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)

Spontaneous equine pulmonary granular cell tumors were diagnosed in six mature horses at slaughter. These tumors were grossly recognized as multiple (5/6) or single (1/6) creamy white, firm nodules. The tumors, located adjacent to bronchi and bronchioles, often invaded airways, resulting in partial to complete occlusion of the lumina. Neoplastic cells were rounded to polyhedral with numerous eosinophilic cytoplasmic granules that reacted uniformly positive with S-100 and neuron-specific enolase antibodies and multifocally with glial fibrillary acidic protein antibodies. These cells were negative for muscle-specific actin, lysozyme, cytokeratin, chromogranin A, and myelin basic protein antigens and did not stain with silver by the Grimelius technique. Uniformly blue-green and scattered pink intracytoplasmic granules were evident with luxol fast blue and periodic acid-Schiff counterstain for myelin and myelin breakdown products. Histochemical and immunohistochemical staining results of these tumors suggest that they are composed primarily of myelinating Schwann cells with lesser numbers of scattered nonmyelinating Schwann cells. The morphologic features of the equine pulmonary granular cell tumors are strikingly similar to those of endobronchial granular cell tumors of human beings.
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PMID:Spontaneous equine pulmonary granular cell tumors: morphologic, histochemical, and immunohistochemical characterization. 777 Oct 48

A 47-year-old man was admitted with appendicitis, and appendectomy was performed. On microscopic examination of the resected specimen, the presence of goblet cell carcinoid in the tip of appendix was revealed. This tumor showed an aggressive nature with perineural and vascular invasion around the appendiceal serosa. The tumor was composed of two main cell populations: mucin-producing (goblet cell type) and silver-positive cells (endocrine differentiation). Additionally, a few cells were also positive for serotonin and lysozyme, but negative for gastrin and ACTH. These findings suggest that goblet cell carcinoid share some functional and histologic characteristics with carcinoid tumors and adenocarcinomas, although it is a distinct entity.
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PMID:Goblet cell carcinoid of the appendix. 794 43

Hen egg-white lysozyme is known to be fungicidal to blastoconidia of Candida albicans under defined in vitro conditions. This lethal action leads to changes in the layering of cell wall and to plasmolysis, caused by unremitting accumulation of wall-like material between the yeast cell wall and cytoplasmic membrane. Here, several methods were applied on ultrathin sections to define the nature of wall-like material: histochemical staining with periodic acid-thiocarbohydrazide-silver proteinate, periodic acid-alkaline bismuth, and phosphotungstic acid at low pH; the localization of the carbohydrate residues with lectin-gold complex; immunocytochemical staining with monospecific antibodies, factor 1 and 6, which recognized major cell wall antigens. The wall-like material was almost uniformly highlighted with periodic acid-thiocarbohydrazide-silver proteinate, factor 1 antibody, concanavalin A-gold and wheat germ agglutinin-ovomucoid-gold, indicating the presence of mannoproteins and chitin. The serotype A-specific epitope recognized by factor 6 antibody was not detected in the wall-like material, although it was demonstrated in the outer cell wall layers after 2 h of exposure to lysozyme.
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PMID:Muramidase-mediated damage to Candida yeast cells. Histochemical and immunochemical characterization of accumulating wall-like material. 840 34

Lysozyme (muramidase) is capable of direct bacteriolytic action by hydrolyzing glycosidic bonds in bacterial cell walls. Although it is broadly distributed in vertebrate tissues and secretions, the cellular and subcellular localizations of the enzyme are still not well known. The present study examines the distribution of lysozyme expression in the various cell types of LR gold-embedded rat parotid gland, applying a postembedding immunogold-silver staining technique for light microscopy. Simultaneously, a postembedding immunogold method for electron microscopy was used to determine the cellular compartments engaged in the biosynthesis and exocytosis of lysozyme. Silver-amplified immunogold staining for lysozyme demonstrated identical localization in both paraffin and semithin LR-gold sections: in the supranuclear parts of acinar and intercalated duct cells. Staining intensity varied even between adjacent cells. In the electron microscope, immunogold labeling was detected over the cell compartments associated with protein synthesis and exocytosis in acinar and intercalated duct cells. Lysozyme antigenic sites were visible over endoplasmic reticulum and throughout the Golgi apparatus, being intense over the trans-Golgi network, but even stronger in the condensing vacuoles and most prominent over secretory granules in both cell types. The findings provide the first immunocytochemical evidence of the synthesis and secretion of lysozyme in parotid acinar and intercalated duct cells.
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PMID:Lysozyme expression in the rat parotid gland: light and electron microscopic immunogold studies. 920 28

