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 effect of diabetes mellitus on the interdental alveolar bone has been long debated. The present study reported the distribution of glycosaminoglycans (GAG) in normal and diabetic alveolar bone using histochemical techniques. Animals were rendered diabetic and killed at 2, 4, 6 and 9 weeks after injections. Tissues were stained with Alcian blue 8GX dye (pH 2.5) to demonstrate GAG and the intensity of the staining reactions compared with age-matched controls. During the experiment, weights of control animals did not change significantly; weights of diabetic animals were significantly less than initial weights from 0-6 weeks (p less than 0.001), but became nearly equal by 9 weeks. Staining intensity of diabetic bone demonstrated initial decrease (0-4 weeks) followed by a marked increase (4-9 weeks) suggesting an early decline in bone GAG levels followed by increased bone GAG levels as compared to age-matched control and initial levels. Bone GAG levels were significantly different between diabetics and age-matched controls at 2 (p less than 0.005) 4 (p less than 0.001), 6 (p less than 0.001) and 9 (p less than 0.001) weeks after streptozotocin injections. Digestion with chondroitinase AC, ABC and streptomyces hyaluronidase suggested significant differences between control and diabetic bone matrix in the levels of chondroitin 4 and 6 sulfates (p less than 0.05) and hyaluronic acid (p less than 0.001) but not dermatan sulfate. In control and diabetic bone, chondroitin sulfates were located within the bone matrix, dermatan sulfate within bone matrix and Sharpey fiber bundles.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Proteoglycans of alveolar bone of diabetic and non-diabetic mice: a histochemical study. 298 Feb 36

Skin biopsies from patients with pseudoxanthoma elasticum (PXE) were studied by electron microscopy either before or after selective digestions with collagenase, elastase, trypsin, hyaluronidase, chondroitinase AC and ABC, with the aim of identifying an eventual organic component associated with mineralization within the elastin fibers and the chemical nature of the enormous aggregates of filaments very often associated with, but distinct from mineralized elastin fibers. The results obtained, on both embedded thin sections and fresh tissue fragments, showed that elastin fibers, whether mineralized or not, were sensitive only to elastase, and they did not contain significant amounts of materials different from elastin that could be accounted for by ion precipitation; the aggregates of microfilaments in strict connection with altered elastin fibers were mostly sensitive to elastase and hyaluronidase, were partially removed by trypsin and chondroitinase, and were not modified by collagenase, which seems to indicate that the microfilaments consist mainly of abnormally aggregated elastin molecules together with low sulfated proteoglycans. It may be concluded that PXE is a complex genetic disorder of the connective tissue, and that mineralization of elastin is only one of the alterations of the extracellular matrix.
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PMID:Effect of selective enzymatic digestions on skin biopsies from pseudoxanthoma elasticum: an ultrastructural study. 301 57

Methods for the analysis of urinary GAGs that can be used for or are applicable to routine assays are described. The most popular method for isolation of GAGs from a urine sample is CPC precipitation, in spite of the fact that it is time-consuming. To identify the different types of GAGs excreted, separation by one-dimensional cellulose acetate electrophoresis followed by staining with alcian blue or toluidine blue may suffice for routine purposes. Solvents such as barium acetate, calcium acetate, barbital buffer and pyridine-formic acid are used for the separation. However, the separation of the seven types of GAGs by conventional one-dimensional electrophoresis is difficult, and a discontinuous electrophoretic method with barium acetate buffer and barium acetate buffer containing ethanol has proved effective for the separation. HPLC separation methods are used for assaying the profiles of enzymatic digestion products of GAGs. Advanced HPLC methods for separating intact GAGs of different types are currently unavailable. Unsaturated disaccharides produced with heparitinase and/or heparinase from heparan sulphate and oligosaccharides produced by hyaluronidase digestion of hyaluronic acid can be separated by HPLC. For chondroitin sulphate isomers, unsaturated disaccharides produced by digestion of the samples with chondroitinase ABC or chondroitinase AC are separated by HPLC and determined by their UV absorbance or by fluorescence labelling. Highly sensitive quantitation of chondroitin sulphate isomers is possible by these methods, which are also efficient for the investigation of the constituents of GAG polymers. Some of these methods have been applied to urine samples from patients with, e.g., mucopolysaccharidoses.
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PMID:Methods for analysis of urinary glycosaminoglycans. 306 22

