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)

Fibronectin content was determined in articular cartilage in a spontaneous dog model and in a meniscectomy rabbit model of osteoarthritis. Determination of the fibronectin content of urea extracts of articular cartilage by an enzyme linked immunosorbent assay (ELISA) disclosed that degenerated cartilage contained from 10- to 40-fold more fibronectin than normal cartilage. The finding that cartilage fibronectin content was increased in both animal models suggests that elevated cartilage fibronectin content is a general feature of the osteoarthritic process. Immunoperoxidase studies disclosed that fibronectin was distributed throughout the matrix in hyaluronidase treated normal and osteoarthritic cartilage from both animal models, but quantitative differences in fibronectin were not observed by these techniques.
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PMID:Presence of fibronectin in articular cartilage in two animal models of osteoarthritis. 370 31

Purpura was grossly observable in albino mice 6 to 8 h after the intraperitoneal injection of sterile, deoxyribonuclease-treated, cell-free extracts prepared by sodium deoxycholate-induced lysis, sonic disruption, Parr bomb treatment, autolysis without sodium deoxycholate, or alternate freezing and thawing of washed suspensions of Streptococcus pneumoniae type I. Cell-free extracts obtained from sonically disrupted, heat-killed cells (100 degrees C for 20 min) did not contain purpurogenic activity. The reaction was maximal at approximately 24 h postinjection, started to fade slowly after 24 to 48 h, and usually was not grossly observable by 4 to 6 days postinjection. The purpura-producing principle (PPP) in the cell-free extract was purified by sequential ammonium sulfate precipitation, protamine sulfate precipitation, Sepharose 6B gel filtration, wheat germ lectin-Sepharose 6MB affinity chromatography, ribonuclease and trypsin treatment, and a second Sepharose 6B gel filtration step. The final preparation (i) contained glucosamine (5.6%), muramic acid (8.0%), neutral carbohydrate (12.8%), phosphate (8.0%), orcinol-reactive material (6.0%), and Lowry-reactive material (1.6%), and (ii) was free of detectable amounts of deoxyribonucleic acid, capsular polysaccharide, neuraminidase, cytolysin, and hyaluronidase. The isoelectric point and molecular size of the PPP were approximately pI 3.0 and several million daltons, respectively, and the activity remained in the supernatant fluid after centrifugation for 1 day at 105,000 x g. PPP activity was destroyed by incubation with egg white lysozyme and sodium metaperiodate but was resistant to trypsin, pronase, alpha-amylase, deoxyribonuclease, ribonuclease, alkaline phosphatase, pancreatic lipase, 7% trichloroacetic acid, 6 M urea, autoclaving (121 degrees C) for 30 min, and mild acid and alkali exposure. Our observations indicate that the PPP requires intact beta-1,4-glucosidic linkages for activity and support the working hypothesis that activity is associated with pneumococcal peptidoglycan solubilized by the bacterium's autolysin.
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PMID:Characterization of pneumococcal purpura-producing principle. 624 53

Hyaluronidase has been purified from the venom of the honey bee, Apis mellifera. The purification proved remarkably difficult, requiring a large number of chromatographic steps culminating in the removal of traces of phospholipase A2 with an affinity purified rabbit anti-phospholipase A2 immunosorbent column. The purified enzyme showed a 1143-fold increase in specific activity and was homogeneous. Electrophoresis in polyacrylamide gels (12%) containing sodium dodecyl sulphate (pH 8.9) or urea (pH 2.8) and electrofocusing in polyacrylamide (5%) gave a single band. The final product contained less than 0.1% phospholipase A2 and less than 1.5% acid phosphatase and gave a single line of precipitation against rabbit anti-hyaluronidase but was not precipitated by rabbit anti-phospholipase A2. Previous reports of instability were not confirmed, and we found the enzyme to be highly stable over a wide range of temperature and pH, and to denaturing agents. Purified hyaluronidase was found to be 'sticky' when highly pure and at low concentration, and adhered strongly to Sephadex G-75. The relative molecular mass was estimated at 35 000-37 000 by gel filtration, and at 41 000 by sodium dodecyl sulphate/polyacrylamide gel electrophoresis. A value of 50 000 was obtained by ultracentrifugation assuming a partial specific volume of 0.73 cm3/g. Hyaluronidase was found to be a minor allergen in bee venom allergic patients.
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PMID:The purification and characterisation of hyaluronidase from the venom of the honey bee, Apis mellifera. 669 11

