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)

When grown on mesenchyme-fibroblastoid monolayers made of 16-day-old embryos, lymphokine-activated killer (LAK) cells in clones derived from nude mouse lymph node cells are signaled to synthesize and secrete two mucoid masses. The first is made of chondroitin sulfate, as determined by the degradation of 35S- and [3H]glucosamine-labeled macromolecules in the extracellular matrix, by hyaluronidase, and by chondroitin sulfate lyase AC. This determination correlates with the distinctive blue staining by periodic acid-Schiff/alcian blue (PAS-Ab) at pH 1.0. In the present study, two different masses were identified when methanol-fixed and dried LAK cells and their secretions were examined prior to staining. The chondroitin-sulfate-containing mass appeared as an optically bright structure. It also produced a positive fluorescence with rabbit anti-mouse perforin. The second structure, which appeared as a flowing material or as filling holes in the first, could be identified by its high optical density. However, it was not stained by PAS-Ab and was not blackened by osmium tetroxide. The biochemical nature of the second mass has yet to be determined. Both masses seemed eventually to mix, producing pools, in lacunae, or to spread into the culture space.
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PMID:Secretion of two different flowing masses by lymphokine-activated killer cells. 843 61

The structural organization of integral and associated components of the ciliary zonule is still not fully understood. The present study is to localize and characterize the proteoglycans associated with the ciliary zonule of the rat eye by Cuprolinic blue (CB) staining and immunocytochemistry. After CB staining, the proteoglycans appeared as electron dense elongated rodlets and were localized with the zonular fibers. They were seen lying on the periphery of the zonular fibers or along the length of the individual fibrils. Most of the CB rodlets had a size of 60-170 nm long (average 130 nm) and 25 nm wide. Smaller CB rodlets measuring 25-60 nm long (average 45 nm) and 12 nm wide were sometimes found associated with the individual zonular fibrils. The CB rodlets were removed after chondroitinase ABC or chondroitinase AC treatment, but were resistant to heparitinase, nitrous acid, keratanase or Streptomyces hyaluronidase digestions. The ciliary zonule was also immunostained with three monoclonal antibodies: 2-B-6 specific for chondroitin 4-sulfate, 3-B-3 for chondroitin 6-sulfate and 1-B-5 for unsulfated chondroitin, using indirect immunoperoxidase or immuno-colloidal gold methods. The zonular fibers were immunoperoxidase stained and immunogold labeled by 2-B-6, but were not reactive to 3-B-3 and 1-B-5. The results demonstrate that chondroitin sulfate proteoglycan is associated with the ciliary zonule of the rat eye.
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PMID:Proteoglycans associated with the ciliary zonule of the rat eye: a histochemical and immunocytochemical study. 857 87

We have investigated the potential association of proteoglycans with intact fibrillin-containing microfibrils from foetal bovine elastic tissues and with newly synthesised fibrillin in human and bovine cell cultures. Microfibril integrity was disrupted by chondroitinase ABC lyase and chondroitinase AC lyase, but not by keratanase or hyaluronidase. Following chondroitinase treatment, beads were disrupted but the underlying fibrillar scaffold appeared intact. Cuprolinic blue was prominently associated with beaded domains at a critical electrolyte concentration. Electron-dense rods were often associated with cuprolinic blue-treated microfibrils isolated from fixed tissues. Positive staining revealed charged foci at the beads. Newly synthesised fibrillin could be labelled with 35S TransLabel, [3H]glucosamine or 35SO4 but its electrophoretic mobility was not influenced by treatment with chondroitinase ABC or AC lyase. A diffuse 35SO4-labelled chondroitinase-sensitive component with a resistant band (Mr 35000) co-immunoprecipitated with fibrillin. These experiments indicate that chondroitin sulphate proteoglycans associate with fibrillin and contribute to microfibril assembly. This association has major implications for microfibril function in health and disease.
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PMID:Fibrillin: evidence that chondroitin sulphate proteoglycans are components of microfibrils and associate with newly synthesised monomers. 864 74

