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.
Enzymes which catalyze the elimination of glucuronate residues from chondroitin A,B, and C or which catalyze the hydrolysis of sulfate groups of the 2-acetamido-2-deoxy-D-galactose 6-sulfate units of chondroitin sulfate. EC 4.2.2.-.
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.
A genus of gram-negative, anaerobic, rod-shaped bacteria. Its organisms are normal inhabitants of the oral, respiratory, intestinal, and urogenital cavities of humans, animals, and insects. Some species may be pathogenic.
A mucopolysaccharide constituent of chondrin. (Grant & Hackh's Chemical Dictionary, 5th ed)
A naturally occurring glycosaminoglycan found mostly in the skin and in connective tissue. It differs from CHONDROITIN SULFATE A (see CHONDROITIN SULFATES) by containing IDURONIC ACID in place of glucuronic acid, its epimer, at carbon atom 5. (from Merck, 12th ed)
Heteropolysaccharides which contain an N-acetylated hexosamine in a characteristic repeating disaccharide unit. The repeating structure of each disaccharide involves alternate 1,4- and 1,3-linkages consisting of either N-acetylglucosamine or N-acetylgalactosamine.
A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in SOIL and WATER. Its organisms are also found in raw meats, MILK and other FOOD, hospital environments, and human clinical specimens. Some species are pathogenic in humans.
Oligosaccharides containing two monosaccharide units linked by a glycosidic bond.
Proteoglycans consisting of proteins linked to one or more CHONDROITIN SULFATE-containing oligosaccharide chains.
A class of enzymes that catalyze the cleavage of C-C, C-O, and C-N, and other bonds by other means than by hydrolysis or oxidation. (Enzyme Nomenclature, 1992) EC 4.
An enzyme that catalyzes the eliminative degradation of polysaccharides containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucuronosyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups. (Enzyme Nomenclature, 1992)
Glycoproteins which have a very high polysaccharide content.

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)

