Chondroitin Lyases
Enzymes which catalyze the elimination of delta-4,5-D-glucuronate residues from polysaccharides containing 1,4-beta-hexosaminyl and 1,3-beta-D-glucuronosyl or 1,3-alpha-L-iduronosyl linkages thereby bringing about depolymerization. EC 4.2.2.4 acts on chondroitin sulfate A and C as well as on dermatan sulfate and slowly on hyaluronate. EC 4.2.2.5 acts on chondroitin sulfate A and C.
Chondroitinases and Chondroitin Lyases
Chondroitin Sulfates
Derivatives of chondroitin which have a sulfate moiety esterified to the galactosamine moiety of chondroitin. Chondroitin sulfate A, or chondroitin 4-sulfate, and chondroitin sulfate C, or chondroitin 6-sulfate, have the sulfate esterified in the 4- and 6-positions, respectively. Chondroitin sulfate B (beta heparin; DERMATAN SULFATE) is a misnomer and this compound is not a true chondroitin sulfate.
Bacteroides
Chondroitin
Dermatan Sulfate
Glycosaminoglycans
Flavobacterium
Chondroitin Sulfate Proteoglycans
Lyases
Chondroitin ABC Lyase
Chromogranin A
A type of chromogranin which was first isolated from CHROMAFFIN CELLS of the ADRENAL MEDULLA but is also found in other tissues and in many species including human, bovine, rat, mouse, and others. It is an acidic protein with 431 to 445 amino acid residues. It contains fragments that inhibit vasoconstriction or release of hormones and neurotransmitter, while other fragments exert antimicrobial actions.
Chromaffin Granules
Heparan Sulfate Proteoglycans
Ubiquitous macromolecules associated with the cell surface and extracellular matrix of a wide range of cells of vertebrate and invertebrate tissues. They are essential cofactors in cell-matrix adhesion processes, in cell-cell recognition systems, and in receptor-growth factor interactions. (From Cancer Metastasis Rev 1996; 15(2): 177-86; Hepatology 1996; 24(3): 524-32)
Keratan Sulfate
A sulfated mucopolysaccharide initially isolated from bovine cornea. At least two types are known. Type I, found mostly in the cornea, contains D-galactose and D-glucosamine-6-O-sulfate as the repeating unit; type II, found in skeletal tissues, contains D-galactose and D-galactosamine-6-O-sulfate as the repeating unit.
Corneal Stroma
Cornea
The transparent anterior portion of the fibrous coat of the eye consisting of five layers: stratified squamous CORNEAL EPITHELIUM; BOWMAN MEMBRANE; CORNEAL STROMA; DESCEMET MEMBRANE; and mesenchymal CORNEAL ENDOTHELIUM. It serves as the first refracting medium of the eye. It is structurally continuous with the SCLERA, avascular, receiving its nourishment by permeation through spaces between the lamellae, and is innervated by the ophthalmic division of the TRIGEMINAL NERVE via the ciliary nerves and those of the surrounding conjunctiva which together form plexuses. (Cline et al., Dictionary of Visual Science, 4th ed)
Identification and characterization of ligands for L-selectin in the kidney. II. Expression of chondroitin sulfate and heparan sulfate proteoglycans reactive with L-selectin. (1/161)
Ligands for the leukocyte adhesion molecule L-selectin are expressed not only in lymph node high endothelial venules (HEV) but also in the renal distal tubuli. Here we report that L-selectin-reactive molecules in the kidney are chondroitin sulfate and heparan sulfate proteoglycans of 500-1000 kDa, unlike those in HEV bearing sialyl Lewis X-like carbohydrates. Binding of L-selectin to these molecules was mediated by the lectin domain of L-selectin and required divalent cations. Binding was inhibited by chondroitinase and/or heparitinase but not sialidase. Thus, L-selectin can recognize chondroitin sulfate and heparan sulfate glycosaminoglycans structurally distinct from sialyl Lewis X-like carbohydrates. (+info)Action of chondroitinases. II. Numerical calculation of the degree of multiple attack. (2/161)
Further investigation was carried out on the action patterns of two chondroitinase-AC [EC 4.2.2.5.] preparations obtained from Arthrobacter aurescens and Flavobacterium heparinum. To infer the action patterns of the chondroitinases, we proposed a new method for the calculation of the degree of multiple attack, based on the concept established by Robyt and French ((1967) Arch. Biochem. Biophys. 122, 8-16). It was shown that the degree of multiple attack (DM) is represented by the ratio of the initial velocity of number-average degree of scission to that of viscosity-average degree of scission. By this method, DM for A-Chase was estimated to be 3.03 and for F-chase, 1.31. (+info)Perineuronal nets of proteoglycans in the adult mouse brain, with special reference to their reactions to Gomori's ammoniacal silver and Ehrlich's methylene blue. (3/161)