Growth of nontransformed 3T3MIT fibroblasts in media containing 200 mM urea leads to the rapid acquisition of the transformed adhesive phenotype as evidenced by an increased rate of divalent cation-independent cell aggregation. The increased rate of divalent cation-independent cell aggregation of urea treated 3T3MIT cells shares many properties with the high rate of aggregation of transformed cells including a sensitivity to treatment with trypsin or hyaluronidase and a reduction in the presence of exogenously added hyaluronic acid. Reversal of the urea-induced increase in aggregation occurs within 24 hours in the absence of urea and can be blocked by 0.2 micrograms/ml cycloheximide. In the presence of cycloheximide, low rates of aggregation can be restored by the addition of urea-conditioned supernatents. The results of these experiments suggest that the loss of an aggregation-inhibitory activity during growth in media containing 200 mM urea is responsible for the increased rate of divalent cation-independent cell aggregation. After removal of this aggregation-inhibitory activity, the normally lowly adhesive 3T3MIT cells become phenotypically transformed with regards to the rate of divalent cation-independent cell aggregation.
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PMID:Effects of urea treatment on the divalent cation-independent cell aggregation of 3T3MIT fibroblasts. 713 Feb 85

Extraction of rat glomerular basement membrane, purified by osmotic lysis and sequential detergent treatment, with 8 M urea containing protease inhibitors solubilizes protein that is devoid of hydroxyproline and hydroxylysine. This material represents 8-12% of total membrane protein, elutes mainly as two high molecular weight peaks on agarose gel filtration, and is associated with glycosaminoglycans. Isolated rat renal glomeruli incorporate [35S]sulfate into basement membrane from which this non-collagenous 35S-labeled fraction can be subsequently solubilized. The radioactivity incorporated into urea-soluble glomerular basement membrane eluted primarily with the higher molecular weight peak (Mr greater than 250 000). Cellulose acetate electrophoresis after pronase digestion of the urea-soluble fraction revealed glycosaminoglycan that was resistant to digestion with Streptomyces hyaluronidase and chondroitinase ABC, sensitive to nitrous acid treatment, and contained [35S]sulfate. The findings indicate that one of the non-collagenous components of glomerular basement membrane is a proteoglycan containing heparan sulfate.
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PMID:Non-collagen protein and proteoglycan in renal glomerular basement membrane. 731 55

Collagen was isolated from human placenta by pepsin digestion and salt precipitation. This collagen was similar in its electrophoretic mobility and immunological reactivity with monoclonal antibody to form B of type VI collagen in the literature (Trueb B, Schreier T, Bruckner P and Winterhalter K. 1987. Eur. J. Biochem. 166: 699-703). We prepared polyclonal rabbit antiserum against alpha 2 chain of type VI collagen and performed an immunohistochemical study using this polyclonal antibody. It reacted in fat tissue and around vessels and peripheral nerves in normal human skin. To confirm the presence of type VI collagen in fat tissue, we isolated collagen from human subcutaneous tissue. This collagen showed a similar pattern in polyacrylamide gel electrophoresis with that from human placenta and cross-reacted with monoclonal or polyclonal antibody against type VI collagen. By immunohistochemical staining, abundant type VI collagen was observed in the septum of subcutaneous fat tissue in morphea or systemic sclerosis. In the mild hyalinizing areas or after treatment with 6M urea or hyaluronidase in highly hyalinized areas, the staining of type VI collagen increased. These data suggest that the amount of type VI collagen in subcutaneous tissue is involved in the early phases of these fibrosing disorders and that type VI collagen accumulates even more in hyalinizing tissue in late phases of these diseases.
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PMID:Human type VI collagen: purification from human subcutaneous fat tissue and an immunohistochemical study of morphea and systemic sclerosis. 756 Apr 37

Type VI collagen beaded microfibrils were extracted from bovine cornea or pig cartilage by limited collagenase digestion. Depolymerization of the microfibril, without strong denaturing reagents linke guanidinium hydrochloride or urea under mild acidic conditions, led to single tetramers and multiples of two to three. However, hyaluronidase digestion in accordance with a published method (Kielty et al. J. Cell Biol. 118:979-990, 1992) was unsuccessful in depolymerizing type VI collagen microfibrils. Also, repolymerization into microfibrils by incubation with hyaluronan was not observed. We further found no binding of native type VI collagen microfibrils to a hyaluronan-Sepharose column. Although a recombinant fragment comprising alpha 3(VI) domains N9-N2 showed apparent binding to the column, electron microscopy did not give any indication of binding of either type VI collagen or fragment N9-N2 to hyaluronan. The present findings suggest that the role of hyaluronan in polymerization of type VI collagen has been overestimated in previous work.
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PMID:Type VI collagen beaded microfibrils from bovine cornea depolymerize at acidic pH, and depolymerization and polymerization are not influenced by hyaluronan. 779 88