Six tetrasaccharide fractions were isolated from shark cartilage chondroitin sulfate D by gel filtration chromatography followed by HPLC on an amine-bound silica column after exhaustive digestion with testicular hyaluronidase. Their structures were determined unambiguously by one- and two-dimensional 500 MHz 1H NMR spectroscopy in conjunction with HPLC analysis of chondroitinase AC-II digests of the tetrasaccharides. One fraction was found to contain two tetrasaccharide components. All of the seven tetrasaccharides shared the common core structure GlcA beta 1-3GalNAc beta 1-4GLcA beta 1-3GalNAc with various sulfation profiles. Four were disulfated comprising of two monosulfated disaccharide units GLcA beta 1-3GalNAc(4-sulfate) and/or GlcA beta 1-3GalNAc(6-sulfate), whereas the other three were hitherto unreported trisulfated tetrasaccharides containing a disulfated disaccharide unit GlcA(2-sulfate)beta 1-3GalNAc(6-sulfate) and a monosulfated disaccharide unit GlcA beta 1-3GalNac(4- or 6-sulfate). These sulfated tetrasaccharides were demonstrated to serve as appropriate acceptor substrates for serum alpha-N-acetylgalactosaminyltransferase, indicating their usefulness as authentic oligosaccharide substrates or probes for the glycobiology of sulfated glycosaminoglycans.
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PMID:Preparation of a series of sulfated tetrasaccharides from shark cartilage chondroitin sulfate D using testicular hyaluronidase and structure determination by 500 MHz 1H NMR spectroscopy. 887 18

We prepared a series of oligosaccharides from king crab cartilage chondroitin sulfate K after exhaustive digestion with testicular hyaluronidase, and determined the structures of four tetrasaccharides and a pentasaccharide by fast atom bombardment mass spectrometry, high performance liquid chromatography analysis of chondroitinase AC-II digests, and 500-MHz 1H NMR spectroscopy. The tetrasaccharides shared the common core structure GlcAbeta1-3GalNAcbeta1-4GlcAbeta1-3GalNAc with various sulfation profiles. One structure was GlcAbeta1-3GalNAc(4S)beta1-4GlcAbeta1-3GalNAc(4S), whereas three of them have the following hitherto unreported structures including a novel glucuronate 3-O-sulfate: GlcA(3S)beta1-3GalNAc(4S)beta1-4GlcAbeta1-3GalNAc(4S), GlcAbeta1-3GalNAc(4S)beta1-4GlcA(3S)beta1-3GalNAc(4S), and GlcA(3S)beta1-3GalNAc(4S)beta1-4GlcA(3S)beta1-3GalNAc(4S), where 3S or 4S represents 3-O- or 4-O-sulfate, respectively. The structure of the pentasaccharide was determined as GlcA(3S)beta1-3GalNAc(4S)beta1-4GlcA(3S)beta1- 3GalNAc(4S)beta1-4GlcA. Chondroitinase ABC digestion of the tetrasaccharides with GlcA(3S) at the internal position destroyed the disaccharide unit containing GlcA(3S) derived from the reducing side and resulted in only the disaccharide unit from the non-reducing side. In contrast, these tetrasaccharides remained totally resistant to chondroitinase AC-II. The results indicated that it is necessary to reevaluate the disaccharide composition of chondroitin sulfate poly- or oligosaccharides purified from various biological sources, since they were usually determined after chondroitinase ABC digestion. It is probable that the structures containing GlcA(3S) would not have been detected.
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PMID:Novel sulfated oligosaccharides containing 3-O-sulfated glucuronic acid from king crab cartilage chondroitin sulfate K. Unexpected degradation by chondroitinase ABC. 890 Jan 54

