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)

Interactions between the epithelial and lymphocytic components of the thymus are required for T cell maturation, yet the molecular bases for these interactions remain elusive. In the development and function of other endodermally derived organs, glycosaminoglycan-containing proteins are known to play a critical role. In contrast, virtually nothing is known about the macromolecules that are major constituents of thymic interstitial spaces. For these reasons, we undertook metabolic labeling studies in vitro with D-(6-3H)glucosamine and 35SO4(-2) to begin to characterize systematically the relative amounts and types of glycosaminoglycans made by enriched subpopulations of cells within the thymus. Hydrocortisone, which depletes the thymus of 90% of its lymphocytes, was used both to enrich for epithelium-derived glycoconjugates and to determine if significant alterations in glycoconjugate metabolism accompany drug-induced premature thymic involution. Results indicate: 1) glycosaminoglycans account for a substantial proportion of the total glycoconjugates synthesized by both thymocytes and epithelium; 2) Glycosaminoglycans show a tissue-specific distribution. Hyaluronic acid is the major glycosaminoglycan synthesized by thymic epithelium, whereas it accounts for less than 15% of the total glycosaminoglycans made by thymocytes; 3) Similar proportions of sulfated glycosaminoglycans are made by thymic epithelium and thymocytes. Chondroitin sulfates predominate (75 to 90%) over heparan sulfates (10 to 25%). Chondroitin sulfates from both nonstimulated thymocytes and epithelium are nearly exclusively sulfated at the 4-position of their N-acetylgalactosamine residues; 4) The major high m.w. glycoconjugate of thymocytes, however, is nonsulfated and is resistant to pronase, hyaluronidase, chondroitinase ABC, nitrous acid, keratanase, and neuraminidase; 5) Although hydrocortisone treatment causes a dramatic inhibitory effect on the incorporation of radioactivity into smaller oligosaccharide side-chains by "cortisone-resistant" thymocytes, the drug exerts negligible effects on the metabolism of glycoconjugates by epithelium. These data, which quantify and categorize the complex arrays of glycoconjugates synthesized by the major cell types of the thymus, establish the necessary foundations for further investigations into the functional roles of these glycoconjugates in thymic epithelium-induced maturation of T lymphocytes.
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PMID:Biosynthesis of glycosaminoglycans by epithelial and lymphocytic components of murine thymus. 660 Nov 42

Experiments with immobilized concanavalin A strongly suggest a glycoprotein nature of three honey-bee venom enzymes, phospholipase A2, hyaluronidase and acid phosphatase. The electrophoretically and chromatographically detectable heterogeneity of phospholipase A2 results from absence of carbohydrate in a subfraction. Mannose, fucose and N-acetylglucosamine, but not galactose nor N-acetylgalactosamine, are present in the con A-binding fraction of bee venom. It is therefore concluded that only N-glycosidically linked carbohydrate occurs in bee venom glycoproteins.
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PMID:The glycoprotein nature of phospholipase A2, hyaluronidase and acid phosphatase from honey-bee venom. 665 11