Yamagata T, Saito H, Habuchi O, Suzuki S (April 1968). "Purification and properties of bacterial chondroitinases and ... Chondroitin ABC lyase (EC 4.2.2.20 EC 4.2.2.21, chondroitinase, chondroitin ABC eliminase, chondroitinase ABC) is an enzyme ... Chondroitin+ABC+lyase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 4.2.2, ... with systematic name chondroitin ABC lyase. This enzyme catalyses the following chemical reaction Eliminative degradation of ...
Suzuki K, Terasaki Y, Uyeda M (2002). "Inhibition of hyaluronidases and chondroitinases by fatty acids". J. Enzyme. Inhib. Med ... The enzyme chondroitin B lyase (EC 4.2.2.19) catalyzes the following process: Eliminative cleavage of dermatan sulfate ... 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 ABC lyase (ambiguous), chondroitin sulfate ABC lyase (ambiguous), ChS ABC lyase (ambiguous), chondroitin sulfate ... Yamagata T, Saito H, Habuchi O, Suzuki S (1968). "Purification and properties of bacterial chondroitinases and ... This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The systematic ... "Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding tetrasaccharides and an exoeliminase preferentially ...
... 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 ...
... 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 ...
Chondroitinases and Chondroitin Lyases [D08.811.520.241.700.350] * Chondroitin Lyases [D08.811.520.241.700.350.500] ... Chondroitinases and Chondroitin Lyases Preferred Term Term UI T008202. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1976). ... Chondroitinases and Chondroitin Lyases [D08.811.277.352.827.180] * Chondroitinsulfatases [D08.811.277.352.827.180.175] ... Chondroitinases and Chondroitin Lyases Preferred Concept UI. M0004324. Registry Number. EC 4.2.2.-. Scope Note. Enzymes which ...
Chondroitinases and Chondroitin Lyases [D08.811.520.241.700.350] * Chondroitin Lyases [D08.811.520.241.700.350.500] ... Chondroitinases and Chondroitin Lyases Preferred Term Term UI T008202. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1976). ... Chondroitinases and Chondroitin Lyases [D08.811.277.352.827.180] * Chondroitinsulfatases [D08.811.277.352.827.180.175] ... Chondroitinases and Chondroitin Lyases Preferred Concept UI. M0004324. Registry Number. EC 4.2.2.-. Scope Note. Enzymes which ...
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 & ... Chondroitin-4-Sulfate Depolymerase - Narrower Concept UI. M0004323. Scope note. Enzymes which catalyze the elimination of ...
Chondroitin Lyases N0000169197 Chondroitin Sulfate Proteoglycans N0000010542 Chondroitin Sulfates N0000168036 Chondroitinases ... N0000179080 cholinophyllin N0000167603 Chondro-4-Sulfatase N0000005998 Chondroitin N0000168038 Chondroitin ABC Lyase ... and Chondroitin Lyases N0000167602 Chondroitinsulfatases N0000006057 Chorionic Gonadotropin N0000171362 Chorionic Gonadotropin ... as Amide-N-Donor N0000168008 Carbon-Nitrogen Lyases N0000167775 Carbon-Oxygen Ligases N0000008169 Carbon-Oxygen Lyases ...
ABC Lyase N0000168037 Chondroitin Lyases N0000010542 Chondroitin Sulfates N0000168036 Chondroitinases and Chondroitin Lyases ... as Amide-N-Donor N0000168008 Carbon-Nitrogen Lyases N0000167775 Carbon-Oxygen Ligases N0000008169 Carbon-Oxygen Lyases ... N0000010373 Cholinesterases N0000167603 Chondro-4-Sulfatase N0000005998 Chondroitin N0000168038 Chondroitin ... Lyase N0000168230 DNA-Activated Protein Kinase N0000169224 DNA-Binding Proteins N0000168286 DNA-Directed DNA Polymerase ...
HYDROLASES CHONDROITINASES AND CHONDROITIN LYASES HYDROLASES CHONDROITINSULFATASES HYDROLASES CHYMOPAPAIN HYDROLASES CHYMOSIN ... ANTINEOPLASTIC AND IMMUNOSUPPRESSIVE AG PHENYLALANINE AMMONIA-LYASE ANTINEOPLASTIC AND IMMUNOSUPPRESSIVE AG PHLEOMYCINS ... ANTINEOPLASTIC AGENTS PHENYLALANINE AMMONIA-LYASE ANTINEOPLASTIC AGENTS PHLEOMYCINS ANTINEOPLASTIC AGENTS PHOSPHORAMIDE ...
Chondroitinases and Chondroitin Lyases. *Iduronate Sulfatase. Below are MeSH descriptors whose meaning is more specific than " ...
Chondroitin sulphate,Chondroitin sulphate Chondroitinases and Chondroitin Lyases,Chondroitinases Chondroitin Lyases Chorionic ... Lyase, Chondroitin ABC Lyase, Chondroitin AC,Lyase, Chondroitin AC Lyase, Chondroitin B,Lyase, Chondroitin B Lyase, Chondroitin ... Chondroitin ABC eliminase Chondroitin ABC lyase,Chondroitin ABC lyase Chondroitin AC Lyase,Chondroitin AC Lyase Chondroitin AC ... Chondroitin AC eliminase Chondroitin AC lyase,Chondroitin AC lyase Chondroitin B Lyase,Chondroitin B Lyase Chondroitin ...
Chondroitin Chondroitin ABC Lyase Chondroitin Lyases Chondroitin Sulfate Proteoglycans Chondroitin Sulfates Chondroitinases and ... Carbon-Nitrogen Lyases Carbon-Oxygen Ligases Carbon-Oxygen Lyases Carbon-Sulfur Ligases Carbon-Sulfur Lyases Carbonated ... Chondroitin Lyases Chondroitinsulfatases Chondroma Chondromalacia Patellae Chondromatosis Chondromatosis, Synovial ... Lyase DNA-Activated Protein Kinase DNA-Binding Proteins DNA-Cytosine Methylases DNA-Directed DNA Polymerase DNA-Directed RNA ...
Chondroitin sulphate,Chondroitin sulphate Chondroitinases and Chondroitin Lyases,Chondroitinases Chondroitin Lyases Chorionic ... Lyase, Chondroitin ABC Lyase, Chondroitin AC,Lyase, Chondroitin AC Lyase, Chondroitin B,Lyase, Chondroitin B Lyase, Chondroitin ... Chondroitin ABC eliminase Chondroitin ABC lyase,Chondroitin ABC lyase Chondroitin AC Lyase,Chondroitin AC Lyase Chondroitin AC ... Chondroitin AC eliminase Chondroitin AC lyase,Chondroitin AC lyase Chondroitin B Lyase,Chondroitin B Lyase Chondroitin ...
Chondroitinases and Chondroitin Lyases / metabolism Actions. * Search in PubMed * Search in MeSH ... Scott JE, Haigh M. Identification of specific binding sites for keratan sulphate proteoglycans and chondroitin-dermatan ...
... isda iscu scopolia isct nonselective iscs iscr glycosylase isca barusiban panniformis indinavir isbt indralin anaerobes lyase ... acetamidomethyl polycyclic gste1 cilostazol grating cd85j inoviridae sigmoidorectal optional tipping hyperoxaluria chondroitin ... dysphagia arupense precedent vacuolatus hexahydroxanthene vacuolatum onchocercal batching vestige mesectoderm chondroitinases ... antiplatelet glomuvenous hsv2 hsv1 campinasensis cyclohexa phycocyanobilin sylvarum mmh2o bitucarpin gemistocyte hst7 lyases ...

No FAQ available that match "chondroitinases and chondroitin lyases"