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)

1. Submandibular glands from four species of mammal have been shown to contain a hyaluronidase active at acid pH; glands from dog and cat had a much higher content of this enzyme than has been found in other sources. 2. Product formation from hyaluronate after 24hr. incubation was almost the same as with testicular hyaluronidase, indicating that the enzyme is an endo-poly-beta-hexosaminidase. 3. When submandibular-gland homogenates were fractionated by the scheme developed for liver by de Duve, Pressman, Gianetto, Wattiaux & Appelmans (1955), all the enzymes assayed, except cytochrome c oxidase, were found to occur partly in the soluble fraction and partly in the particulate fractions. Among the particular fractions, the highest specific activity was found in the heavy-mitochondrial fraction for cytochrome c oxidase, in the microsomal fraction for alkaline phosphatase and in the light-mitochondrial fraction for acid phosphatase, beta-N-acetylhexosaminidase and acid-active hyaluronidase. 4. Release of the enzyme activity from the sedimentable fractions occurred in 0.1% Triton X-100 or after high-speed homogenization. 5. Stimulation of dogs by pilocarpine was found to decrease the hyaluronidase content of the submandibular gland by 5% and to cause the occurrence of a corresponding amount of acid-active hyaluronidase in the submandibular saliva. 6. The results are discussed in relation to the subcellular localization of hyaluronidase.
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PMID:Canine submandibular-gland hyaluronidase. Identification and subcellular distribution. 430 7

Smooth muscle cells were dissociated from normal rabbit aorta by incubating the tissue in Hanks' solution containing elastase, collagenase, and hyaluronidase. The isolated cells contained significant amounts of the following acid hydrolases: N-acetyl-beta-glucosaminidase, N-acetyl-beta-galactosaminidase, beta-galactosidase, beta-glucuronidase, alpha-mannosidase, beta-glucosidase, acid phosphatase, and cathepsins C and D. The cells were disrupted and fractionated by isopycnic centrifugation on sucrose density gradients in the Beaufay automatic zonal rotor. Lysosomes with a modal density of 1.16 were identified by the distribution of these acid hydrolases and by the latency of N-acetyl-beta-glucosaminidase and beta-galactosidase. Other particulate enzymes studied in these sucrose gradients included cytochrome oxidase and monoamine oxidase (mitochondria), 5'-nucleotidase and leucyl-beta-naphthylamidase (plasma membrane), and catalase (? peroxisome). This microanalytical subcellular fractionation technique is applicable to the study of milligram quantities of many other tissues, both normal and pathological.
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PMID:Lysosomes of the arterial wall. I. Isolation and subcellular fractionation of cells from normal rabbit aorta. 434 42

The findings are presented of a morphologic, quantitative, cytochemical and cytoenzymologic study of the mononucleated nonlymphoid cells in knee synovial fluids from osteoarthritis and various inflammatory diseases. The morphologic criteria allowed the identification of subtypes, including phagocytic subtypes, among synoviocytic and monocytic cells in the fluids. The quantitative study showed an important afflux of monocytes and a hyperexfoliation of synoviocytes in the inflammatory diseases. In fluids with intermediate cellularity, the ratio of monocytes to synoviocytes allowed the differential cytodiagnosis between osteoarthrosis and arthritis. All monocytic subtypes, especially the phagocytic one, were highly significantly increased in the inflammatory diseases. A lower increase was shown by the synoviocytic subtypes, except the phagocytic one, which was not changed. Giant multinucleated synoviocytes were found in every type of disease and thus do not constitute a cytodiagnostic marker. Alcian blue staining without hyaluronidase treatment showed hyaluronate in only a small percentage of the synoviocytes. Cytoenzymologic study showed that synoviocytes and monocytes were positive for all tested hydrolases (beta glucuronidase, acid phosphatase and alpha naphthyl acetate esterase), with the reactivities always higher in the synoviocytes. The synoviocytes were always negative with peroxidase, so this reaction, although it marks only a minority of the monocytic population, can be used as an extra cytologic criterion for the discrimination of mononucleated cells in synovial fluid. There was no significant quantitative difference at the cellular level between osteoarthrosis and arthritides in the reaction to these four enzymes. The lysosomal enzymatic activity in both monocytic and synoviocytic cells confirmed their heterophagic properties. However, synoviocytic heterophagy seems to be a physiologic process, either little or not affected by inflammatory events. On the other hand, monocytic heterophagy and then the macrophagic transformation of monocytes appears to be a major aspect of intrasynovial inflammatory reactions. The question remains as to why, if a large majority of exfoliated synoviocytes comes from type A synovial-lining cells and if they belong to mononuclear phagocytic system, do they so weakly, or not at all, participate as phagocytes in the inflammatory reaction.
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PMID:Morphologic, quantitative and cytoenzymologic studies of synoviocytic and monocytic cells in synovial fluid. 609 67