During the course of a study of elucidate the role of modification of the common polysaccharide-protein linkage structure, GlcA beta 1-3Gal beta 1-3Gal beta 1-4Xyl beta 1-O-Ser, in biosynthetic sorting mechanisms of the different sulfated glycosaminoglycan chains, a novel N-acetylgalactosamine (GalNAc) transferase was discovered in fetal bovine serum. The enzyme catalyzed the transfer of [3H]GalNAc from UDP-[3H]GalNAc to linkage tetrasaccharide and hexasaccharide serines synthesized chemically and to various regular oligosaccharides containing terminal D-glucuronic acid (GlcA), which were prepared from chondroitin and chondroitin sulfate using testicular hyaluronidase digestion. The labeled products obtained with the linkage tetra- and hexasaccharide serines and with the tetrasaccharide (GlcA beta 1-3GalNAc)2 were resistant to digestion with chondroitinase AC-II and beta-N-acetylhexosaminidase but sensitive to alpha-N-acetylgalactosaminidase digestion, indicating that the enzyme is an alpha-N-acetylgalactosaminyltransferase. This finding is in contrast to that of Rohrmann et al. (Rohrmann, K., Niemann, R., and Buddecke, E. (1985) Eur. J. Biochem., 148, 463-469), who reported that a corresponding product was susceptible to digestion with beta-N-acetylhexosaminidase. The presence of a sulfate group at C4 of the penultimate GalNAc or Gal units markedly inhibited the transfer of GalNAc to the terminal GlcA, while a sulfate group at C6 of the GalNAc had little effect on the transfer. Moreover, a slight but significant transfer of [3H]GalNAc was observed to an oligosaccharide containing terminal 2-O-sulfated GlcA as acceptor, whereas no incorporation was detected into oligosaccharides containing terminal unsaturated or 3-O-sulfated GlcA units. These results suggest that this novel serum enzyme is a UDP-GalNAc:chondro-oligosaccharide alpha 1-3- or 1-4-N-acetylgalactosaminyltransferase. The possibility of involvement of this enzyme in glycosaminoglycan biosynthesis is discussed.
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PMID:N-acetylgalactosamine (GalNAc) transfer to the common carbohydrate-protein linkage region of sulfated glycosaminoglycans. Identification of UDP-GalNAc:chondro-oligosaccharide alpha-N-acetylgalactosaminyltransferase in fetal bovine serum. 767 97

Hyaluronidase from the venom of the honeybee (Apis mellifera) has been purified by gelpermeation and cation exchange chromatography. Its asparagine-linked carbohydrate chains were released from tryptic glycopeptides with N-glycosidase A and reductively aminated with 2-aminopyridine. Separation of the fluorescent derivatives by size-fractionation and reversed-phase HPLC afforded eighteen fractions which were analysed by two-dimensional HPLC mapping combined with exoglycosidase digestions. The bulk of the N-linked glycans of hyaluronidase consisted of small oligosaccharides (Man1-3GlcNAc2), most of which were either alpha 1,3-monofucosylated or alpha 1,3-(alpha 1,6-)difucosylated at the innermost GlcNAc residue. High-mannose type structures constituted the minor fractions, together making up about 5% of the oligosaccharide pool from hyaluronidase. Four fractions, making up 8% of the N-linked glycans, contained the terminal trisaccharide GalNAc beta 1-4[Fuc alpha 1-3]GlcNAc beta 1- in beta 1,2-linkage to the core alpha 1,3-mannosyl residue. No evidence for the presence of O-glycans or sialic acids could be found.
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PMID:The asparagine-linked carbohydrate of honeybee venom hyaluronidase. 779 17

The low-sulfated chondroitin 4-sulfate(LSC) chain from human urinary trypsin inhibitor was purified and the structure was characterized. After hyaluronidase SD digestion of LSC, an oligosaccharide which contains the linkage region could be obtained. The structure of oligosaccharide was analyzed by HPLC and 500 MHz 1H-NMR spectroscopy. The analytical results revealed that 4-O-sulfo GalNAc residues were located in the neighborhood of the linkage region.
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PMID:Structural analysis of a low-sulfated chondroitin sulfate chain in human urinary trypsin inhibitor. 826 67

Streptococcus intermedius, part of the 'Streptococcus milleri group', has the ability to produce glycosaminoglycan depolymerising enzymes (hyaluronidase and chrondroitin sulphate depolymerase) which is unique amongst the viridans streptococci and may contribute to their virulence in brain and liver abscesses. The growth of S. intermedius strain UNS 35 was studied in basal medium supplemented with chondroitin sulphate A (CS-A, sulphated at position 4 of the N-acetylgalactosamine moiety) or chondroitin sulphate C (CS-C, sulphated at position 6 of the N-acetylgalactosamine moiety) as the major carbohydrate source. CS-A but not CS-C supported the growth of S. intermedius. Extracellular degradation of CS-A resulted in the initial accumulation of 2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-delta-enepyranosyluronic acid)-D-galactose (deltaUA GalNAc-0S), and low levels of 2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-delta-enepyranosyl uronic acid)-4-O-sulpho-D-galactose (deltaUA GalNAc-4S) in the medium with GalNAc-0S being subsequently utilised during bacterial growth. Metabolic end-products included formate and ethanol but not lactate, indicating that growth was probably carbon-limited. The CS-A contained 30% CS-C, which was also depolymerised resulting in the formation of 2-acetamido-2-deoxy-3-O-(beta-D-gluco-4-delta-enepyranosyluronic acid)-6-O-sulpho-D-galactose (deltaUA GalNAc-6S) in the culture supernate, but this unsaturated disaccharide was apparently not utilised during growth. The results indicate that S. intermedius produced CS-AC depolymerase, which was inducible and extracellular, and sulphatase activity. Experiments with authentic deltaUA GalNAc-4S and deltaUA GalNAc-6S demonstrated that deltaUA GalNAc4S rather than deltaUA GalNAc-6S was the preferred substrate for the sulphatase. Therefore, it is suggested that the CS-AC depolymerase of S. intermedius may play a role in the destruction of CS in host tissues, facilitating bacterial spread, and also in bacterial nutrition by the liberation of nutrients at the site of infection.
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PMID:Degradation and utilisation of chondroitin sulphate by Streptococcus intermedius. 863 52