As our previous studies have indicated, many subsets of neurons in the vertebrate brain possess a sulfated proteoglycan surface coat which reacts to cationic iron colloid and aldehyde fuchsin. The present study demonstrated that this surface coat is supravitally stained with Ehrlich's methylene blue, and doubly with this blue and aldehyde fuchsin, a finding suggesting its being identical to Cajal's superficial reticulum (red superficial) and to Golgi's reticular coating (revetement reticulare). The perineuronal surface coat was further stained with Gomori's ammoniacal silver, and doubly with this silver and cationic iron colloid. These neurons with such a proteoglycan surface coat usually expressed cell surface glycoproteins which were labeled with lectin Wisteria floribunda agglutinin. Hyaluronidase digestion did not interfere with this lectin labeling of the glycoproteins, methylene blue and Gomori's ammoniacal silver staining of the surface coat, while it erased the cationic iron colloid and aldehyde fuchsin staining of the surface coat. These findings suggest that the perineuronal proteoglycan surface coat is associated with some additional molecules which are resistant to hyaluronidase digestion and stainable with methylene blue and Gomori's ammoniacal silver. The possibility is suggested that these molecules might represent "ligand proteoglycans" connecting the perineuronal proteoglycans and cell surface glycoproteins. (+info)Isolation and characterization of proteoglycans from human follicular fluid. (4/161)
Two proteoglycans differing in size and composition were isolated from human follicular fluid. The larger one of high density had a molecular mass of 3.0x10(6) Da, as determined by laser light-scattering, and was substituted with 15-20 chondroitin sulphate (CS) chains (Mr 60000-65000). Half of the CS disaccharides were 6-sulphated, whereas the remaining ones were non-sulphated. Digestion of the CS proteoglycan with chondroitinase ABC lyase, followed by SDS/PAGE, yielded a protein core of 600 to 700 kDa including substituted oligosaccharides, and a band of 70 kDa that was identified as the heavy-chain component of the inter-alpha-trypsin inhibitor (ITI). Western blotting of the CS proteoglycan showed that this had reactivity with antibodies raised against human versican. Electron microscopy (EM) of the CS proteoglycan also revealed a versican-like structure, with one globular domain at each end of a long extended segment substituted with CS side chains, as well as a structure interpreted as being the heavy chain of ITI attached to CS chains. Laser light-scattering revealed that the smaller proteoglycan had a molecular mass of 1. 1x10(6) Da, and EM demonstrated that it had a globular-protein core structure. The core protein, which showed immunological reactivity with perlecan antibodies, was substituted with approximately seven heparan sulphate (HS) and CS chains of similar size (50-55 kDa), the CS disaccharides being mainly 6-sulphated (68%), with a small proportion being 4-sulphated. The protein core was shown to be heterogeneous, with bands occurring at 215, 330 and 400 kDa after enzymic degradation of the glycosaminoglycan chains followed by SDS/PAGE analysis. The demonstration of intact molecules and fragments obtained after stepwise degradations, as shown by gel chromatography, supported a 'composite' structure of this proteoglycan. (+info)Differentiation of human monocytes to monocyte-derived macrophages is associated with increased lipoprotein lipase-induced tumor necrosis factor-alpha expression and production: a process involving cell surface proteoglycans and protein kinase C. (5/161)
The aim of the present study was to (1) evaluate the responsiveness of human mononuclear cells to lipoprotein lipase (LPL), as assessed by tumor necrosis factor-alpha (TNFalpha) production, during the process of differentiation of monocytes to macrophages, and (2) determine the mechanisms by which LPL exerts its effect on these cells. Treatment of human monocytes with purified endotoxin-free bovine LPL (1 microgram/mL) resulted in a 161+/-15% increase in TNFalpha production over control values (P<0.01). A further increase in TNFalpha production was observed after treatment of monocyte-derived macrophages (MDMs) with LPL (490+/-81% over control values, P<0.01). Increased TNFalpha mRNA expression and protein kinase C activity were also observed in LPL-treated human monocytes and MDMs. These LPL effects were abrogated by the specific protein kinase C inhibitor calphostin C (1 micromol/L). Although heparinase totally abolished LPL-induced TNFalpha production in human monocytes, this agent did not significantly inhibit LPL effect in human MDMs. In contrast, treatment of MDMs with chondroitinase suppressed LPL-induced TNFalpha production. Taken together, these data suggest that (1) differentiation of human monocytes to MDMs is associated with increased LPL-induced TNFalpha mRNA expression and production, (2) a protein kinase C-dependent pathway is involved in the induction of TNFalpha by LPL in these cells, and (3) LPL effect is mediated by cell surface proteoglycans. As MDMs secrete LPL in the vascular wall, we propose that LPL, by acting as an autocrine activator of MDM function, may contribute to the high level of TNFalpha found in the atheromatous lesion. (+info)The macromolecular characteristics of cartilage proteoglycans do not change when synthesis is up-regulated by link protein peptide. (6/161)