In this study, we used an in vitro model to test the capacity of tissue transglutaminase to increase the adhesive strength at a cartilage-cartilage interface. Full-thickness cartilage-bone cylinders were prepared from fresh adult bovine shoulder joints, and the superficial half of the hyaline cartilage was then removed to provide a plane surface. Tissue transglutaminase was applied to the freshly cut surface of one cylinder, and a calcium-chloride solution (to act as an activating agent) was applied to that of the other. The cartilage surfaces were immediately apposed, one on top of the other, and an eighty-gram weight was applied to the upper cylinder for ten minutes at 37 degrees Celsius under defined humidity conditions. A measured force was then applied transversely to the upper cylinder until it was displaced from the lower one (which was clamped in a holding device), and the force recorded at this point was taken as a measure of the adhesive strength achieved at the cartilage-cartilage interface. The adhesive strength increased linearly with an increasing concentration of tissue transglutaminase (0.25 to 2.75 milligrams per milliliter) and was enhanced by increasing the duration of incubation, but it was not influenced by the level of humidity. The adhesive strength was improved by as much as 40 per cent when the cartilage surfaces had been pretreated with chondroitinase AC or hyaluronidase to remove glycosaminoglycan chains of proteoglycans, which are largely responsible for the intrinsic anti-adhesive properties of cartilage.
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PMID:A new biological glue for cartilage-cartilage interfaces: tissue transglutaminase. 905 38

Novel sulfated tetrasaccharide structures containing 3-O-sulfated GlcA were isolated recently from king crab cartilage chondroitin sulfate K [Sugahara, K., Tanaka, Y., Yamada, S., Seno, N., Kitagawa, H., Haslam, S. M., Morris, H. R., & Dell, A. (1996) J. Biol. Chem. 271, 26745-26754]. In this study, we prepared a series of oligosaccharides from the same source after exhaustive digestion with testicular hyaluronidase and determined the structures of a pentasaccharide, two hexasaccharides, and two heptasaccharides by means of fast atom bombardment mass spectrometry and 500-MHz 1H-NMR spectroscopy. All the oligosaccharides had the following hitherto unreported structures including a novel glucuronate 3-O-sulfate: GlcA(3S)(beta1-3)GalNAc(4S)(beta1-4)GlcA(3S)(beta1-3)GalNAc( 4S)(beta1-4)GlcA(beta1-3)GalNAc(4S), GlcA(3S)(beta1-3)GalNAc(4S)(beta1-4)GlcA(3S)(beta1-3)GalNAc( 4S)(beta1-4)GlcA(3S)(beta1-3)-GalNAc(4S), GlcA(3S)(beta1-3)GalNAc(4S)(beta1-4)(Fuc alpha1-3)GlcA(beta1-3)GalNAc(4S), GlcA(3S)(beta1-3)-GalNAc(4S)(beta1-4)(Fuc alpha1-3)GlcA(beta1-3)GalNAc(4S)(beta1-4)GlcA(beta1-3)GalNAc (4S), and GlcA(3S)(beta1-3)GalNAc(4S)(beta1-4)GlcA(3S)(beta1-3)GalNAc( 4S)(beta1-4)(Fuc alpha1-3)GlcA(beta1-3)GalNAc(4S), where 3S or 4S represent 3-O- or 4-O-sulfate, respectively. Furthermore, the three latter structures contained a novel combination of both 3-O-sulfated and 3-O-fucosylated GlcA residues. The pentasaccharide with 3-O-fucosylated GlcA at the internal position remained totally resistant to chondroitinase AC-II, whereas it was degraded by chondroitinase ABC into a disaccharide unit containing GlcA(3S) derived from the nonreducing side and a trisaccharide unit containing fucose from the reducing side.
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PMID:A novel pentasaccharide sequence GlcA(3-sulfate)(beta1-3)GalNAc(4-sulfate)(beta1-4)(Fuc alpha1-3)GlcA(beta1-3)GalNAc(4-sulfate) in the oligosaccharides isolated from king crab cartilage chondroitin sulfate K and its differential susceptibility to chondroitinases and hyaluronidase. 909 30

