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:3.2.1.36 (hyaluronidase)
4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The specificity of lactoperoxidase-catalyzed iodination for the proteins of the hepatoma tissue culture cell plasma membrane was examined by histochemical, biochemical, and cell fractionation techniques. Light microscope autoradiography of sectioned cells shows the incorporated label to be localized primarily at the periphery of the cell. Most of this label can be released from the cell by trypsin but not by collagenase or hyaluronidase. The label is recovered from the cells as either monoiodotyrosine or diiodotyrosine after hydrolysis of cell extracts with a mixture of proteolytic enzymes. The label co-purifies during cell fractionation with an authentic liver cell plasma membrane marker enzyme, 5'-nucleotidase. Thus, the incorporated iodide is itself a valid marker for those membrane polypeptides having tyrosine residues accessible to the lactoperoxidase. The polypeptide complexity of the purified plasma membrane was examined by high resolution dodecyl sulfate-polyacrylamide gel electrophoresis. At least 50 polypeptides in the membrane are accessible to iodination. These polypeptides probably represent the bulk of the protein mass of the membrane and iodinating them does not affect cell viability, growth rate, or cell function. Labeling experiments with fucose and glucosamine show that at least nine of the iodinated peptides may be glycoproteins.
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PMID:Proteins of the hepatoma tissue culture cell plasma membrane. 0 57

A method is described that uses trypsin digestion combined with collagenase-hyaluronidase which produces a population of gap junction vesicles. The hexagonal lattice of subunits ("connexons") comprising the gapjunctions appears unaltered by various structural criteria and by buoyant density measurements. The gap junction vesciles are closed by either a single or a double profile of nonjunctional "membrane," which presents a smooth, particle-free fracture face. Horseradish peroxidase and cytochrome c studies have revealed that about 20% of the gap junction vesicles are impermeable to proteins 12,000 daltons or larger. The increased purity of the trypsinized junction preparation suggests that one of the disulfide reduction products of the gap-junction principal protein may be a nonjunctional contaminating peptide. The gap junction appears to be composed of a single 18,000-dalton protein, connexin, which may be reduced to a single 9,000-dalton peak. The number of peptides in this reduced peak are still unknown.
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PMID:In vitro formation of gap junction vesicles. 5 58

The fat body lobes of Galleria mellonella are surrounded by basement membrane - a fine granular layer of connective tissue. This membrane has an affinity for ruthernium red. The results obtained after treatment of the fat body with neuraminidase, hyaluronidase, phospholipase C and proteolytic enzymes suggest that glycoproteins and phospholipoproteins are constituents of this basement membrane. The basement membrane also has the ability to bind concanavalin A-peroxidase, which is associated with the presence of mannoside residues.
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PMID:The ultrastructure and ultracytochemistry of the basement membrane of the Galleria mellonella fat body. 13 74

By light microscopy the subdermal nodule of a patient with fibrodysplasia ossificans progressiva (FOP) had a fibromatoid histologic appearance. The cytoplasm of the cells stained strongly for mannose-rich glycoprotein with the concanavalin A-horseradish peroxidase (con A-HRP) method. The tumors also exhibited abundant hyaluronidase-digestible mucopolysaccharide in the interstitium with various basic staining reagents. This material appeared to consist principally of hyaluronic acid or chondroitin sulfate with few or mainly masked sulfate esters. At the ultrastructural level, cells interpreted as the tumor cells in the subdermal nodule from the patient displayed extremely hyperplastic granular reticulum and well-developed Golgi elements and appeared very active in synthesis and secretion of protein. The material in the dilated cisternae of the granular reticulum stained for glycoprotein with the con-A-HRP method. Macrophages which comprised the other main cell type in the nodules commonly contacted the tumor cells and occasionally evidenced engulfment of these cells. The intercellular matrix of the nonossified subdermal nodule exhibited greatly increased mucosubstance and, by electron microscopy, showed an unusual network of dialyzed iron-reactive acid muco-substance in the interstitium.
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PMID:Histochemical and ultrastructural studies in fibrodysplasia ossificans progressiva (myositis ossificans progressiva). 14 Dec 14

Submandibular glands of 4-week-old rats were dissociated by a procedure involving digestions with collagenase and hyaluronidase, chelation with ethylenediaminetetraacetic acid, and mechanical force. The isolated cells were purified by centrifugation in a Ficoli solution and were maintained in culture for 36 hours. On the basis of trypan blue exclusions, about 70 per cent of the dissociated cells were viable. Electron microscopic observations indicated that the isolated acinar cells and intercalated and striated duct cells retained their essential in situ ultrastructural characteristics. During a 36-hour culture period the number of viable cells declined to about 40 per cent, and the various cell types formed mixed aggregates. The ultrastructural features of the intercalated and duct cells changed relatively little, but the acinar cells revealed several structural alterations. These included a decrease in the number of the secretory granules, fusions of the secretory granules, and an increase in the rough surfaced endoplasmic reticulum. In general, the polarity of acinar cells became less distinct. The endogenous peroxidase activity in the acinar cells gradually diminished during the culture. Isoproterenol when added to the cultured cells failed to stimulate the incorporation of radioactive thymidine or the discharge of the secretory material from the acinar cells.
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PMID:Short term culture of dissociated rat submandibular gland cells. 16 89

