disease activity. 608 73

Culture supernatants obtained from a radiation leukemia virus-transformed, hen egg-white lysozyme (HEL)-specific, suppressor T cell line are able, when injected into mice, to specifically suppress the anti-HEL antibody response. Suppression is observed on both primary and secondary anti-HEL antibody responses evaluated by direct and developed hemolytic plaque assays. Culture supernatants from this HEL-specific suppressor T cell line do not suppress the antibody response induced by a structurally related lysozyme, demonstrating the presence in the culture supernatant of a suppressor factor endowed with fine antigenic specificity. The suppressor factor is able to selectively suppress the anti-HEL antibody response induced by the N-terminal C-terminal peptide of the HEL molecule indicating that the fine specificity of this factor is restricted to an antigenic epitope present in this region of the HEL molecule. The suppressive activity is restricted by genes located within the H-2 complex and analysis of the suppression induced in recombinant mice demonstrates that the interaction between HEL-specific suppressor T cell factor and its cellular target requires identity in the I-J region of the H-2 complex.
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PMID:Fine antigenic specificity and genetic restriction of lysozyme-specific suppressor T cell factor produced by radiation leukemia virus-transformed suppressor T cells. 618 26

The contribution of proteins from saliva and gingival crevicular fluid (GCF) to plaque was determined by comparing extracts of supragingival plaque of unknown age formed on normal teeth with plaque formed on artificial teeth in complete or partial dentures where crevicular fluid is absent. There was a total absence of albumin and a virtual absence of IgG from denture plaque samples, confirming their crevicular origin. The concentration of lactoferrin was much higher than that of lysozyme in all supragingival but not in the denture plaque samples, suggesting that GCF provided more lactoferrin than lysozyme to plaque. Amylase was a component in both denture and supragingival plaque, present in similar amounts in both deposits. Cysteine-containing phosphoproteins from saliva were in low concentration but present in all plaque samples; proline-rich proteins were virtually absent, reflecting the high vulnerability to proteolysis of these proteins. Salivary proteins in plaque extracts do not correspond with their relative concentrations in saliva.
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PMID:Immunochemical study of host proteins in human supragingival compared with denture plaque. 620 85

In the present investigation 11 females of normal constitution were subjected to a standardized fasting diet for 8 days. Three subjects dropped out early during the experimental period. Saliva and blood samples were collected before, during and after the fasting period. Serum analyses were made of some parameters often studied during undernutrition. As expected, values for creatinine and uric acid were increased. Secretion rate, pH, buffer capacity, electrolytes, total protein, carbohydrates, some antibacterial substances, the amount of Streptococcus mutans, total streptococci, and lactobacilli were determined in the saliva samples. The rate of plaque formation was also estimated. The effect of fasting on the measured parameters varied greatly among the individuals. Fasting caused a significant decrease in secretion rate, concentration of phosphate and sialic acid in stimulated whole saliva. There was no significant increase in concentration of any substance measured. The decrease of the ratio of sialic acid to protein indicates a disturbance of glycoprotein synthesis. In resting saliva the activity of a bacteria-aggregating glycoprotein appeared to be unchanged, whereas the decreases in thiocyanate concentration and lysozyme activity were statistically significant. Lactoperoxidase activities did not change significantly. The amount of IgA, IgG, IgM as well as the microbial counts showed no changes. The rate of plaque formation increased during fasting.
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PMID:Studies of the effect of diet on saliva secretion and caries development: the effect of fasting on saliva composition of female subjects. 620 45

The plaque-forming cell (PFC) response to human lysozyme (HUL) is regulated by an Ir gene(s) located within the major histocompatibility complex of the mouse. Mice of H-2a, H-2k, H-2v and H-2r haplotypes respond to HUL, whereas mice with H-2b, H-2d, H-2q, H-2s and H-2u haplotypes fail to generate substantial anti-HUL PFC responses. In contrast, only mice carrying the H-2b and H-2s haplotypes are non-responders to the distantly related hen eggwhite lysozyme (HEL). The major genetic control of the anti-HUL PFC response maps to the I-A subregion of the H-2 complex with perhaps a minor influence by a gene mapping to the right of the I-B subregion. HUL and HEL induce a cross-reactive suppressor cell, directed against a particular determinant found on both lysozymes. Once generated, these antigen-specific suppressor cells can affect the in vitro primary response to either lysozyme conjugated to sheep red blood cells. Despite this overlap, the strain distribution pattern of responsiveness is different for the two lysozymes. In the discussion, this was attributed to the MHC-related failure to process and/or present HEL to the HEL/HUL cross-reactive suppressor T cell in H-2q, d and u strains.
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PMID:Partial overlap of Ir gene-controlled responses to two proteins of limited relatedness: hen egg-white lysozyme and human lysozyme. 644 69

B10 (H-2b) mice are genetic nonresponders to hen egg-white lysozyme (HEL) and the distantly related human lysozyme (HUL). However, anti-HEL or anti-HUL primary antibody responses in vivo or in vitro can be obtained in B10 mice by immunization with the appropriate lysozyme coupled to erythrocytes. T cells able to suppress either anti-lysozyme plaque-forming cells (PFC) response are induced in B10 mice after immunization with HEL-complete Freund's adjuvant (CFA) or HUL-CFA. This cross-reactivity of HEL and HUL in the induction and the expression of suppressive activity is in marked contrast to their very low cross-reactivity at the PFC level. These results suggest that either HEL or HUL can stimulate a suppressor T cell which recognizes a particular epitope present on both lysozymes. Suppressor cells induced by HEL or HUL bear the same predominant idiotype found on the majority of anti-HEL antibodies, and on the small proportion of anti-HUL antibodies cross-reactive with HEL. B10.Q (H-2q) mice are responders in vivo to HEL-CFA, but not to HUL-CFA. In contrast to B10, HEL-CFA priming in B10.Q micr induces helper cells whereas HUL-CFA priming induces suppressor cells. These suppressor cells are cross-reactive with HEL and are fully able to suppress HEL-specific helper cells. The presence of HEL-specific suppressor cell precursors in B10.Q mice which are not activated by HEL, seems to implicate differential choice by the antigen presenting system as a basis for Ir gene control, rather than the absence of a regulatory cell type from the T cell repertoire.
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PMID:Differential major histocompatibility complex-related activation of idiotypic suppressor T cells. Suppressor T cells cross-reactive to two distantly related lysozymes are not induced by one of them. 644 50