Distribution of complex carbohydrates in the peripheral and central nervous systems was investigated cytochemically with a lectin that binds specifically to terminal alpha GalNAc and with monoclonal antibodies against carbohydrate epitopes, including glucuronic acid 3-SO4 and chondroitins 6-SO4 and 4-SO4. Comparative staining with these methods differentiated and partially characterized several glycoconjugates in various sites and allowed a comparison of chemical heterogeneity to neural specialization. Distal terminals of sensory neurons concerned with hearing, balance, taste, touch, and sight expressed glucuronyl 3-SO4, which apparently was present in an undefined glycoprotein. Some neurons in sensory nuclei of the brainstem exhibited a similar constituent on their surfaces. Retinal rod outer segments and the cerebellar granular layer possessed masked glucuronyl 3-SO4 that became immunopositive after digestion with chondroitinase ABC and that occurred in chondroitin 6-SO4 and chondroitin 4-SO4, respectively. The surface of neurons in the eighth nerve root and in neighboring nodes of Ranvier stained for unmasked glucuronic acid 3-SO4 and chondroitin 6-SO4. Some neurons of the cerebral cortex expressed unmasked glucuronyl 3-SO4, chondroitin 6-SO4, and terminal alpha GalNAc on their surfaces. Certain cortical neurons and nerve tracts with chondroitin 6-SO4 and terminal alpha GalNAc lacked glucuronyl 3-SO4, and other neurons possessing chondroitin 6-SO4 failed to express either glucuronyl 3-SO4 or terminal alpha GalNAc. Lability of lectin affinity to hyaluronidase suggested the presence of terminal alpha GalNAc in the chondroitin 6-SO4 on cortical neurons. The findings document further the heterogeneity of neural glycoconjugates, expand knowledge about the diversity of neurons with respect to their content of partially characterized glycoconjugates, and link glucuronyl 3-SO4 with or without chondroitin 6-SO4 spatially to sites of active Na+ transport in sensory nerves.
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PMID:Differentiation of glycoconjugates localized to sensory terminals and selected sites in brain. 882 66

