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)

Rabbit aortic changes were investigated after different sclerogenic diets. A subintimal chondroitin sulfate layer was characterized by toluidine blue metachromatic staining at pH 1--3, CEC value expressed in MgCl2 concentration: 0.4M, hyaluronidase sensitivity. This layer becomes disorganized during plaque formation and partly disaappears. A long-lasting sclerogenic diet, as well as a diet containing several sclerogenic factors, produced an increase of frequency and extension of the media necrosis, calcification, and chondroid metaplasia of the aortic wall. In these lesions, an increase of mucopolysaccharide secretion of modified smooth muscle cells was observed.
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PMID:Histological investigation of aortic wall in experimental sclerosis of rabbits. 14 19

From studies of isolated cartilage proteoglycans in solution it has been inferred that they occur in the tissue as aggregates of high molecular weight which consist of proteoglycan monomers, hyaluronic acid and specific link proteins. The present investigation provides direct evidence for the existence of hyaluronic acid-containing aggregates in vivo, as indicated by the following observations: Treatment of sections of coastal cartilage from newborn rabbits with Streptomyces hyaluronidase led to complete disappearance of the electron dense granules, which have been previously identified as chondroitin sulfate proteglycans, from the extracellular matrix. Similar results were obtained on digestion with leech hyaluronidase which, like the Streptomyces enzyme, specifically degrades hyaluronic acid. Proteoglycan aggregation occurs not only in the extracellular compartment but intracellularly as well, since a portion of the hyaluronidase-senstive, electron dense proteoglycan granules are found in intracellular vesicles. It is concluded that the ability of proteoglycan monomers to form aggregates is a true reflection of the in vivo organization of these molecules and that aggregate formation is an important factor in the maintenance of the normal physiological function of cartilage tissue.
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PMID:Role of hyaluronic acid in the in vivo aggregation of cartilage proteoglycans. 15 Sep 64

The glomerular basement membrane was subjected to digestion with specific enzymes to determine the chemical nature (sialoglycoproteins, collagenous peptides, or glycosaminoglycans) of the anionic sites previously demonstrated in the laminae rarae. Enzyme digestion was carried out both in situ and in vitro. Kidneys were perfused in situ with enzyme solutions followed by perfusion with fixative containing the cationic dye, ruthenium red, to detect the anionic sites. Glomerular basement membranes were isolated by detergent treatment of glomeruli and incubated with enzyme solutions, followed by incubation with cationized ferritin (pI 7.3-7.5) to label the anionic sites. Only highly purified enzymes free of proteolytic activity were used. The findings were the same both in situ and in vitro. The anionic sites were unaffected by treatment with neuraminidase, chondroitinase ABC, and testicular or leech hyaluronidase. However, they could no longer be demonstrated after digestion with crude heparinase, purified heparitinase, or Pronase or after nitrous acid oxidation. The results demonstrate that the sites contain heparan sulfate since they are removed by treatment with heparitinase and by nitrous acid oxidation-procedures specific for heparan sulfate; and that sialoglycoproteins or other glycosaminoglycans do not represent major components of these sites since the latter are not affected by digestion with neuraminidase and other glycosaminoglycan-specific enzymes. Identical findings were obtained on basement membranes in other locations (Bowman's capsule, tubule epithelium, and endothelium of peritubular capillaries). The presence of heparan sulfate in the glomerular basement membrane is discussed in relation to the charge-selective properties of the glomerular filter and in relation to its potential involvement in various types of glomerular injury.
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PMID:Presence of heparan sulfate in the glomerular basement membrane. 15 19