A mitogenic component, designated fraction C (Fr C), has been purified from a mutanolysin enzyme digest of Actinomyces cell walls by CM Sephadex C-25 ion-exchange and G-100 gel filtration chromatography. Good mitogenic responses were obtained with Fr C over a broad dose range with peak mitogenesis seen with 500 micrograms/culture. Fraction C (mol. wt. = 35,000-40,000) consists of 75% carbohydrate and 23% protein, is non-dialysable, resistant to heat, lysozyme or protease treatment, and partially sensitive to base, and all mitogenic activity is destroyed by either periodate or acid treatment. Fraction C is a B-cell mitogen since it induced responses in nude (nu/nu) and nu/+ BALB/c spleen cell cultures and purified splenic B-cell cultures, but did not stimulate purified splenic T-cell cultures. Similar mitogenic fractions for B cells have been obtained from cell walls of A. naeslundii and from a human isolate of A. viscosus. Good polyclonal IgM synthesis and plaque-forming cell responses to hapten or erythrocytes were obtained in vitro with the purified cell wall fractions derived from all three Actinomyces strains studied. These results indicate that the Actinomyces cell wall possesses a carbohydrate-rich component which activates B cells and may represent a common determinant of this genus.
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PMID:Lymphoid cell responses to bacterial cell wall components: murine B-cell responses to a purified cell wall moiety of Actinomyces. 660 Dec 94

Using a modification of the protein A plaque assay, human lysozyme-releasing cells were detected as plaque-forming cells (PFC). Blood and bone marrow contained higher numbers of muramidase secretors compared to adenoid and tonsil cell suspensions. Human peripheral blood cell cultures were found to contain cells detected as PFC in the presence of antimuramidase immunoglobulin as a developing agent. Lysozyme-producing cells were also found in human bone marrow cultures. High cell densities and a short culture period were optimal conditions for lysozyme release in bone marrow cell cultures. Addition of the activating ligand lipopolysaccharide directly into the plaque assay altered the number of muramidase-secreting cells.
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PMID:Characterization of human lysozyme (muramidase)-releasing cells. Organ distribution and functional properties as analyzed in a protein A plaque assay. 675 41

Mice carrying the H-2b and H-2s haplotypes are genetically nonresponsive to hen egg-white lysozyme (HEL). Analysis of the anti-HEL response patterns of F1, F2 and backcross progeny showed that responsiveness was dominant and H-2 linked. From plaque-forming cell and serum assays in intra-H-2 recombinant mice, it was established that two I loci were implicated, the possession of either leading to responsiveness to HEL. One of the I genes maps in I-A, and the second in I-C, S or G. While the nonresponse phenotype was determined by the H-2 haplotype, there were codominant non-H-2 genes which contributed to a severe reduction in the level of antibody produced in responder strains. A model is presented attributing the outcome of an encounter with HEL to the regulatory balance of helper and suppressor T cells, which have been activated by different subregions of the major histocompatibility complex.
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PMID:Multiple H-2 and non-H-2 genes controlling the antilysozyme response: alternative gene constellations can lead to responsiveness. 677 80

Samples of human cerebral cortex were obtained from twelve autopsied patients with Alzheimer's disease or "normal" aging. Rabbit or goat anti-human antisera to the following plasma proteins: IgG, F(ab')2, Fc, kappa and lambda light chains, IgM, IgA, fibrinogen, albumin, C3, lysozyme, haptoglobin, macroglobulin, and microglobulin; antibodies to the following intracellular proteins: glial fibrillary acidic (GFA) protein, filamin, actin, non-muscle myosin, tubulin, cholinergic vesicle proteins, and neurofilament (NF) proteins were utilized in the immunoglobulin peroxidase bridge. Amyloid cores of classical or perivascular plaques and dyshoric angiopathy exhibited a strong reaction for intact IgG and for both of its light chains, moderate reactions for lysozyme, fibrinogen, albumin and IgA, and weak reactions for IgM, C3, Fc, F(ab')2, haptoglobin, macroglobulin and microglobulin. Antibodies to all three NF proteins, individually and pooled, stained dyshoric and plaque amyloid, while antibodies to other intracellular proteins did not. The coronae of classical plaques and many primitive plaques stained for GFA, but inconsistently for IgG, both light chains, lysozyme, actin, tubulin, and NF proteins. Affected vessels of three patients with Congophilic angiopathy were reactive for all plasma proteins (especially IgG, fibrinogen, and albumin) and for NF proteins. NF staining in Congophilic blood vessels, although variable, revealed a peripheral or adventitial distribution, whereas plasma proteins tended to be localized in the media of the vessel wall. The distributions of Congo red and NF positivity were often identical. Both NF and Congo red staining was sensitive to oxidation. Isolated NF proteins were Congophilic and capable of displaying apple-green birefringence. A hypothesis concerning the role of NF proteins in senile cerebral amyloid is presented.
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PMID:An immunoperoxidase study of senile cerebral amyloidosis with pathogenetic considerations. 679 14


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