Previous studies have shown that a synthetic, unglycosylated analogue of the N-terminal peptide from link protein can function as a growth factor and up-regulate proteoglycan biosynthesis in explant cultures of normal human articular cartilage from a wide age range of subjects (McKenna et al., Arthritis Rheum. 41 (1998) 157-162). The present work further shows that link peptide increased proteoglycan synthesis by cartilage cultured in both the presence and absence of serum, suggesting that the mechanism of up-regulation may be different from that of insulin-like growth factors. The proteoglycans synthesised during stimulation with link peptide were of normal hydrodynamic size and the ratio of core protein to glycosaminoglycan side chains and the proportions of the large proteoglycan aggrecan to the small proteoglycans, decorin and biglycan, remained constant. Aggrecan molecules were equally capable of forming aggregates as those from control tissues and the relative proportions of decorin and biglycan were unchanged showing that both were co-ordinately up-regulated. These results confirmed that this novel peptide is a potent stimulator of proteoglycan synthesis by articular cartilage and showed that the newly synthesised proteoglycans were of normal composition. (+info)Mutations in the heparin binding domain of fibronectin in cooperation with the V region induce decreases in pp125(FAK) levels plus proteoglycan-mediated apoptosis via caspases. (7/161)
Intact fibronectin (FN) protects cells from apoptosis. When FN is fragmented, specific domains induce proteinase expression in fibroblasts. However, it is not known whether specific domains of FN can also regulate apoptosis. We exposed fibroblasts to four recombinant FN fragments and then assayed for apoptosis using criteria of cellular shape change, condensed nuclear morphology, and DNA fragmentation. The fragments extended from the RGD-containing repeat III10 to III15; they included (V(+)) or excluded (V(-)) the alternatively spliced V region and contained either a mutated (H(-)) or an unmutated (H(+)) heparin binding domain. Only the V(+)H(-) fragment triggered decreases in pp125(FAK) levels and apoptosis, which was rescued by intact FN and inhibitors of caspase-1 and caspase-3. This apoptotic mechanism was mediated by a chondroitin sulfate proteoglycan, since treating cells with chondroitin sulfate or chondroitinase reversed the apoptotic cell shape changes. The alpha4 integrin receptor may also be involved, since using a blocking antibody to alpha4 alone induced apoptotic cell shape changes, whereas co-treatment with this antibody plus V(+)H(+) reversed these effects. These results demonstrate that the V and heparin binding domains of FN modulate pp125(FAK) levels and regulate apoptosis through a chondroitin sulfate proteoglycan- and possibly alpha4 integrin-mediated pathway, which triggers a caspase cascade. (+info)Heparan sulfate proteoglycans as extracellular docking molecules for matrilysin (matrix metalloproteinase 7). (8/161)
Many matrix metalloproteinases (MMPs) are tightly bound to tissues; matrilysin (MMP-7), although the smallest of the MMPs, is one of the most tightly bound. The most likely docking molecules for MMP-7 are heparan sulfate proteoglycans on or around epithelial cells and in the underlying basement membrane. This is established by extraction experiments and confocal microscopy. The enzyme is extracted from homogenates of postpartum rat uterus by heparin/heparan sulfate and by heparinase III treatment. The enzyme is colocalized with heparan sulfate in the apical region of uterine glandular epithelial cells and can be released by heparinase digestion. Heparan sulfate and MMP-7 are expressed at similar stages of the rat estrous cycle. The strength of heparin binding by recombinant rat proMMP-7 was examined by affinity chromatography, affinity coelectrophoresis, and homogeneous enzyme-based binding assay; the K(D) is 5-10 nM. Zymographic measurement of MMP-7 activity is greatly enhanced by heparin. Two putative heparin-binding peptides have been identified near the C- and N-terminal regions of proMMP-7; however, molecular modeling suggests a more extensive binding track or cradle crossing multiple peptide strands. Evidence is also found for the binding of MMP-2, -9, and -13. Binding of MMP-7 and other MMPs to heparan sulfate in the extracellular space could prevent loss of secreted enzyme, provide a reservoir of latent enzyme, and facilitate cellular sensing and regulation of enzyme levels. Binding to the cell surface could position the enzyme for directed proteolytic attack, for activation of or by other MMPs and for regulation of other cell surface proteins. Dislodging MMPs by treatment with compounds such as heparin might be beneficial in attenuating excessive tissue breakdown such as occurs in cancer metastasis, arthritis, and angiogenesis. (+info)
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Product information, instructions, health benefits, and usage for Chondroitin Sulfate
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Prostatic chondroitin sulfate is increased in patients with metastatic disease but does not predict survival outcome<...
