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.-.
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.
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 mucopolysaccharide constituent of chondrin. (Grant & Hackh's Chemical Dictionary, 5th ed)
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)
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 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)
Glycoproteins which have a very high polysaccharide content.
Oligosaccharides containing two monosaccharide units linked by a glycosidic bond.
Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form.
Spherical particles of nanometer dimensions.
Penetrating and non-penetrating injuries to the spinal cord resulting from traumatic external forces (e.g., WOUNDS, GUNSHOT; WHIPLASH INJURIES; etc.).
Small uniformly-sized spherical particles, of micrometer dimensions, frequently labeled with radioisotopes or various reagents acting as tags or markers.
A biocompatible polymer used as a surgical suture material.
A cylindrical column of tissue that lies within the vertebral canal. It is composed of WHITE MATTER and GRAY MATTER.
The functions, behavior, and activities of bacteria.

Action of chondroitinases. II. Numerical calculation of the degree of multiple attack. (1/149)

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)

Substrate specificity studies of Flavobacterium chondroitinase C and heparitinases towards the glycosaminoglycan--protein linkage region. Use of a sensitive analytical method developed by chromophore-labeling of linkage glycoserines using dimethylaminoazobenzenesulfonyl chloride. (2/149)

Bacterial chondroitinases and heparitinases are potentially useful tools for structural studies of chondroitin sulfate and heparin/heparan sulfate. Substrate specificities of Flavobacterium chondroitinase C, as well as heparitinases I and II, towards the glycosaminoglycan-protein linkage region -HexA-HexNAc-GlcA-Gal-Gal-Xyl-Ser (where HexA represents glucuronic acid or iduronic acid and HexNAc represents N-acetylgalactosamine or N-acetylglucosamine) were investigated using various structurally defined oligosaccharides or oligosaccharide-serines derived from the linkage region. In the case of oligosaccharide-serines, they were labeled with a chromophore dimethylaminoazobenzenesulfonyl chloride (DABS-Cl), which stably reacted with the amino group of the serine residue and rendered high absorbance for microanalysis. Chondroitinase C cleaved the GalNAc bond of the pentasaccharides or hexasaccharides derived from the linkage region of chondroitin sulfate chains and tolerated sulfation of the C-4 or C-6 of the GalNAc residue and C-6 of the Gal residues, as well as 2-O-phosphorylation of the Xyl residue. In contrast, it did not act on the GalNAc-GlcA linkage when attached to a 4-O-sulfated Gal residue. Heparitinase I cleaved the innermost glucosaminidic bond of the linkage region oligosaccharide-serines of heparin/heparan sulfate irrespective of substitution by uronic acid, whereas heparitinase II acted only on the glucosaminidic linkages of the repeating disaccharide region, but not on the innermost glucosaminidic linkage. These defined specificities of chondroitinase C, as well as heparitinases I and II, will be useful for preparation and structural analysis of the linkage oligosaccharides.  (+info)

Sulfate incorporation from ascorbate 2-sulfate into chondroitin sulfate by embryonic chick cartilage epiphyses. (3/149)

Radioactivity was significantly incorporated from ascorbate 2-[35S]sulfate into chondroitin sulfate by embryonic chick cartilage epiphyses. The extent of incorporation was comparable with that from inorganic [35S]sulfate. The radioactive chondroitin sulfate formed from ascorbate 2-[35S]sulfate gave two radioactive disaccharides on chondroitinase-ABC [EC 4.2.2.4] digestion. The incorporation was markedly decreased by inorganic sulfate. The time course of incorporation from ascorbate 2-[35S]sulfate and inorganic [35S]sulfate into chondroitin sulfate and the constituent disaccharides suggest that the incorporation rates from the two radioactive substances are different.  (+info)

Sulphation heterogeneity in the trisaccharide (GalNAcSbeta1, 4GlcAbeta1,3GalNAcS) isolated from the non-reducing terminal of human aggrecan chondroitin sulphate. (4/149)