Properties of native and aldehyde dextran-modified hyaluronidase (with surface amino group modification about 98%) were investigated. Optimal endoglycosidase activity of the native enzyme was observed at 0.15 M NaCl and pH 5.5 and electrostatic interactions influenced the enzyme activity. The inhibitory effect of heparin on hyaluronidase activity slightly differed at pH 5.5 (1.5-fold inhibition) and 7.5 (1.2-fold inhibition). Ionic strength of the reaction medium only slightly influenced the effect of heparin. Modification of hyaluronidase with dextran increased hydrophobic interactions and steric hindrance. Conjugation with dextran increased the resistance of hyaluronidase activity to denaturing agents (urea, guanidinium hydrobromide) and extended the optimal conditions for maximal endoglycosidase activity (pH 4.5-6.5, the range of NaCl concentration from 0.1 to 0.3 M). The conjugation also reduced electrostatic effects on the active site of hyaluronidase and efficacy of heparin inhibition. At pH 7.5 the enzyme was almost insensitive to heparin. The resistance of dextran-modified hyaluronidase to heparin points to approaches for subsequent studies of the heparin-binding site of this enzyme and biomedical trial of the stabilized enzyme for the treatment of acute cardiovascular lesions.
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PMID:Resistance of dextran-modified hyaluronidase to inhibition by heparin. 1140 55

Using the death of mice due to the growth of tumor homografts as an end point, the distribution and properties of a tumor homograft-promoting substance(s), the "enhancing substance," were studied. Activity was most largely present in tumor and spleen tissues while that in the liver, kidney, and stomach was relatively slight. Activity was widely distributed in fractions prepared from tumor. Although DNAP and crude RNAP fractions were active, activity could not be associated with either RNA or DNA. The fraction possessing the highest concentration of activity was a residue fraction which was insoluble in water or in dilute or strong saline solutions. Extraction of lyophilized tumor with acetone or 3:1 alcohol:ether reduced, but did not eliminate, activity in the insoluble fraction. However, activity was completely lost after extraction with 80 per cent alcohol at room temperature. Enhancing activity of a tumor fraction was irreversibly lost after exposure for 1 hour to a solution more acid than pH 5 or more alkaline than pH 9. Activity was completely lost after exposure to 50 per cent urea or 90 per cent phenol. Activity was not altered by incubation with trypsin, hyaluronidase, DNAase or the receptor-destroying enzyme of V. cholerae, but it was decreased when trypsin or hyaluronidase was injected with the incubated tumor fraction. Activity was rapidly destroyed by treatment with dilute solutions of sodium periodate at pH 7. Under similar conditions, treatment with KMnO(4) resulted in less extensive destruction of activity while H(2)O(2), K(2)Cr(2)O(7), and NaIO(4) previously inactivated by reaction with glucose had no apparent effect on activity. These results are interpreted as indicating the presence of both carbohydrate and protein in the structure of the activity substance.
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PMID:Studies on a substance that promotes tumor homograft survival (the enhancing substance); its distribution and some properties. 1340 73

We developed a method to extract differentially chondroitin sulfate proteoglycans (CSPGs) that are diffusely present in the central nervous system (CNS) matrix and CSPGs that are present in the condensed matrix of perineuronal nets (PNNs). Adult rat brain was sequentially extracted with Tris-buffered saline (TBS), TBS-containing detergent, 1 m NaCl, and 6 m urea. Extracting tissue sections with these buffers showed that the diffuse and membrane-bound CSPGs were extracted in the first three buffers, but PNN-associated CSPGs remained and were only removed by 6 m urea. Most of the CSPGs were extracted to some degree with all the buffers, with neurocan, brevican, aggrecan, and versican particularly associated with the stable urea-extractable PNNs. The CSPGs in stable complexes only extractable in urea buffer are found from postnatal day 7-14 coinciding with PNN formation. Disaccharide composition analysis indicated a different glycosaminoglycan (GAG) composition for PGs strongly associated with extracellular matrix (ECM). For CS/dermatan sulfate (DS)-GAG the content of nonsulfated, 6-O-sulfated, 2,6-O-disulfated, and 4,6-O-disulfated disaccharides were higher and for heparan sulfate (HS)-GAG, the content of 6-O-sulfated, 2-N-, 6-O-disulfated, 2-O-, 2-N-disulfated, and 2-O-, 2-N-, 6-O-trisulfated disaccharides were higher in urea extract compared with other buffer extracts. Digestions with chondroitinase ABC and hyaluronidase indicated that aggrecan, versican, neurocan, brevican, and phosphacan are retained in PNNs through binding to hyaluronan (HA). A comparison of the brain and spinal cord ECM with respect to CSPGs indicated that the PNNs in both parts of the CNS have the same composition.
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PMID:Composition of perineuronal net extracellular matrix in rat brain: a different disaccharide composition for the net-associated proteoglycans. 1664 27


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