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List of MeSH codes (D08)
... chondroitinases and chondroitin lyases MeSH D08.811.520.241.700.350.500 - chondroitin lyases MeSH D08.811.520.241.700.350. ... chondroitinases and chondroitin lyases MeSH D08.811.277.352.827.180.175 - chondroitinsulfatases MeSH D08.811.277.352.827.180. ... chondroitin abc lyase MeSH D08.811.520.241.700.512 - heparin lyase MeSH D08.811.520.241.700.675 - hyaluronoglucosaminidase MeSH ... tyrosine phenol-lyase MeSH D08.811.520.232.300 - amidine-lyases MeSH D08.811.520.232.300.200 - adenylosuccinate lyase MeSH ...
Chondroitin-sulfate-ABC endolyase
... and ChS ABC lyase I. Yamagata T, Saito H, Habuchi O, Suzuki S (1968). "Purification and properties of bacterial chondroitinases ... chondroitin ABC lyase (ambiguous), chondroitin sulfate ABC lyase (ambiguous), ChS ABC lyase (ambiguous), chondroitin sulfate ... specifically those carbon-oxygen lyases acting on polysaccharides. The systematic name of this enzyme class is chondroitin- ... "Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding tetrasaccharides and an exoeliminase preferentially ...
Chondroitin B lyase
Suzuki K, Terasaki Y, Uyeda M (2002). "Inhibition of hyaluronidases and chondroitinases by fatty acids". J. Enzyme. Inhib. Med ... In enzymology, a chondroitin B lyase (EC 4.2.2.19) is an enzyme that catalyzes the chemical reaction Eliminative cleavage of ... The systematic name of this enzyme class is chondroitin B lyase. Other names in common use include chondroitinase B, ChonB, and ... V, Sasisekharan R, Cygler M (2004). "The structure of chondroitin B lyase complexed with glycosaminoglycan oligosaccharides ...
Glycans are involved in RANTES binding to CCR5 positive as well as to CCR5 negative cells
... heparan sulfate and chondroitin sulfate in the binding of full length (1--68) RANTES not only to CCR5 positive human primary ... Chondroitin Sulfates / pharmacology * Chondroitinases and Chondroitin Lyases * Glycosaminoglycans / metabolism * Heparin / ... heparan sulfate and chondroitin sulfate in the binding of full length (1--68) RANTES not only to CCR5 positive human primary ... heparin or chondroitin sulfate), significantly inhibited RANTES binding. Such effects were not observed with truncated (10--68 ...
Chondroitin B lyase - Wikipedia
Suzuki K, Terasaki Y, Uyeda M (2002). "Inhibition of hyaluronidases and chondroitinases by fatty acids". J. Enzyme. Inhib. Med ... In enzymology, a chondroitin B lyase (EC 4.2.2.19) is an enzyme that catalyzes the chemical reaction Eliminative cleavage of ... The systematic name of this enzyme class is chondroitin B lyase. Other names in common use include chondroitinase B, ChonB, and ... V, Sasisekharan R, Cygler M (2004). "The structure of chondroitin B lyase complexed with glycosaminoglycan oligosaccharides ...
Chondroitin Lyase from a Marine Arthrobacter sp. MAT3885 for the Production of Chondroitin Sulfate Disaccharides | SpringerLink
Chondroitin sulfate (CS) saccharides from cartilage tissues have potential application in medicine or as dietary supplements ... An improved methodology to produce Flavobacterium heparinum chondroitinases, important instruments for diagnosis of diseases. ... Chondroitin sulfate Chondroitin sulfate lyase Marine Arthrobacter sp. This is a preview of subscription content, log in to ... Chondroitin Lyase from a Marine Arthrobacter sp. MAT3885 for the Production of Chondroitin Sulfate Disaccharides. ...