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

The relationship between sulfation and polymerization in chondroitin sulfate (CS) biosynthesis has been poorly understood. In this study, we investigated the specificity of bovine serum UDP-GalNAc: CS beta-GalNAc transferase responsible for chain elongation using structurally defined acceptor substrates. They consisted of tetra- and hexasaccharide-serines that were chemically synthesized and various regular oligosaccharides with a GlcA residue at the nonreducing terminus, prepared from chondroitin and CS using testicular hyaluronidase. The enzyme preparation was obtained from fetal bovine serum by means of heparin-Sepharose affinity chromatography. The preparation did not contain the alpha-GalNAc transferase recently demonstrated in fetal bovine serum (Kitagawa et al., J. Biol. Chem., 270, 22190-22195, 1995), that utilizes common acceptor substrates. The beta-GalNAc transferase used as acceptors, two hexasaccharide-serines GlcA beta 1-3GalNAc beta 1-4GlcA beta 1-3Gal beta 1-3Gal beta 1-4Xyl beta 1-O-Ser and GlcA beta 1-3GalNAc(4-sulfate) beta 1-4GlcA beta 1-3Gal (4-sulfate) beta 1-3Gal beta 1-4Xyl beta 1-O-Ser, but neither the monosulfated hexasaccharide-serine GlcA beta 1-3GalNAc(4-sulfate) beta 1-4GlcA beta 1-3Gal beta 1-3Gal beta 1-4Xyl beta 1-O-Ser nor tetrasaccharide-serines with or without a sulfate group at C-4 of the third sugar residue Gal-3 from the reducing end. The results indicated that the sulfate group at the Gal-3 C-4 markedly affected the transfer of GalNAc to the terminal GlcA. In addition, a sulfate group at C-4 of the reducing terminal GalNAc of regular tetrasaccharides remarkably enhanced the GalNAc transfer, suggesting that the enzyme recognizes up to the fourth saccharide residue from the nonreducing end. The level of incorporation into a tetra- or hexasaccharide containing a terminal 2-O-sulfated GlcA residue was significant, whereas there was no apparent incorporation into tetra- or hexasaccharides containing a terminal 3-O-sulfated GlcA or penultimate 4,6-O-disulfated GalNAc residue. These results indicated that sulfation reactions play important roles in chain elongation and termination.
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PMID:Regulation of chondroitin sulfate biosynthesis by specific sulfation: acceptor specificity of serum beta-GalNAc transferase revealed by structurally defined oligosaccharides. 918 34

We previously isolated novel tetrasaccharides containing 3-O-sulfated glucuronic acid from king crab cartilage chondroitin sulfate K and demonstrated that the disaccharide units containing 3-O-sulfated glucuronic acid were decomposed by chondroitinase ABC digestion (Sugahara, K., Tanaka, Y., Yamada, S., Seno, N., Kitagawa, H., Haslam, S. M., Morris, H. R., and Dell, A. (1996) J. Biol. Chem. 271, 26745-26754). The findings indicated the necessity to re-evaluate the disaccharide compositions of chondroitin sulfate preparations purified from other biological sources and analyzed using the above enzyme. In this study, to evaluate squid cartilage chondroitin sulfate E a series of even-numbered oligosaccharides were isolated after exhaustive digestion with sheep testicular hyaluronidase and subsequent fractionation by gel chromatography. The tetrasaccharide fraction was subfractionated by high performance liquid chromatography on an amine-bound silica column. Systematic structural analysis of five major fractions, h, l, m, n, and q, by fast atom bombardment mass spectrometry, enzymatic digestions in conjunction with capillary electrophoresis, and 500-MHz 1H NMR spectroscopy revealed one disulfated, three trisulfated, and one tetrasulfated tetrasaccharide structure: fraction h, GlcAbeta1-3GalNAc(4S)beta1-4GlcAbeta1-3GalNAc(4S); fraction l, GlcA(3S)beta1-3GalNAc(6S)beta1-4GlcAbeta1-3GalNAc(4S); fraction m, GlcA(3S)beta1-3GalNAc(4S)beta1-4GlcAbeta1-3GalNAc(4S); fraction n, GlcAbeta1-3GalNAc(4S,6S)beta1-4GlcAbeta1-3GalNAc(4S); and fraction q, GlcA(3S)beta1-3GalNAc(4S,6S)beta1-4GlcAbeta1-3GalNAc(4S), where 3S, 4S, and 6S represent 3-O-, 4-O- and 6-O-sulfate, respectively. The structures found in fractions h and m as well as the unsaturated counterpart of that found in fraction n have been reported, whereas those in fractions l and q are novel in that they contained unusual disulfated and trisulfated disaccharide units where GlcA(3S) is directly linked to GalNAc(6S) and GalNAc(4S,6S), respectively. These novel tetrasaccharide sequences are distinct from those found in other chondroitin sulfate isoforms and may play key roles in the biological functions and activities of chondroitin sulfate E not only from squid cartilage but also from mammalian cells and tissues.
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PMID:Novel tetrasaccharides isolated from squid cartilage chondroitin sulfate E contain unusual sulfated disaccharide units GlcA(3-O-sulfate)beta1-3GalNAc(6-O-sulfate) or GlcA(3-O-sulfate)beta1-3GalNAc. 924 20


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