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)

Lenses of late gestational and postnatal normal-eyed mice were tested for accumulated sulfated materials by using Spicer's high-iron-diamine staining method and also for newly incorporated sulfate autoradiographically following administration of 35SO4 either in vivo or in isolated and organ-cultured lenses. Accumulated and newly incorporated sulfate was observed in all lenses for each age group tested. Discrete regional differences were seen in histochemical staining patterns for sulfate on the lens capsule in specimens of all ages, and distinct laminar zonations were seen in the various regions of the capsule in older specimens. Typically, the anterior and equatorial regions of the capsule demonstrated three histochemically distinct laminar zones while the posterior capsule usually demonstrated two laminar zones. Autoradiographic results indicated that sulfate was indeed being incorporated into these regions, and in the same general pattern as seen with histochemistry. The materials were largely insensitive to testicular hyaluronidase but were preferentially sensitive to nitrous acid digestion, indicating the presence of capsular heparan sulfates. Autoradiographic results from organ-cultured lenses indicated that this tissue itself is a primary source of these materials.
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PMID:Accumulation and distribution of sulfated materials in the maturing mouse lens capsule. 363 45

The distribution of polyanionic glycosaminoglycans (GAGs) in the developing mouse vitreous was studied histologically by P.A.S. reaction, metachromatic staining by toluidin blue at various pH's, alcian blue at pH 0.5 and alcian blue at various pH's, alcian blue at pH 0.5 and alcian blue C.E.C. stainings, modified Hale's method with colloidal iron, and enzymatically with bovine testicular hyaluronidase. A subdivision of the vitreous developmental period into four phases and an early distinction between, the posterior and equatorial vitreous portions are suggested on basis of the results. The early vitreous, during the first developmental phase, exhibits a high content in GAGs. This property gradually vanishes in the posterior part during the second phase of development, while acid GAGs including possibly hyaluronate are present in the equatorial zone. During this second phase, the lens capsule present a strong P.A.S.-reactivity, especially positive in it's posterior part. During the third phase, sulphated GAGs reappear in the posterior vitreous while non-sulphated material remains present in the equatorial zone. During the first two postnatal weeks (fourth developmental phase), acid GAG's disappear in the equatorial part of the vitreous but the maturing zonular fibres display the properties of sulphated GAGs. It is suggested that the histochemical maturation of the secondary vitreous starts around the 16th or 17th fetal day, i.e. much earlier than its morphological differentiation.
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PMID:Histochemical study on glycosaminoglycans in the developing mouse vitreous. 369 24

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

The location of lectin binding sites and of anionic components was studied in the embryonic rat cerebral cortex after the formation of the cortical plate at embryonic day 18. The cortical layers advanced in differentiation, i.e. the sub-plate region and the marginal zone, showed a predominant staining with peroxidase conjugates of wheat germ agglutinin (WGA), peanut agglutinin (PNA), and after immunocytochemical detection of PNA binding sites. This pattern was obtained also with the colloidal iron hydroxide staining method. In contrast to this, the binding of concanavalin A and of succinylated WGA did not reveal a prevalent staining of the sub-plate region and the marginal zone. The further histochemical analysis of the substances responsible for the selective staining of these layers was performed by lipid extractions and by enzymatic treatment of the tissue sections with trypsin, hyaluronidase or neuraminidase prior to the binding of lectins or colloidal iron. The results obtained indicated high concentrations of sialylated galactosylglycoproteins in coexistence with glycosaminoglycans. Electron microscopy was performed with peroxidase conjugates of WGA and PNA. Binding sites of both of the lectins in the sub-plate region and in the marginal zone were located mainly at cell surfaces of the different cellular structures. The most intensive binding of WGA and PNA was detected at the surface membranes and at intracellular material of amoeboid microglial cells and astrocyte-like cell processes. It can be concluded that in distinct brain areas during early differentiation specific glycoproteins in coexistence with glycosaminoglycans are situated at, or associated with cell surfaces in high concentrations. The identical histochemical features previously described in mesenchymal tissues suggest that these glycoconjugates might be related to common morphogenetic processes in which non-neuronal cells of brain and body are specifically involved.
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PMID:Lectin binding sites and anionic components related to differentiation in the prenatal rat cerebral cortex. 384 46