The immune response to honey bee venom in thirty-seven bee keepers' sera was studied by several methods. Specific IgE antibody levels studied by RAST were generally low, whereas specific IgG antibody levels studied by a Sepharose protein A technique were high. Crossed radioimmunoelectrophoresis was applied for a detailed analysis of the antibody specificities towards the different components of venom in seventeen of the bee keepers' sera. Significant amounts of IgG antibodies were found towards most bee-venom components. The highest IgG response was directed towards phospholipase A. Hyaluronidase, acid phosphatase and two uncharacterized antigens also showed distinct IgG binding. The IgG binding to melittin was low. The IgE binding to the bee venom components was low and primarily directed to the phospholipase. IgE binding to hyaluronidase and acid phosphatase occurred, but was also in very small amounts. One bee-keeper serum caused heavy radiostaining to melittin but the others did not show IgE binding to this component. Thus a low IgE but a high IgG response was demonstrated in bee keepers. The major immunogen was phospholipase A, which is known to be the major allergen in bee venom. Generally, the strongest IgG responses were found to the components capable of inducing the strongest IgE responses.
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PMID:Bee keepers' IgG and IgE antibody responses to bee venom studied by means of crossed radioimmunoelectrophoresis. 620 90

Glycosaminoglycan polysulfate (GAGPS = Arteparon) is used for the treatment of degenerative joint diseases; it inhibits enzymes that dissociate ground substance, e.g. hyaluronidase, beta-glucuronidase, and acid phosphatase. In turn, an improved synthesis of hyaluronate from the synovial lining cells to hyaluronic acid increases viscosity (Verbruggen and Veys 1977). From January 1975 to December 1979, in the Orthopedic Division of the Clinic "St. Elizabeth" in Saarlouis, West-Germany, we treated 754 patients with a total of approximately 8000 intra-articular injections of Arteparon. The problem with drugs influencing the metabolism of joint cartilage is that the results cannot - for obvious reasons - be as conspicuous as e.g. with corticoid injections, although the latter sometimes involve also marked side-effects. After several courses of therapy, on the other hand, the cartilage-protective effect of Arteparon becomes apparent, with an effect lasting for several months. The indications to include the patients into our study were: arthrosis and other cartilage disorders that had been diagnosed prior to onset of therapy by means of either X-ray, surgery, arthrography etc. Therapeutic results were measured by the parameters: subsidence of pain, recession of edema, improved joint motion, etc. Arteparon, applied intra-articularly, was well tolerated; local irritation, and swelling of the treated joints were reported in only 4.7% of the treated cases; the therapeutic overall result was good. Occasionally, a case of headache was observed, however, no case of joint infection was reported.
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PMID:[Clinical studies of intra-articular injections of Arteparon. Retrospective study following the treatment of 754 patients]. 621 39

Young rats, fed a low calcium and vitamin D deficient diet for 2 weeks, developed hypocalcemia, an increased activity of serum alkaline phosphatase and an increase in the serum concentration of immunoreactive parathyroid hormone. An increased activity of lactate dehydrogenase and cytochrome oxidase in odontoblasts was found. No shift in the general energy metabolic pathway was found as visualized in the lactate dehydrogenase iso-enzyme pattern. The dominating lactate dehydrogenase isoenzyme in odontoblasts from both the normal and the deficient rats was LDH 1 (H4, LD5), thus indicating primarily an aerobic energy-metabolism Also the activities of the lysosomal enzymes acid phosphatase, cathepsin D and hyaluronidase in the odontoblasts from the deficient animals were increased when compared to the normal animals. No significant change could be demonstrated for beta-glucuronidase and beta-N-acetylglucosaminidase. It was earlier found that this deficient diet caused an increase in odontoblast alkaline phosphatase activities and protein synthesis in vitro. In view of the present findings it might be concluded that the low calcium and vitamin D deficient diet causes a general increase in the odontoblast metabolism. It is not known whether this is due to the increase in parathyroid hormone or if it is a direct effect of the lowered serum calcium concentration.
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PMID:Odontoblast metabolism in rats deficient in vitamin D and calcium. IV. Lysosomal and energy metabolic enzymes. 625 18

The effect of in vitro capacitation (events that occur before the acrosome reaction) on the acrosomal enzymes of human spermatozoa was determined. Capacitation of human spermatozoa was assessed by their ability to penetrate denuded hamster oocytes. The activities of a number of enzymes commonly associated with the sperm acrosome, including nonzymogen acrosin, proacrosin, inhibitor-bound acrosin, hyaluronidase, acid phosphatase, beta-glucuronidase, beta-glucosidase, beta-N-acetylglucosaminidase, beta-galactosidase and beta-N-acetylgalactosaminidase were assessed. With the exception of acid phosphatase, no alteration in enzyme activity occurred after 4 h of incubating the spermatozoa under capacitation conditions although gamete fusion took place. The acid phosphatase levels decreased twofold, presumably due to the loss of seminal (prostatic acid phosphatase that loosely adheres to spermatozoa. After 8 h of capacitation, a large decrease in sperm enzyme levels took place only in the case of hyaluronidase, although small decreases were also noted in total acrosin, proacrosin and inhibited acrosin. No new electrophoretically migrating forms of acrosin were observed. Decreases in total acrosin and proacrosin, but not in inhibited acrosin, also occurred when spermatozoa were incubated under noncapacitating conditions for 8 h, indicating that capacitation may specifically cause the release of some acrosin inhibitor from human spermatozoa. It is concluded that, with the possible exception of hyaluronidase, the in vitro capacitation of human spermatozoa does not cause a major change in its acrosomal enzyme content so that these hydrolases are fully present before the acrosome reaction takes place during gamete fusion. Serum albumin appears to protect against the loss of some of these enzymes since the activity of several glycosidases was significantly reduced when the spermatozoa were incubated for 8 h in human serum albumin-free medium.
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PMID:Acrosomal enzymes of human spermatozoa before and after in vitro capacitation. 640 71

