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)

Some biological and neurochemical properties of the venom of stonefish (Syanceja horrida) were investigated. The venom exhibited oedema-inducing, haemolytic, hyaluronidase, thrombin-like, alkaline phosphomonoesterase, 5' nucleotidase, acetylcholinesterase, phosphodiesterase, arginine esterase, and arginine amidase activities. Recalcification clotting time, prothrombin, and kaolin-cephalin clotting times were increased 1.7-2.3- and 2.4-fold respectively. The LD50 (i.v. mouse) was 300 micrograms/Kg. Its effects on uptake and stimulation of neurotransmitter synthesis and release were observed in rat brain synaptosomes. In the presence of 100 micrograms venom, uptake of [methyl-3H] choline in rat brain synaptosomes was inhibited 70%, while that of 4-amino-n-[U-14C] butyric acid was inhibited 20%. The toxin also stimulated the release of [3H]-acetylcholine from the synaptosomes.
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PMID:Biological activities of Synanceja horrida (stonefish) venom. 136 68

The venom of the wandering spider Cupiennius salei was analysed biochemically by gel filtration, cation exchange chromatography, RP-HPLC, IEF, SDS-PAGE and TLC-electrophoresis. The native venom contains high levels of Na+, K+, Ca2+, histamine and taurine. It shows considerable activity of hyaluronidase, but not proteolytic activity. Thirteen peptides (CSTX-1 to CSTX-13) with an apparent mol. wt between 2.6 and 12.5 kDa causing differently strong toxic, effects were purified. Toxicity data of the crude venom (insects and mouse) are given and compared with the toxicity of CSTX-1, which causes most of the crude venom's toxicity. CSTX-1 has a mol. wt of 8352.6 and its amino acid sequence of 74 amino acids is given.
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PMID:Purification of toxic peptides and the amino acid sequence of CSTX-1 from the multicomponent venom of Cupiennius salei (Araneae:Ctenidae). 801 51

Pompe disease (glycogen storage disease type II) is a glycogen storage disease caused by a deficiency of the lysosomal enzyme, acid maltase/acid alpha-1,4 glucosidase (GAA). Deficiency of the enzyme leads primarily to intra-lysosomal glycogen accumulation, primarily in cardiac and skeletal muscles, due to the inability of converting glycogen into glucose. Enzyme replacement therapy (ERT) has been applied to replace the deficient enzyme and to restore the lost function. However, enhancing the enzyme activity to the muscle following ERT is relatively insufficient. In order to enhance GAA activity into the muscle in Pompe disease, efficacy of hyaluronidase (hyase) was examined in the heart, quadriceps, diaphragm, kidney, and brain of mouse model of Pompe disease. Administration of hyase 3000 U/mouse (intravenous) i.v. or i.p. (intraperitoneal) and 10 min later recombinant human GAA (rhGAA) 20 mg/kg i.v. showed more GAA activity in hyase i.p. injected mice compared to those mice injected with hyase via i.v. Injection of low dose of hyase (3000 U/mouse) or high dose of hyase (10,000 U/mouse) i.p. and 20 min or 60 min later 20 mg/kg rhGAA i.v. increased GAA activity into the heart, diaphragm, kidney, and quadriceps compared to hyase untreated mice. These studies suggest that hyase enhances penetration of enzyme into the tissues including muscle during ERT and therefore hyase pretreatment may be important in treating Pompe disease.
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PMID:Hyaluronidase increases the biodistribution of acid alpha-1,4 glucosidase in the muscle of Pompe disease mice: an approach to enhance the efficacy of enzyme replacement therapy. 1702 13

The possibility of using hyaluronidase for the regulation of the state of different pools of mesenchymal precursors in vivo was demonstrated. The reaction of mesenchymal precursor cells depended on the dose of the enzyme. Administration of hyaluronidase in a dose of 20 U/mouse increased the content of stromal precursors and mesenchymal stem cells in the bone marrow and promotes mobilization of precursor cells induced by granulocyte CSF. Administration of high dose of hyaluronidase (100 U/mouse) reduced the content of mesenchymal precursors in hemopoietic tissue and abolished granulocyte CSF-induced mobilization of mesenchymal precursor cells of different maturity.
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PMID:Role of hyaluronidase in the regulation of functions of mesenchymal precursor cells. 1821 20

We studied the possibility of modification of hematotropic effects of granulocytic CSF and hyaluronidase. It was found that hyaluronidase in a dose of 20 U/mouse potentiates the specific effect of granulocytic CSF on granulocytopoiesis, while granulocytic CSF potentiates the stimulating effect of the enzyme on the erythroid stem. Functional activity of hemopoiesis precursors, secretion of humoral factors by adherent myelokaryocytes, and serum content of hemopoietins increased under these conditions. Hyaluronidase (100 U/mouse) against the background of treatment with granulocytic CSF leads to uncoupling of proliferation and differentiation of hemopoietic cells and abolishes the mutually activating hematotropic effect of preparations.
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PMID:Effects of granulocyte colony-stimulating factor and hyaluronidase on the formation of blood system reactions. 1911 May 50

We evaluated whether immobilized hyaluronidase can modify the hematotropic effect of immobilized granulocyte CSF (G-CSF). The preparation of immobilized hyaluronidase (50 arb. units per mouse) potentiated the specific effect of immobilized G-CSF on granulomonocytopoiesis. The preparation was shown to facilitate the indirect effect of immobilized G-CSF on hemopoiesis (stimulation of the erythroid and lymphoid hemopoietic stems). These changes were accompanied by an increase in functional activity of hemopoietic precursor cells, secretion of humoral factors by bone marrow myelokaryocytes, and concentration of hemopoietins in the serum.
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PMID:Modulation of the blood-stimulating effect of immobilized granulocyte colony-stimulating factor by immobilized hyaluronidase. 2245 78