The middle ear effusion specimens were obtained by myringotomy and aspiration from 4 children of 4-7 years old, who had been diagnosed as patients with secretory otitis media on the basis of conductive hearing loss and tympanogram. In cases 1 and 2, their ear fluids were macroscopically serous, while those of cases 3 and 4 were mucous. These ear fluids were digested with pronase and the digests were analyzed by cellulose acetate membrane electrophoresis with alcian blue and high-iron-diamine stainings. All samples were found to contain glycopeptides possibly derived from sulfated mucin-type glycoproteins with small amounts of glycosaminoglycans. The glycoconjugates from cases 3 and 4 were further examined after hyaluronidase and chondroitinase ABC treatments, followed by heparitinase digestion. The resultant glycopeptide fractions appeared to be electrophoretically homogeneous and their chemical compositions suggested that they were typical mucin-type glycopeptides. Furthermore, they contained sulfates. The data suggest that in secretory otitis media, one of the major components of middle ear effusions is sulfated mucin-type glycoprotein.
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PMID:Sulfated glycopeptides from middle ear effusions of secretory otitis media. 407 40

Noninbred Sprague-Dawley rats were maintained on a choline-deficient diet containing 0.05% ethionine. After 10-13 weeks, livers were dispersed with collagenase, lysozyme, collagenase and hyaluronidase. Pronase, or a selected batch of trypsin. The highest yield of cells with histochemically demonstrable gamma-glutamyl transpeptidase (GGT) was obtained with trypsin. After velocity sedimentation in an isokinetic gradient of Ficoll in tissue culture medium, two modal populations of cells with histochemically demonstrable GGT were observed. The first mode contained cells that were morphologically different from hepatocytes and that may be oval cells. The second, more rapidly sedimenting modal population of cells with GGT was morphologically similar to hepatocytes as assessed with Wright's stain; the location of this population in the gradient was the same as the location of cells with the appearance of hepatocytes that lacked iron and that had decreased glucose 6-phosphatase. In multiple experiments, the purest fractions contained 71.7 +/- 3.5% cells (mean +/- SD) with the appearance of hepatocytes with histochemically demonstrable GGT.
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PMID:Separation of two populations of cells with gamma-glutamyl transpeptidase from carcinogen-treated rat liver. 611 83

Proteoglycans (PGs) are closely associated with cartilage calcification. We have examined the hypertrophic zone of rat epiphyseal cartilage, in which calcification is occurring, using the high-iron diamine-thiocarbohydrazide-silver proteinate (HID-TCH-SP) method for sulfated glycosaminoglycans, an immunoferritin method specific for chondroitin sulfate A, and the tannic acid-ferric chloride (TA-Fe) method to stain cartilage matrix granules (MGs) presumed to be PG monomers. HID-TCH-SP produced stain deposits with a diameter of 11.2 +/- 3.2 nm (mean +/- SD; n = 200) in the MGs. However, HID-TCH-SP staining was not discernible in membrane-limited matrix vesicles (MVs). In areas of advanced calcification, partially disrupted MVs and globular bodies (GBs), derived in part from disrupted and/or degenerated MVs, contained a few too many small HID-TCH-SP stain deposits. Further down the epiphyseal cartilage, intact MVs markedly decreased and the GBs, containing many small HID-TCH-SP stain deposits, significantly increased in number. These GBs were found exclusively in the longitudinal septa rather than in the transverse septa. After enzyme digestion with testicular hyaluronidase, small (7.2 +/- 1.2 nm in diameter) stain deposits remained in the MGs and GBs, presumably localized to keratan sulfate. Immunoferritin localizing chondroitin sulfate strongly stained MGs, whereas MVs and GBs lacked staining. TA-Fe staining of glycoconjugates in the GBs demonstrated a striking decrease in the diameter of MGs associated with calcification in the GBs as compared with those in the noncalcifying area around the GBs. These results indicate that the GBs containing needle-like apatite crystals in morphologic preparations represent sites of chondroitin sulfate degradation. Testicular hyaluronidase-resistant sulfated glycosaminoglycans presumed to be keratan sulfate and partially degraded PGs selectively remain within the GBs as a probable requisite for expansion of the initial calcification in MVs.
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PMID:Ultrastructural cytochemistry and immunocytochemistry of proteoglycans associated with epiphyseal cartilage calcification. 613 41