Ultrastructure, lysozyme and glycoconjugate activity in duodenal Paneth cells were observed concurrently in the horse. Paneth cells were seen to uniformly line the base of the equine intestinal glands. The round secretory granules have centrally located electron densities with peripherally located electron lucent halos. Histochemically, the peripheral halo layer was positively stained for carbohydrates by the periodic acid-thiocarbohydrazide-silver protein-physical development (PA-TCH-SP-PD) method and the entire granules reacted positively to the WGA. The central core area reacted with anti-lysozyme. We identified a young (Type I) and an old (Type II) cell population in the same crypt, but we suggest that the observed populations are variations of the same cell type with the varied appearance due to aging of the secretory granules.
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PMID:Fine structural and histochemical study of equine Paneth cells. 959 75

The exposure to light (20 mW/cm2, an incandescence lamp) of weakly alkaline protein solutions which contained silver nitrate and formaldehyde initiated reduction of silver ions with the subsequent generation of colored silver colloids. At light intensities lower than 0.2 mW/cm2 the generation of colored silver colloids was delayed. The rate of silver reduction depended on the protein type and on the light spectral structure. In particular, solutions which contained prealbumin, lysozyme, gamma-globulin, and transferrin were more photosensitive than solutions which contained albumin, pepsin, and beta-amylase. The formation of [Ag(NH3)2]+ complex after an addition of ammonium ions into the solutions preferentially suppressed silver reduction in the dark and under exposure to red light, thus resulting in a significant difference in the time of appearance of colored silver colloids when the solutions were exposed to violet or red light. These findings are promising for the elaboration of selective silver development of proteins in polyacrylamide gels.
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PMID:Effect of light on generation of colored silver colloids in protein solutions. 963 87

Although human labial gland secretions contain serous components such as the bactericidal enzyme, lysozyme, the presence of serous cells in this gland has yet to be clearly visualized under the electron microscope. The present study identifies lysozyme-expressing cells of the labial glands using microwave-fixed, Epon-Araldite-embedded specimens, which showed excellent preservation of both ultrastructural detail and antigenicity for post-embedding immunogold labeling of lysozyme. Ultrastructurally, all of the secretory cells of the glands appeared to be a mucous-type and have a serial maturation relationship, consistent with a previous report by TANDLER et al. (1969a): their secretory granules were electron-lucent and exhibited reactivity for mucus staining by the periodic acid-thiocarbohydrazide-silver proteinate (PA-TCH-SP) method. We classified them into two immature types (I, II) and two mature types (I, II). Their distinctive features were the following: 1) relatively small (0.5-1 microm) secretory granules and well-developed basal rough endoplasmic reticulum for the immature types; 2) larger (1-2 microm) secretory granules and well-developed Golgi apparatus, which showed intense PA-TCH-SP reactivity in the 2-3 trans-cisterns, for the mature types; 3) few secretory granules in the immature type I; and 4) the darkest appearance for the mature type II. Immunogold labeling with anti-lysozyme showed specific labeling of the two immature-type cells, in which gold particles were found mainly over the secretory granules and Golgi apparatus, and moderately over the rough endoplasmic reticulum. In the secretory granules, the labeling was distributed throughout the contents and was present even if they showed strong PA-TCH-SP reactivity; in the Golgi area, it was seen over the stacked cisternae, trans-Golgi networks, and condensing vacuoles. No specific labeling was seen in the mature-type cells or in the duct cells. These immature- and mature-type cells were almost equivalent to the "serous demilune or acinus" and "mucous tubule" cells, respectively, at the light-microscopic level. These results indicate that the traditional "immature mucous-type cells" of the human labial glands produce lysozyme and should be classified as seromucous cells.
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PMID:Immunoelectron microscopic identification of lysozyme-expressing cells in human labial salivary glands. 975 97