Glycoconjugate modifications were analysed in the zona pellucida during development of oocytes in dog and cat using conventional histochemical staining methods with or without previous carbohydrate digestion. A series of lectins combined with desulphation and sialic acid degradation were applied. No differences were observed between dog and cat follicles using conventional histochemical staining methods. In both species, the zona pellucida and follicular fluid/intercellular matrix strongly reacted with PAS and high iron diamine stain (HID) and reacted moderately with low iron diamine stain (LID). Treatment with testicular hyaluronidase, chondroitinase ABC, chondroitinase AC and chondroitinase B treatment diminished HID and LID positivity of follicular fluid and intercellular matrix. Lectins that gave the most intense staining of the zona pellucida of both species were SBA, PNA, RCA-I, GSA-IB4 and WGA, indicating the presence of beta-D-GalNAc, D-Gal and GlcNAc residues. Sulpho- and asulpho-carbohydrates were identified in terminal and/or subterminal positions linked to sialic acid residues. In conclusion, the results indicate that glycosaminoglycans are not present in the zona pellucida of both species. Differences were observed in carbohydrate residues and in their spatial distribution, depending on species and developmental stage of the follicles. The similarity in lectin affinity between ooplasm and zona pellucida of oocytes present in follicles at different stages of development confirm the involvement of oocytes in zona pellucida production.
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PMID:Glycohistochemical investigation of canine and feline zonae pellucidae of preantral and antral oocytes. 1033 57

The decidual reaction in mice is characterized by the transformation of a specific population of endometrial fibroblasts into epithelioid cells, known as decidual cells. An important feature of decidualization in mice is a remarkable modification of the endometrial extracellular matrix. The present work is an ultrastructural cytochemical study of matrix with the purpose of analyzing the arrangement of collagen-associated proteoglycans (PGs) at various regions of nulliparous endometrium and of the antimesometrial decidua of mice using the cationic dye cuprolinic blue associated with enzymatic treatments with chondroitinase ABC, chondroitinase AC, and hyaluronidase. The staining with cuprolinic blue showed PGs as rods and granules of several sizes. Rods measuring 40-60 nm in length (named F2-rods) were apposed to thin collagen fibrils whereas granules were associated with thick collagen fibrils, particularly in the region occupied by mature decidual cells on the 7th day of pregnancy. The amount of granules was higher than that of F2-rods. Both F2-rods and granules were affected by chondroitinase ABC or AC treatment, indicating that they were PGs containing chondroitin sulfate and dermatan sulfate chains. However, the granules associated with thick collagen fibrils were more resistant to chondroitinase AC treatment than F2-rods, indicating the presence of dermatan sulfate chains that contain both L-iduronic and D-glucuronic acid sugar residues. We suggest that the differences of the nature and amount of PGs may be associated with the changes of the thickness of collagen fibrils observed during decidualization of the endometrium in the mouse.
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PMID:Ultrastructural cytochemical characterization of collagen-associated proteoglycans in the endometrium of mice. 1090 33

Chondroitin Sulfate ABC lyase I from Proteus vulgaris is an endolytic, broad-specificity glycosaminoglycan lyase, which degrades chondroitin, chondroitin-4-sulfate, dermatan sulfate, chondroitin-6-sulfate, and hyaluronan by beta-elimination of 1,4-hexosaminidic bond to unsaturated disaccharides and tetrasaccharides. Its structure revealed three domains. The N-terminal domain has a fold similar to that of carbohydrate-binding domains of xylanases and some lectins, the middle and C-terminal domains are similar to the structures of the two-domain chondroitin lyase AC and bacterial hyaluronidases. Although the middle domain shows a very low level of sequence identity with the catalytic domains of chondroitinase AC and hyaluronidase, the residues implicated in catalysis of the latter enzymes are present in chondroitinase ABC I. The substrate-binding site in chondroitinase ABC I is in a wide-open cleft, consistent with the endolytic action pattern of this enzyme. The tryptophan residues crucial for substrate binding in chondroitinase AC and hyaluronidases are lacking in chondroitinase ABC I. The structure of chondroitinase ABC I provides a framework for probing specific functions of active-site residues for understanding the remarkably broad specificity of this enzyme and perhaps engineering a desired specificity. The electron density map showed clearly that the deposited DNA sequence for residues 495-530 of chondroitin ABC lyase I, the segment containing two putative active-site residues, contains a frame-shift error resulting in an incorrectly translated amino acid sequence.
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PMID:Crystal structure of Proteus vulgaris chondroitin sulfate ABC lyase I at 1.9A resolution. 1270 21


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