We report here the isolation and sulphation isomer analyses of trisaccharides GalNAcS(beta1,4)GlcA(beta1,3)GalNAcS (in which S indicates sulphate) derived from the non-reducing termini of aggrecan chondroitin sulphate. Rat chondrosarcoma and human aggrecans were digested for 1 h at 37 degrees C with 30 micro-units of endo-chondroitinase ABC per microgram of chondroitin sulphate, and trisaccharides were isolated from the digests by ToyoPearl HW40S gel-filtration chromatography. Four trisaccharide species were identified; their sulphation isomer compositions, as determined by digestion with chondroitinase ACII and fluorescence-based ion-exchange HPLC, were GalNAc4Sbeta1,4GlcAbeta1,3GalNAc4S, GalNAc4Sbeta1,4GlcAbeta1,3GalNAc6S, GalNAc4,6Sbeta1,4GlcAbeta1, 3GalNAc4S and GalNAc4,6Sbeta1,4GlcAbeta1,3GalNAc6S. The abundances of such sequences in chondroitin sulphate on aggrecan from normal (foetal to 72 years of age) and from osteoarthritic human knee cartilages were also established. The results showed that non-reducing terminal GalNAc4S or GalNAc4,6S can be linked to either a 4-sulphated or a 6-sulphated disaccharide, suggesting that the sulphation of the last disaccharide might not have a direct effect on the specificity of chondroitin sulphate terminal GalNAc sulphotransferases. Furthermore, for each aggrecan preparation examined, the 4S-to-6S ratio of all chain interior disaccharides was equivalent to that in the last repeating disaccharides at the non-reducing terminus, suggesting that neither chondroitin 4-sulphotransferase nor chondroitin 6-sulphotransferase shows preferential activity near the chain terminus.  (+info)

Isolation and expression in Escherichia coli of cslA and cslB, genes coding for the chondroitin sulfate-degrading enzymes chondroitinase AC and chondroitinase B, respectively, from Flavobacterium heparinum. (5/149)

In medium supplemented with chondroitin sulfate, Flavobacterium heparinum synthesizes and exports two chondroitinases, chondroitinase AC (chondroitin AC lyase; EC 4.2.2.5) and chondroitinase B (chondroitin B lyase; no EC number), into its periplasmic space. Chondroitinase AC preferentially depolymerizes chondroitin sulfates A and C, whereas chondroitinase B degrades only dermatan sulfate (chondroitin sulfate B). The genes coding for both enzymes were isolated from F. heparinum and designated cslA (chondroitinase AC) and cslB (chondroitinase B). They were found to be separated by 5.5 kb on the chromosome of F. heparinum, transcribed in the same orientation, but not linked to any of the heparinase genes. In addition, the synthesis of both enzymes appeared to be coregulated. The cslA and cslB DNA sequences revealed open reading frames of 2,103 and 1,521 bp coding for peptides of 700 and 506 amino acid residues, respectively. Chondroitinase AC has a signal sequence of 22 residues, while chondroitinase B is composed of 25 residues. The mature forms of chondroitinases AC and B are comprised of 678 and 481 amino acid residues and have calculated molecular masses of 77,169 and 53,563 Da, respectively. Truncated cslA and cslB genes have been used to produce active, mature chondroitinases in the cytoplasm of Escherichia coli. Partially purified recombinant chondroitinases AC and B exhibit specific activities similar to those of chondroitinases AC and B from F. heparinum.  (+info)

A fingerprinting method for chondroitin/dermatan sulfate and hyaluronan oligosaccharides. (6/149)