This paper describes the immobilization of ten proteins and two low-molecular-weight ligands on mixed self-assembled monolayers (SAMs) of alkanethiolates on gold generated from the tri(ethylene glycol)-terminated thiol 1 (HS(CH2)11(OCH2CH2)3OH) (chi(1) = 1.0-0.0) and the longer, carboxylic acid-terminated thiol2(HS(CH2)11(OCH2-CH2)6OCH2CO2H) (chi(2) = 0.0-1.0). The immobilization was achieved by a two-step procedure: generation of reactive N-hydroxysuccinimidyl esters from the carboxylic acid groups of 2 in the SAM and coupling of these groups with amines on the protein or ligand. Because this method involves a common reactive intermediate that is easily prepared, it provides a convenient method for attaching ligands to SAMs for studies using surface plasmon resonance spectroscopy (and, in principle, other bioanalytical methods that use derivatized SAMs on gold, silver, and other surfaces). These SAMs were resistant to nonspecific adsorption of proteins having a wide range of molecular weights and isoelectric points. The pH of the coupling buffer, the concentration of protein, the ionic strength of the solution of protein, and the molecular weight of the protein all influenced the amount of the protein that was immobilized. For the proteins investigated in detail--carbonic anhydrase and lysozyme--the highest quantities of immobilized proteins were obtained when using a low ionic strength solution at a value of pH approximately one unit below the isoelectric point (pI) of the protein, at a concentration of approximately 0.5 mg mL-1. Comparisons of the kinetic and thermodynamic constants describing binding of carbonic anhydrase and vancomycin to immobilized benzenesulfonamide and N-alpha-Ac-Lys-D-Ala-D-Ala groups, respectively, on mixed SAMs (by methods described in this paper) and in the carboxymethyl dextran matrix of commercially available substrates yielded (for these systems) essentially indistinguishable values of Kd, koff, and kon.
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PMID:A strategy for the generation of surfaces presenting ligands for studies of binding based on an active ester as a common reactive intermediate: a surface plasmon resonance study. 1005 46

The research was planned to study the subcellular distribution of enzymatic secretory products within the secretory structures of the mouse major salivary glands at light and electron microscopy level by immunogold silver stain (IGSS) technique and double-sided post-embedding immunogold binding and silver amplification in order to speculate about their compartmentation. In particular, we experimented the above immunogold labeling approaches to localize the lysozyme and to verify its distribution patterns in relation to another secretion enzyme, alpha-amylase. Co-presence of lysozyme and alpha-amylase was observed in the convoluted granular tubule cells of the submandibular gland and in the demilunar cells of the sublingual gland as well as in the electron-dense regions of the mottled secretory granules in the parotid gland. Exclusive binding patterns of lysozyme were observed in the acinar cells of the submandibular and sublingual glands where alpha-amylase did not occur.
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PMID:Cellular compartmentation of lysozyme and alpha-amylase in the mouse salivary glands. Immunogold approaches at light and electron microscopy level. 1080 51

The chemical content of the secretion of the sheep lacrimal gland was analysed at the light and electron microscope levels by applying histochemical techniques and an ultrastructural histochemical method (periodic acid, thiocarbohydrazide and silver proteinate). Mucosubstance histochemistry demonstrated acidic glycoconjugates, mainly sulphated, in the mucous and seromucous glandular cells and in the apical portion of the cells lining the terminal ducts. Moreover, secretory granules, stained with PA-TCH-SP, showed a different localization of the reaction product. The presence of lysozyme was also found in the glandular serous cells. These histochemical studies demonstrate that the secretion of sheep lacrimal glands is mixed, having serous, mucous and seromucous components, and that an excellent correlation exists between the secretory granule substructure and glycoprotein localization.
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PMID:Complex carbohydrate histochemistry and ultracytochemistry of the sheep lacrimal gland. 1082 Aug 98


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