Vitreous fibrosis was induced in rabbit eyes by intravitreal injection of erythrocytes. The fibrotic vitreous removed from experimental animals were then incubated with [3H]glucosamine at 37 degrees C for 24 h. The newly synthesized 3H-labeled glycosaminoglycans were isolated by 4 M guanidium hydrochloride extraction followed by pronase digestion. The 3H-labeled glycosaminoglycans were then characterized by gel filtration column chromatography and by specific enzymatic degradation, i.e., hyaluronidase, chondroitinase AC, and/or chondroitinase ABC. The disaccharides derived from chondroitinase ABC degradation were identified by thin-layer chromatography. We previously demonstrated that 91% of the total glycosaminoglycan synthesized by normal vitreous was hyaluronic acid. Our present results indicate that in the fibrotic vitreous, the synthesis of hyaluronic acid was decreased to 26%, whereas the synthesis of chondroitin sulfate increased to 59% of the total newly synthesized glycosaminoglycans. These results suggest that cells present in fibrotic vitreous resemble fibroblasts with respect to their activities in glycosaminoglycans synthesis.
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PMID:Change in the synthesis of glycosaminoglycans by fibrotic vitreous induced by erythrocytes. 308 30

Rabbit annulus fibrosus and nucleus pulposus were analysed for hydroxyproline, chondroitin sulphate, keratan sulphate and dermatan sulphate. Tissue proteoglycans were stained for electron microscopy with Cupromeronic blue, used in the critical electrolyte concentration mode, with and without prior digestion by chondroitinase AC or ABC, hyaluronidase or keratanase. Collagen bands, a-e were demonstrated with UO2++. A chondroitin sulphate proteoglycan was found orthogonally associated with loosely packed collagen fibrils in annulus fibrosus at the d and e bands. The close metabolic and structural analogies with the dermatan sulphate proteoglycans previously shown to be located at collagen d-e bands in tendon, skin, etc. (Scott and Haigh (1985) Biosci. Rep. 5:71-81), are discussed. Tightly packed annulus collagen fibrils were surrounded by axially oriented proteoglycan filaments, mostly without specific locations.
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PMID:Proteoglycan-collagen interactions in intervertebral disc. A chondroitin sulphate proteoglycan associates with collagen fibrils in rabbit annulus fibrosus at the d-e bands. 310 6

Each of the known classes of mammalian glycosaminoglycans, with the exception of keratan sulphate, was found in cerebral cortex samples from patients with Alzheimer-type dementia and age-matched controls. These molecules were quantitated, after electrophoresis and staining with Alcian Blue dye, by scanning densitometry. No significant differences were found between the mean levels of each of the above glycosaminoglycans in frontal cortex from patients with dementia compared with controls. An increase (26%; p less than 0.05) in the mean level of hyaluronate, but not of other glycosaminoglycans, was found in temporal cortex samples. On the other hand, the uronic acid content of hyaluronate degradation products following Streptomyces hyaluronidase treatment of brain glycosaminoglycans did not reveal any statistically significant changes in Alzheimer's disease. HPLC of disaccharide products from Arthrobacter chondroitinase AC digests did not reveal any significant changes in sulphate substitution of chondroitin sulphate in Alzheimer brain.
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PMID:Glycosaminoglycans in cortical autopsy samples from Alzheimer brain. 313 40

Granulosa cells from small or large bovine follicles were pretreated with enzymes that hydrolyze various glycosaminoglycans, and binding of [3H]-heparin to the granulosa was measured. Binding of [3H] heparin increased significantly after enzymatic pretreatments with chondroitinase ABC and fungal hyaluronidase, and similar results were obtained with granulosa from small and large follicles. No changes in binding of [3H] heparin were detected after hydrolyses with chondroitinase AC and heparinase in either follicle size. Heparitinase, which hydrolyzes heparan sulfate, led to a significant 50% increase in binding of [3H] heparin to granulosa from large follicles but was without effect in small follicles. These results suggest that the lower binding of [3H] heparin, which has been reported with follicular enlargement, may be due to heparan sulfate occupying or obstructing binding sites for heparin on granulosa from large follicles.
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PMID:Removal of glycosaminoglycans from bovine granulosa cells contributes to increased binding of hydrogen-3 heparin. 370 Jul 94