The viscous mucoid fluid that accumulates within syphilitic lesions may be due to breakdown of host tissue during infection, or may be synthesized by Treponema pallidum. Experiments were performed to investigate the acidic mucopolysaccharides that occur at the surface of T. pallidum (Nichols strain). These mucopolysaccharides were demonstrated by reaction with acidified bovine serum albumin and by agglutination with wheat germ agglutinin and soybean agglutinin. The polycations ruthenium red and toluidine blue influenced treponemal survival. Concentrations of both compounds at 200 mug/ml inhibited survival, whereas concentrations at 0.1mug/ml enhanced survival. The mucopolysaccharide concentration within the mucoid fluid that accumulates during intratesticular infection was determined by reaction with acidified bovine serum albumin; it ranged from 10,000 mug/ml to less than 8 mug/ml. The addition of this mucoid fluid to treponemal suspensions resulted in differing effects on T. pallidum survival. Some preparations were inhibitory, and others were stimulatory. Commercial preparations of hyaluronic acid and chondroitin sulfate at 400, 200, 100, and 50 mug/ml were detrimental to treponemal survival. The organisms exhibited pronounced clumping in the presence of the higher concentrations of hyaluronic acid. These clumps of treponemes were comprised of mucopolysaccharides as shown by acidified bovine serum albumin and toluidine blue reactions and by hyaluronidase degradation. Results are discussed in terms of the derivation and potential role of acidic mucopolysaccharides at the surface of T. pallidum.
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PMID:Surface mucopolysaccharides of Treponema pallidum. 15 96

Attempts were made to relate Treponema pallidum to the acidic mucopolysaccharides that occur in vivo within host ground substance and in vitro on the surface of cultured testicular cells. Infected testicular tissue was fixed and processed for transmission electron microscopy in the presence of ruthenium red. The use of this inorganic dye demonstrated the large quantity of mucopolysaccharide within testicular tissue and the intimate association of treponemes with this material. Wheat germ agglutinin and soybean agglutinin agglutinated freshly harvested trypsinized testicular cells and trypsinized cultured cells derived from normal rabbit testes (NRT). When stained with toluidine blue, both cell preparations were metachromatic. Prior treatment of cultured NRT cells with hyaluronidase slightly decreased their sensitivity to agglutination by wheat germ agglutinin and soybean agglutinin. Lectin agglutination, metachromasia, and hyaluronidase susceptibility indicated that freshly harvested testicular cells and NRT cells have surface-associated acidic mucopolysaccharides that are probably hyaluronic acid and chondroitin sulfate. A rabbit erythrocyte "sandwich" technique was devised to show that hyaluronidase removed wheat germ agglutinin receptors from the cultured NRT cells. Prior incubation of NRT cells with hyaluronidase, followed by the addition of T. pallidum, resulted in a reduction in numbers of treponemes attached to the NRT cells. The attachment of T. pallidum appears to be mediated through the acidic mucopolysaccharides on the surface of NRT cells. The findings are discussed in terms of the importance of host ground substance mucopolysaccharide to the syphilitic infective process.
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PMID:Relationship of Treponema pallidum to acidic mucopolysaccharides. 15 97

Commercial testicular hyaluronidase preparations are contaminated by a small amount of protease activity which is partially inhibited by serine-protease inhibitors or pepstatin. These protease inhibitors can be shown by Sepharose gel column chromatography to abolish or reduce hyaluronidase-induced degradation of bovine nasal cartilage proteoglycan subunit without affecting the ability of the enzyme to degrade chondroitin sulfate. In addition, immunodiffusion studies indicate that pretreatment of hyaluronidase with these protease inhibitors reduces or abolishes the ability of the enzyme to produce a second "link-related" immunoprecipitin line upon digestion of link protein-containing proteoglycan fractions. Thus, the enhancement of immune reactivity and the unmasking of an additional antigen noted after digestion of cartilage proteoglycan with testicular hyaluronidase are most likely due to the exposure of additional antigenic sites or the the release of more highly immunoreactive fragments by the contaminant proteases rather than to the action of hyaluronidase itself.
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PMID:The effect of contaminant proteases in testicular hyaluronidase preparations on the immunological properties of bovine nasal cartilage proteoglycan. 15 47