A previously published method for the analysis of glycosaminoglycan disaccharides by high pH anion exchange chromatography (Midura,R.J., Salustri,A., Calabro,A., Yanagishita,M. and Hascall,V.C. (1994), Glycobiology,4, 333-342) has been modified and calibrated for chondroitin and dermatan sulfate oligosaccharides up to hexasaccharide in size and hyaluronan oligosaccharides up to hexadecasaccharide. For hyaluronan oligosaccharides chain length controls elution position; however, for chondroitin and dermatan sulfate oligosaccharides elution times primarily depend upon the level of sulfation, although chain length and hence charge density plays a role. The sulfation position of GalNAc residues within an oligosaccharide is also important in determining its elution position. Compared to 4-sulfation a reducing terminal 6-sulfate retards elution; however, when present on an internal GalNAc residue it is the 4-sulfate containing oligosaccharide which elutes later. These effects allow discrimination between oligosaccharides differing only in the position of GalNAc sulfation. Using this simple methodology, a Dionex CarboPac PA-1 column with NaOH/NaCl eluents and detection by absorbance at 232 nm, a quantitative analytical fingerprint of a chondroitin/dermatan sulfate chain may be obtained, allowing a determination of the abundance of chondroitin sulfate, dermatan sulfate, and hyaluronan along with an analysis of structural features with a linear response to approximately 0.1 nmol. The method may readily be calibrated using either commercial disaccharides or the di- and tetrasaccharide products of a limit digest of commercial chondroitin sulfate by chondroitin ABC endolyase. Commercially available and freshly prepared shark, whale, bovine, and human cartilage chondroitin sulfates have been examined by this methodology and we have confirmed that freshly isolated shark cartilage CS contains significant amounts of the biologically important GlcA2Sbeta(1-3)GalNAc6S structure.  (+info)

Iduronic acid-containing glycosaminoglycans on target cells are required for efficient respiratory syncytial virus infection. (7/149)

Respiratory syncytial virus (RSV) is an important human respiratory pathogen, particularly in infants. Glycosaminoglycans (GAGs) have been implicated in the initiation of RSV infection of cultured cells, but it is not clear what type of GAGs and GAG components are involved, whether the important GAGs are on the virus or the cell, or what the magnitude is of their contribution to infection. We constructed and rescued a recombinant green fluorescent protein (GFP)-expressing RSV (rgRSV) and used this virus to develop a sensitive system to assess and quantify infection by flow cytometry. Evaluation of a panel of mutant Chinese hamster ovary cell lines that are genetically deficient in various aspects of GAG synthesis showed that infection was reduced up to 80% depending on the type of GAG deficiency. Enzymatic removal of heparan sulfate and/or chondroitin sulfate from the surface of HEp-2 cells also reduced infection, and the removal of both reduced infection even further. Blocking experiments in which RSV was preincubated with various soluble GAGs revealed the relative blocking order of: heparin > heparan sulfate > chondroitin sulfate B. Iduronic acid is a component common to these GAGs. GAGs that do not contain iduronic acid, namely, chondroitin sulfate A and C and hyaluronic acid, did not inhibit infection. A role for iduronic acid-containing GAGs in RSV infection was confirmed by the ability of basic fibroblast growth factor to block infection, because basic fibroblast growth factor binds to GAGs containing iduronic acid. Pretreatment of cells with protamine sulfate, which binds and blocks GAGs, also reduced infection. In these examples, infection was reduced by pretreatment of the virus with soluble GAGs, pretreatment of the cells with GAG-binding molecules, pretreatment of the cells with GAG-destroying enzymes or in cells genetically deficient in GAGs. These results establish that the GAGs involved in RSV infection are present on the cell rather than on the virus particle. Thus, the presence of cell surface GAGs containing iduronic acid, like heparan sulfate and chondroitin sulfate B, is required for efficient RSV infection in cell culture.  (+info)

Distribution of sulfated glycosaminoglycans in the animal kingdom: widespread occurrence of heparin-like compounds in invertebrates. (8/149)