The possible direct role of inflammatory cells in resistance to Trichinella spiralis was studied by observing the effects of lamina propria cells from the small intestine (LP cells) of immunized rats on various stages of the parasite. Effects produced by physically disrupted cells were compared to those produced by intact cells on worms exposed to phytohemagglutinin or immune serum. LP cells were isolated from the rat intestine by collagenase digestion of everted gut segments that were previously denuded of epithelium by treatment with hyaluronidase. Disrupted cells, but not intact ones, selectively killed T. spiralis juvenile and adult worms in vitro, whereas larvae were unaffected by similar treatment. Attempts to identify the lethal component of disrupted cells led to an evaluation of the enzyme, peroxidase. Mucosal peroxidase is localized in LP cells and its activity increases several-fold during intestinal trichinosis. It is presumed to be myeloperoxidase, a particulate-bound enzyme of myeloid-derived leukocytes that functions as part of a potent antimicrobial system in combination with H2O2 and a halide. Results indicated that the vermicidal component of LP cells was associated with the pellet fraction of disrupted centrifuged LP cells, but was not linked to a peroxidase-H2O2-halide system.
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PMID:Lethality of disrupted intestinal lamina propia cells for Trichinella spiralis in vitro. 17 21

Antibodies to proteoglycan (PG) and glycoprotein of bovine nasal cartilage were conjugated with fluorescein isothiocyanate and with horseradish peroxidase. Hyaluronidase digestion of cartilage tissue-specimens increased the intensity of immune reactions; pronase digestion or extraction with 4 M guanidinium chloride abolished the staining. In the intercellular matrix fine filaments beaded with small granules were seen forming an irregular network. The interstices of the network are filled with collagen fibers linked together by the filaments and granules. In view of the linear conformation of core proteins of PGs and the globular conformation of glycoproteins (link proteins), it may be supposed that the granules and filaments represent these two protein components of PG-aggregates. In chondrocytes a homogeneous staining was recorded in the endoplasmic reticulum, in the juxtanuclear areas and in several smooth-walled vesicles and elongated areas situating subjacent to the cell membrane. In contrast to the extracellular immune reactions, this homogeneous intracellular staining was never enhanced by hyaluronidase digestion. This is interpreted in the sense that conformation changes of molecules secreted, and the aggregation of PGs, occur extracellularly.
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PMID:The localization of proteoglycans and glycoproteins in the hyaline cartilage. 33 74

The objective of this work was to examine changes in a surface component of cells from the chick embryo during morphogenetic migrations of gastrulation. Two electron microscope techniques were used to localize cell-bound wheat germ agglutinin (WGA), a lectin which specifically binds N-acetyl glucosamine residues. One technique involved conjugation of peroxidase to WGA before reaction with the cells; the other technique used glucose oxidase to mark WGA which was already cell-bound. In both cases, binding was revealed using diaminobenzidine. Before formation of the primitive streak, all surfaces of the two-layered embryo bound WGA. After migration of cells through the streak, to form the three-layered embryo, not all cell surfaces bound WGA equally. Epiblast cells generally bound WGA lateral to the primitive streak but not during passage through the streak. Mesenchyme cells, after passage through the streak, bound WGA increasingly as they migrated away from the streak. A WGA-binding matrix was observed in the vicinity of the mesenchyme cells and on the dorsal surface of the endoblast. The ventral surface of the endoblast bound the lectin very poorly. In some instances, a peroxidase reaction product was consistently seen on certain surfaces which was not removable by addition of the simple hapten N-acetyl glucosamine. In these cases, the density of the deposit was lessened by use of diacetyl chitobiose as a hapten. This result, together with the reduction of reaction product following certain hyaluronidase treatments, suggests that WGA may be binding to hyaluronic acid as well as membrane glycoproteins.
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PMID:Ultrastructural localization of wheat germ agglutinin-binding sites on surfaces of chick embryo cells during early differentiation. 37 23

Unencapsulated variants of encapsulated, M-protein-positive group A streptococci are oxygen sensitive and secrete inhibitory concentrations of hydrogen peroxide when grown in aerated broth cultures. The organisms were equally sensitive to hydrogen peroxide, and neither exhibited catalase or peroxidase activity, suggesting that differences in oxygen sensitivity reflect dissimilarity in oxygen uptake. The encapsulated parental culture was found to grow in aggregates that take up oxygen more slowly than unencapsulated, oxygen-sensitive derivatives. Moreover, the latter grow in an unaggregated, homogenous suspension. The enzyme hyaluronidase was able to disrupt aggregates of the encapsulated strain increase the rate that these cells take up oxygen, and cause the accumulation of toxic concentrations of hydrogen peroxide earlier in their growth cycle. The evidence presented shows that the aggregation of streptococcal cells by their hyaluronic acid capsule provides this organism with a novel means to avoid self-destruction by oxygen metabolites--cells are shielded from oxygen. The reduced surface-to-volume ratio and limited diffusion of oxygen into the interior of aggregates are proposed as the protective mechanism.
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PMID:Hyaluronic acid capsule: strategy for oxygen resistance in group A streptococci. 39 98

Smears of washed spermatozoa are treated by an indirect immunocytochemical technique. The first antiserum used is prepared in rabbits against ovine (or bovine) hyaluronidase. A sheep antiserum against rabbit globulin, labeled with fluorescerine or peroxidase, is used at the second reagent. Hyaluronidase is localized in the anterior segment of the sperm acrosomes of ram, bull and other species. The specificity of the immunocytochemical staining is checked by appropriate controls. Anti-hyaluronidase serum adsorbed with the antigen, or normal serum, is used as the first reagent. The spermatozoa are also treated with the labeled antiserum only.
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PMID:[Immunocytochemical localization of hyaluronidase in the spermatozoa of domestic mammals]. 80 70


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