Expression System for High Levels of GAG Lyase Gene Expression and Study of the hepA Upstream Region in Flavobacterium...
Purification of GAG lyases.Purification of the heparinases and chondroitinases from F. heparinum was described previously (11, ... The higher chondroitin sulfate A-degrading activity seen in strain FIBX6 grown in chondroitin sulfate A medium could not be ... Two chondroitinases from F. heparinum, chondroitinases AC (ChnA) and B (ChnB), were purified and characterized. It was shown ... Enzyme assay.Heparin-, heparan sulfate-, chondroitin sulfate A-, chondroitin sulfate C-, and dermatan sulfate-degrading ...
List of MeSH codes (D08) - Wikipedia
... chondroitinases and chondroitin lyases MeSH D08.811.520.241.700.350.500 - chondroitin lyases MeSH D08.811.520.241.700.350. ... chondroitinases and chondroitin lyases MeSH D08.811.277.352.827.180.175 - chondroitinsulfatases MeSH D08.811.277.352.827.180. ... chondroitin abc lyase MeSH D08.811.520.241.700.512 - heparin lyase MeSH D08.811.520.241.700.675 - hyaluronoglucosaminidase MeSH ... tyrosine phenol-lyase MeSH D08.811.520.232.300 - amidine-lyases MeSH D08.811.520.232.300.200 - adenylosuccinate lyase MeSH ...
Glycomics expression analysis of sulfated glycosaminoglycans of human colorectal cancer tissues and non-neoplastic mucosa by...
The identity of the different S-GAG was confirmed by degradation with specific lyases: chondroitinases B, AC (Seikagaku Kogyo ... CS: chondroitin sulphate.. Figure 2 Mass spectroscopy to identify chondroitin sulphate oligosaccharides. Chondroitin sulphate ... The substrate specificity of chondroitinases B, AC were CS A and C, chondroitin, and hyaluronic acid. The chondroitinase AC ... The products were compared with the standard of chondroitin-4-sulphated and chondroitin-6-sulphated products ...
Microvascular effects of chondroitinase ABC and chymopapain. An in vivo experimental study on hamsters and rabbits
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Chromaffin granule and PC12 cell chondroitin sulfate proteoglycans and their relation to chromogranin A - Fingerprint
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- Augusta University Research Profiles
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Lokeshwar, V. B., Morera, D. S., Hasanali, S. L., Yates, T. J., Hupe, M. C., Knapp, J., Lokeshwar, S. D., Wang, J., Hennig, M. J. P., Baskar, R., Escudero, D. O., Racine, R. R., Dhir, N., Jordan, A. R., Hoye, K., Azih, I., Manoharan, M., Klaassen, Z. W. A., Kavuri, S. K., Lopez, L. E. & 2 others, Ghosh, S. & Lokeshwar, B. L., Jul 1 2020, In : Clinical cancer research : an official journal of the American Association for Cancer Research. 26, 13, p. 3455-3467 13 p.. Research output: Contribution to journal › Article ...
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DeCS
Chondroitinases et chondroitin lyases Entry term(s):. Chondroitin 4 Sulfate Depolymerase. Chondroitin-4-Sulfate Depolymerase. ... Chondroitinases and Chondroitin Lyases - Preferred Concept UI. M0004324. Scope note. Enzymes which catalyze the elimination of ... CHONDROITIN LYASES is available. Allowable Qualifiers:. AD administration & dosage. AE adverse effects. AI antagonists & ... Enzymes which catalyze the elimination of glucuronate residues from chondroitin A,B, and C or which catalyze the hydrolysis of ...
Wei-Ping Lee - Research Output
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A permeability barrier surrounds taste buds in lingual epithelia - Fingerprint
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A Heparan Sulfate-containing Fraction of Bone Marrow Stroma Induces Maturation of HL-60 Cells in Vitro<...
Chondroitinases and Chondroitin Lyases Medicine & Life Sciences View full fingerprint Cite this. * APA ... Other stromal components such as laminin, fibronec-tin, collagen I, collagen IV, or chondroitin sulfate did not alter the HL-60 ... Other stromal components such as laminin, fibronec-tin, collagen I, collagen IV, or chondroitin sulfate did not alter the HL-60 ... Other stromal components such as laminin, fibronec-tin, collagen I, collagen IV, or chondroitin sulfate did not alter the HL-60 ...