To investigate the dystrophic influence on the characteristics of actin, a method for the isolation of F-actin filaments from the skeletal muscle of small sizes, i.e., less than 0.5 g, was devised. In this method, minced muscle was treated with collagenase and hyaluronidase, and the isolated filaments were washed with adenosine triphosphate (ATP). Upon examination in the sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the ATP-washed filaments showed a protein component identical in mobility to actin in untreated myofibrils or to that prepared by the conventional method. Electron microscopic appearances of the filaments were similar to those of F-actin filaments described in the literature. The dimensions of the filaments were 0.5--2.5 micrometer in length and 60--70 A in diameter. The ability to activate the Mg-adenosine triphosphatase or myosin was found to be Ca2+ independent. In all aspects of the above characteristics, the filaments from leg muscles of 129/Re dydy dystrophic mice and their litter mates were observed to be identical.
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PMID:Isolation of F-actin filaments. Comparison of F-actin filament preparations from normal and dystrophic mouse muscle. 15 92

Urine from normal human adults (11 males, 4 females) was collected for 24 hours in four-hour samples, commencing at 08.00 hours. The urine volume, and concentrations of chondroitin sulfate, heparan sulfate, cetylpyridinium turbidity, and creatinine were measured on every sample. Concentrations and total output of glycosaminoglycans were significantly higher in male urine than in female urine. Chondroitin sulfate total output/four hours showed a significant negative correlation with creatinine concentration in males, but not in females. A testicular hyaluronidase is implicated. No such correlation was observed for heparan sulfate. Glycosaminoglycans are filtered into the urine. Plasma clearances are very low. Heparan sulfate is excreted with a circadian rhythm, as is glycosaminoglycan assayed by cetyl pyridinium turbidity. Peak excretions are at 06.00 and 10.00 hours respectively. Chondroitin sulfate excretion is not rhythmic in the male, perhaps because hyaluronidase activity in the urine complicates the assay. A rhythm may be present in the female.
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PMID:Circadian rhythms and the urinary excretion of acid glycosaminoglycans in normal human adults. 15 86

Glycosaminoglycans were isolated from purified fractions of glomerular basement membranes and partially characterized by chemical analysis and cellulose acetate electrophoresis. Basement membranes were prepared by detergent treatment of rat glomeruli and subjected to digestion with papain and Pronase. Glycosaminoglycans were isolated from the digests by precipitation with cetyl pyridinium chloride and ethanol. Results of cellulose acetate electrophoresis of the isolated glycosaminoglycan fraction revealed the presence of one major and one minor spot. The major spot was identified as heparan sulfate because it comigrated with the heparan sulfate standard and was sensitive to heparinase and to nitrous acid oxidation but insensitive to chondroitinase ABC and to testicular or leech hyaluronidase. The minor spot was tentatively identified as hyaluronic acid based on its migratory behavior and sensitivity to leech and testicular hyaluronidase. The chemical composition of the isolated glycosaminoglycan was typical of that of heparan sulfate (high carbazole/orcinol ratio, high sulfate content, absence of galactosamine). The data support and confirm the cytochemical data obtained previously [Kanwar, Y. S. & Farquhar, M. G. (1979) Proc. Natl. Acad. Sci. USA 76, 1303-1307] demonstrating that heparan sulfate is the only sulfated glycosaminoglycan detectable in the glomerular basement membrane. The present results suggest that in addition to sulfated glycosaminoglycan some nonsulfated glycosaminoglycan (hyaluronic acid) may also be present in the glomerular basement membrane.
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PMID:Isolation of glycosaminoglycans (heparan sulfate) from glomerular basement membranes. 15 57

Urinary acid mucopolysaccharides (AMPS) excretion was investigated in a Japanese case with Multiple Sulfatase Deficiency (MSD) (Mucosulfatidosis). The patient excreted AMPS 4 to 5 times more (as carbazoluronic acid) than controls. The cellulose acetate gel electrophoresis clearly indicated two major AMPS which co-migrated with heparan sulfate and chondroitin sulfate A/C. Enzymic digestion with chondroitinase AC and ABC, and by testicular hyaluronidase plus amino sugar analysis also confirmed that our case excreted heparan sulfate and chondroitin sulfate A/C. These findings suggest that there are heterogeneities of urinary AMPS excretion among cases with MSD.
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PMID:Urinary acid mucopolysaccharides in multiple sulfatase deficiency (mucosulfatidosis). 15 21


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