IgE antibodies to purified proteins and peptides from honeybee venom have been measured by the RAST. Trace amounts (less than 0.1%) of the major venom protein phospholipase A2 (PLA2) grossly distorted the measurement of IgE antibody to the other venom proteins, acid phosphatase (Acid P) and hyaluronidase (HYAL), and overemphasized their importance. Reduction of antigen coupled to the cellulose paper discs, which were used in the assay, diluted out the contaminating PLA2 without apparent loss in sensitivity. The reduction of disc-bound antigen increased the competition between IgE and IgG antibodies but did not affect measurement of IgE antibodies in sera taken from 35 untreated patients who had a history of general allergic reactions to bee stings. In 54% of sera from bee venom--allergic patients, the greatest IgE antibody response was to PLA2. In all, IgE antibodies to PLA2 were present in 91% of these sera. IgE antibodies to Acid P, HYAL, or melittin were present in 60%, 51%, and 31% of sera, respectively, and accounted for the highest level of binding in 17%, 17%, and 6% of these. Only 6% of sera were positive for whole venom but negative for the isolated antigens. A low level of IgE antibody was found to peptide 401 in 6% of sera. No IgE antibodies were found to apamin. While confirming the central role played by PLA2 in bee sting allergy, these results show that other venom components are also important in some patients.
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PMID:Antibodies to purified bee venom proteins and peptides. I. Development of a highly specific RAST for bee venom antigens and its application to bee sting allergy. 660 72

Antibodies to individual bee venom antigens were studied in detail in nine bee sting-allergic patients who received venom immunotherapy without side effects, in two patients who failed to reach maintenance, and in two whose sensitivity returned. The study was confined to patients who had IgE antibodies to at least one of four purified bee venom antigens at the start of treatment. IgE and IgG antibodies to phospholipase A2 (PLA2), hyaluronidase (HYAL), and acid phosphatase (ACID P) and IgE antibodies to melittin (MEL) were measured, and changes in the antibody levels were followed during bee venom immunotherapy. Two contrasting patterns of antibody response were seen in the nine successfully treated patients. In five patients there was a rise in serum IgG antibodies to the same antigens as the IgE antibodies. In two patients' serum IgE antibody to HYAL or ACID P fell without a marked IgG antibody response to these antigens, although high levels of IgG antibody to PLA2 were present in both. Although the first pattern is consistent with a "blocking" role for IgG antibody, clearly the second is not. Not all patients can be conveniently divided into these two categories, and two patients did not show any significant change in either IgG or IgE antibody but were nevertheless able to tolerate the maintenance dose of 100 micrograms of venom. Two patients who failed to reach the maintenance dose of 100 micrograms because of their allergic reactions to the injections of venom were distinguished by (1) very high serum IgE antibody and (2) a low ratio of IgG/IgE antibody. Passive immunization with IgG antibody from a hyperimmune beekeeper was, however, protective in these patients, although it did not raise their overall serum IgG antibody level very much. We are unable to explain either the failure of conventional therapy or the beneficial effect of passive immunization in these two patients. Two bee sting--allergic beekeepers lost their sensitivity to stings, but later, when their sera contained IgE antibody to another bee venom antigen, they reacted to stings and inhalation of beehive dander. These data suggest that either falling IgE antibody or IgG- "blocking" antibody could be responsible for providing clinical protection to bee venom--allergic subjects. Renewed clinical sensitivity was observed when the IgE response was modulated, with patients making IgE antibody first to one antigen and then to another.
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PMID:Antibodies to purified bee venom proteins and peptides. II. A detailed study of changes in IgE and IgG antibodies to individual bee venom antigens. 661 52

Experiments with immobilized concanavalin A strongly suggest a glycoprotein nature of three honey-bee venom enzymes, phospholipase A2, hyaluronidase and acid phosphatase. The electrophoretically and chromatographically detectable heterogeneity of phospholipase A2 results from absence of carbohydrate in a subfraction. Mannose, fucose and N-acetylglucosamine, but not galactose nor N-acetylgalactosamine, are present in the con A-binding fraction of bee venom. It is therefore concluded that only N-glycosidically linked carbohydrate occurs in bee venom glycoproteins.
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PMID:The glycoprotein nature of phospholipase A2, hyaluronidase and acid phosphatase from honey-bee venom. 665 11


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