Chondroitin Sulfate And Cancer - Chondroitin Sulfate
B. GalAG Lyase-Mediated Degradation of GAGs. Chondroitinases (Table VI) are produced in soil and intestinal bacteria. ... C. Chondroitinases from Pedobacter heparinus. Chondroitinase ABC from P. heparinus is a broad substrate specificity lyase that ... Chondroitin lyases have been isolated and characterized from a variety genera, most notably Pedobacter (Fethiere et al., 1999; ... has actually been found to comprise two distinct lyases, chondroitinases ABC I and II. Both enzymes cleave a wide variety of ...
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chondroitin sulphate-dermatan sulphate hybrid (1) 1 Filter by. Remove filter. chondroitinases and chondroitin lyases - ... Chondroitinases and Chondroitin Lyases - metabolism , Sulfates - metabolism , Disaccharides - metabolism , Glycosaminoglycans ... Chondroitin sulphate , N-linked oligosaccharide , Site-directed mutagenesis , Tunicamycin , Chondroitin 4-sulphotransferase ( ... C4ST-1 (chondroitin 4-sulphotransferase-1) transfers sulphate to position 4 of N-acetylgalactosamine in chondroitin. We showed ...
DeCS
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Chondroitinases and Chondroitin Lyases/isolation & purification , Chromatography/methods , Flavobacterium/enzymology , ... Chondroitin Sulfates/chemistry , Chondroitin Sulfates/isolation & purification , Culture Media , Dermatan Sulfate/chemistry , ... Cellular adhesion to laminin involves a chondroitin sulfate proteoglycan Elias, M. C. Q. B; Veiga, S. S; Gremski, W; Brentani, ... Chondroitinases AC and B were separated from each other and also from glucuronidases and sulfatases by hydrophobic interaction ...
ExplorEnz: EC 4.2.2.19
chondroitin B lyase. Comments:. This is the only lyase that is known to be specific for dermatan sulfate as substrate. The ... Suzuki, K., Terasaki, Y. and Uyeda, M. Inhibition of hyaluronidases and chondroitinases by fatty acids. J. Enzyme 17 (2002) 183 ... chondroitin B lyase. Reaction:. Eliminative cleavage of dermatan sulfate containing (1→4)-β-D-hexosaminyl and (1→3)-β-D- ... The structure of chondroitin B lyase complexed with glycosaminoglycan oligosaccharides unravels a calcium-dependent catalytic ...
Proteoglycans and GAG research | amsbio
GAG Oligosaccharides for Heparin, Hyaluronic Acid, Chondroitin Sulfate and Dermatan Sulfate. Disaccharide standards for ... GAG Degrading Enzymes including Chondroitinases (ABC, AC I and II,), heparinase / heparitinase family, Hyaluronidases, ... keratanases and new K5 heparan lyase (Technical Bulletin). *Chondroitinase ABC enzyme, Chondroitin Sulfate "stub antibodies" ... Monoclonal antibodies to Chondroitin Sulfate, Heparan Sulfate, Keratan Sulfate. *Recombinant Hyaluronic Acid Binding Protein ...
Recent progress on deep eutectic solvents in biocatalysis | Bioresources and Bioprocessing | Full Text
2014), benzaldehyde lyase (Maugeri and Domínguez de María 2014) and phospholipase D (Yang and Duan 2016), also showed improved ... Chondroitinases ABCI. ChCl/Gly (1:2). Chondroitin. Improving thermal stability remarkably. Daneshjou et al. (2017) ... Daneshjou S, Khodaverdian S, Dabirmanesh B, Rahimi F, Daneshjoo S, Ghazi F, Khajeh K (2017) Improvement of chondroitinases ABCI ... Maugeri Z, Domínguez de María P (2014) Benzaldehyde lyase (BAL)-catalyzed enantioselective CC bond formation in deep-eutectic- ...
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The incubations with chondroitin (Fig. 6A) showed a 13-fold upregulation of 4-O-activity in tumor tissue as compared with ... To this end, CS/DS was purified and extensively degraded into disaccharides by a mixture of chondroitinases ABC, AC-I, and B ... In both cases, the digest solutions were incubated at 37°C, and after 2 hours, another aliquot of lyases was added. ... Involvement of chondroitin sulfate E in the liver tumor focal formation of murine osteosarcoma cells. Glycobiology 2009;19:735- ...