The interphotoreceptor matrix (IPM) is a mixture of acidic mucosubstances, which can be demonstrated histochemically with cationic dyes, such as Alcian blue, and metal precipitates, such as colloidal iron. In the normal rat retina, staining of the IPM with these reagents is found predominantly at the apical surface of the retinal pigment epithelium (RPE) and, to a lesser extent, at the junction of the photoreceptor inner and outer segments (basal IS/OS zone). The authors have attempted to characterize the IPM in these two regions using histochemical staining of wax-embedded sections. Prior to staining, the following chemical treatments or enzymatic digestions were performed: neuraminidase (NA), with or without prior deacetylation, mild acid hydrolysis (MAH), testicular hyaluronidase (TH), Streptomyces hyaluronidase (SH), and chondroitinase AC (ChAC). NA alone, deacetylation/NA, and MAH all result in great reduction or total loss of stainable IPM at the RPE apical surface, and only slight or no reduction of stainable IPM in the basal IS/OS zone. Since these procedures remove sialoglycoconjugates, the findings suggest that the IPM concentrated at the apical surface of the RPE is composed in large part of sialoglycoconjugates, that little sialoglycoconjugate is present in the basal zone, and that the sialoglycoconjugates are of a neuraminidase-labile group. SH produces little or no reduction of stainable IPM in either the apical RPE or basal IS/OS zones. TH and ChAC also cause little or no reduction of stainable IPM at the RPE apical surface, but produce a great reduction of stainable IPM in the basal IS/OS zone, leaving a small amount of residual basal material. Since SH digests only hyaluronic acid, and TH and ChAC both digest hyaluronic acid and chondroitin SO4 A and C, the findings suggest that little or no hyaluronic acid is present in either the apical RPE or basal IS/OS zones, and the IPM at the RPE apical surface contains little or no chondroitin SO4 A and C, whereas the stainable IPM in the basal IS/OS zone is composed, at least in large part, of chondroitin SO4 A and C. Predominant basal localization of chondroitin SO4 is further suggested by the staining of this region with Alcian blue at low pH. Sequential digestion with TH/MAH or ChAC/NA produces a complete removal of all stainable IPM, including the TH-insensitive residual basal material. This residual material at the basal IS/OS zone, therefore, appears to be sialoglycoconjugate.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Histochemical demonstration of spatial heterogeneity in the interphotoreceptor matrix of the rat retina. 377 Nov 38

Vitreous fibrosis was induced in rabbit eyes by intravitreal injection of monocytes and lymphocytes. The fibrotic vitreous and normal vitreous removed from experimental animals were then incubated with [3H]-glucosamine at 37 degrees C for 24 hr. The newly synthesized 3H-labeled glycosaminoglycans (GAGs) were isolated by 4 M GuHCl extraction followed by pronase digestion. The 3H-labeled GAGs were then characterized by gel-filtration column chromatography and by specific enzymatic degradation, i.e. hyaluronidase, chondroitinase AC and/or chondroitinase ABC. The disaccahrides derived from chondroitinase ABC degradation were identified by thin-layer chromatography. Our results indicated that 91% of the total glycosaminoglycan synthesized by normal vitreous was hyaluronic acid. In contrast, in the fibrotic vitreous, the synthesis of hyaluronic acid was decreased to 30% whereas the synthesis of chondroitin sulfate increased to 47% of the total newly synthesized glycosaminoglycans. Control vitreous which was injected with freeze-thawed monocytes and lymphocytes synthesized 70% hyaluronic acid and 12% chondroitin sulfate although no fibrosis was observed.
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PMID:Synthesis of chondroitin sulfate by fibrotic vitreous induced by monocytes and lymphocytes. 393 25

In order to localize and characterize proteoglycans in human lung alveoli, we have used the cationic dye Cuprolinic Blue according to the critical electrolyte concentration method. After staining, five types of Cuprolinic Blue-positive filaments become apparent: two types in the basement membranes of type I and type II epithelial cells respectively and lying in one or two layers; one type, more scattered, localized in the basement membrane of the endothelial cells and another kind associated with collagen fibrils and separated from each other according to the main banding period (+/- 60 nm) of these fibrils. Finally, there was a type of filament which was only locally present at a variety of places. The basement membrane filaments were sensitive to heparinase, heparitinase, pronase (without prefixation) and nitrous acid treatment, but not to Streptomyces hyaluronidase, neuraminidase, chondroitinase ABC, chondroitinase AC, pronase (after prefixation) and 2.0 M MgCl2 treatment. The basement membrane filaments, therefore, represent heparan sulphate-containing proteoglycans. On the other hand, the collagen fibril associated filaments were sensitive to treatment with heparinase, chondroitinase ABC and pronase (without prefixation), but insensitive to Streptomyces hyaluronidase, neuraminidase, nitrous acid, heparitinase, chondroitinase AC, pronase (after prefixation) and 2.0 M MgCl2 (after prefixation) treatment. These filaments thus represent iduronic acid-rich dermatan sulphate-containing proteoglycans. Several physiological functions for these proteoglycans are discussed.
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PMID:Ultrastructural localization and characterization of proteoglycans in human lung alveoli. 397 3


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