To test the value of Streptomyces hyaluronidase in carbohydrate histochemistry, the effects of digestion with the enzyme on the staining of cartilage and non-cartilaginous tissues by Alcian Blue (AB) pH 1.0, AB pH 2.5, high iron diamine, low iron diamine, aldehyde fuchsin, dialysed iron-ferrocyanide and AB pH 2.5-periods acid-Schiff were studied by light microscopy. The results obtained lead to the conclusion that the Streptomyces enzyme releases not only hyaluronic acid but also chondroitin sulphates and keratan sulphates in cartilage. Since hyaluronic acid is known to be linked to chondroitin sulphate proteoglycans, the enzyme is of limited value in localizing hyaluronic acid in cartilage. However, it is useful in localizing hyaluronic acid in most non-cartilaginous tissues.
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PMID:Effects of Streptomyces hyaluronidase digestion on the histochemical reactions of proteoglycans in cartilage compared with its effects on certain non-cartilaginous tissues. 617 84

The location and chemical composition of anionic sites in Bruch's membrane (BM) were examined using cationic probe molecules demonstrable in electron microscopic preparations and tissue digestion with specific degradative enzymes. Ruthenium red and native lysozyme revealed densities distributed at regular intervals in two major components of BM: the basal laminae of the retinal pigment epithelium (RPE) and choriocapillary endothelium (EN). Staining was not observed with succinylated lysozyme (anionic). Colloidal iron also failed to stain BM components. Following crude heparinase treatment at 43 degrees C (specific for heparan sulfate) anionic sites in the RPE basal lamina were not demonstrable with either ruthenium red or native lysozyme. Sites in the EN basal lamina were not affected. Chondroitinase treatment removed almost all of the ruthenium red-positive material in the EN basal lamina; lysozyme binding here was markedly reduced. No changes were observed in the RPE basal lamina after chondroitinase digestion. There was no morphological evidence for site removal by either neuraminidase or leech hyaluronidase, although a detachment of the RPE from BM often occurred after incubation of eye tissue in the latter. Pronase E removed all stainable material. These findings indicate that anionic sites in BM consist to a large extent of chondroitin sulfates and heparan sulfate.
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PMID:Location and chemical composition of anionic sites in Bruch's membrane of the rat. 617 64

The role of osteoclasts or chondroclasts in degradation and synthesis of complex carbohydrates was investigated using the high iron diamine-thiocarbohydrazide-silver proteinate method (HID-TCH-SP) for sulfated glycoconjugates and the periodate-thiocarbohydrazide-silver proteinate (PA-TCH-SP) method for vicinal glycol-containing glycoconjugates. HID-TCH-SP stained the calcified cartilage matrix, the osteoclast ruffled border, vacuoles and heterophagosomes but not the Golgi apparatus and primary lysosomes. The size and number of HID-TCH-SP stain deposits progressively decreased from the calcified cartilage matrix to the ruffled border (p less than 0.001). Enzyme digestion with testicular hyaluronidase removed most HID-TCH-SP stain deposits averaging 13 nm. in diameter in the extracellular matrix, cytoplasmic vacuoles, and heterophagosomes of osteoclasts. Only sparse stain deposits averaging 8 nm. in diameter and presumed to be keratan sulfate remained in these sites after enzyme digestion. Osteoclast heterophagosomes contained the highest concentration of hyaluronidase-resistant material suggesting delayed degradation of keratan sulfate at this site. PA-TCH-SP strongly stained collagen fibrils in the calcified cartilage matrix. Reactive collagen fibrils were also observed in extracellular channels but only rarely were identifiable collagen fibrils observed in cytoplasmic vacuoles. A progressive decrease in the diameter of PA-TCH-SP reactive collagen fibrils was observed between the calcified cartilage matrix and the ruffled border region (p less than 0.001). PA-TCH-SP stained cisternae of rough endoplasmic reticulum, Golgi saccules, and primary lysosomes consistent with the synthesis and packaging of glycoprotein enzymes at these sites. These results indicate that the dissolution of sulfated glycoconjugates requires osteoclastic engulfment of degraded material and subsequent intracellular digestion, whereas the dissolution of collagen fibrils appears to be completed extracellularly.
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PMID:Extracellular and intracellular digestion of complex carbohydrates by osteoclasts. 617 27


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