Sulfated glycosaminoglycans were isolated from 23 species of 13 phyla of invertebrates and characterized by their electrophoretic migration in three different buffer systems coupled with enzymatic degradation using bacterial heparinase, heparitinases and chondroitinase AC. Heparan sulfate is a ubiquitous compound present in all species analyzed whereas chondroitin sulfate was present in 20 species and heparin-like compounds in 12 species of the invertebrates. The heparin-like compounds were purified from the echinoderm Mellita quinquisperforata (sand dollar) and the crustacean Ucides cordatus (crab) with anticoagulant activities of 60 and 52 IU/mg, respectively. Degradation of these heparins with heparinase produced significant amounts of the trisulfated disaccharide typical of mammalian heparins. This was confirmed by 13C-NMR spectroscopy of the crab heparin. An updated phylogenetic tree of the distribution of sulfated glycosaminoglycans in the animal kingdom is also presented.  (+info)

Chondroitin lyases are a group of enzymes that breakdown chondroitin, which is a type of proteoglycan found in connective tissues such as cartilage. These enzymes cleave chondroitin at specific points by removing certain sugar units, thereby breaking down the large, complex molecule into smaller fragments. Chondroitin lyases are classified based on their site of action and the type of fragment they produce. They play important roles in various biological processes, including tissue remodeling, growth, and development. In some cases, chondroitin lyases may also be used in research and medical settings to study the structure and function of proteoglycans or for the production of smaller chondroitin fragments with therapeutic potential.

Chondroitinases and chondroitin lyases are enzymes that break down chondroitin sulfate, a type of glycosaminoglycan (GAG) found in connective tissues such as cartilage. Glycosaminoglycans are long, unbranched polysaccharides made up of repeating disaccharide units. In the case of chondroitin sulfate, the disaccharide unit consists of a glucuronic acid residue and a N-acetylgalactosamine residue that may be sulfated at various positions.

Chondroitinases are enzymes that cleave the linkage between the two sugars in the chondroitin sulfate chain, specifically between the carbon atom in the fourth position of the glucuronic acid and the nitrogen atom in the first position of the N-acetylgalactosamine. This results in the formation of unsaturated disaccharides. Chondroitinases are produced by certain bacteria and are used in research to study the structure and function of chondroitin sulfate and other GAGs.

Chondroitin lyases, on the other hand, are enzymes that cleave the same linkage but in the opposite direction, resulting in the formation of 4,5-unsaturated disaccharides. Chondroitin lyases are also produced by certain bacteria and are used in research to study the structure and function of chondroitin sulfate and other GAGs.

It is important to note that while both chondroitinases and chondroitin lyases break down chondroitin sulfate, they do so through different mechanisms and produce different products.

Bacteroides are a genus of gram-negative, anaerobic, rod-shaped bacteria that are normally present in the human gastrointestinal tract. They are part of the normal gut microbiota and play an important role in breaking down complex carbohydrates and other substances in the gut. However, some species of Bacteroides can cause opportunistic infections, particularly in individuals with weakened immune systems or when they spread to other parts of the body. They are resistant to many commonly used antibiotics, making infections caused by these bacteria difficult to treat.

Chondroitin sulfates are a type of complex carbohydrate molecules known as glycosaminoglycans (GAGs). They are a major component of cartilage, the tissue that cushions and protects the ends of bones in joints. Chondroitin sulfates are composed of repeating disaccharide units made up of glucuronic acid and N-acetylgalactosamine, which can be sulfated at various positions.

Chondroitin sulfates play a crucial role in the biomechanical properties of cartilage by attracting water and maintaining the resiliency and elasticity of the tissue. They also interact with other molecules in the extracellular matrix, such as collagen and proteoglycans, to form a complex network that provides structural support and regulates cell behavior.

Chondroitin sulfates have been studied for their potential therapeutic benefits in osteoarthritis, a degenerative joint disease characterized by the breakdown of cartilage. Supplementation with chondroitin sulfate has been shown to reduce pain and improve joint function in some studies, although the evidence is not consistent across all trials. The mechanism of action is thought to involve inhibition of enzymes that break down cartilage, as well as stimulation of cartilage repair and synthesis.

Chondroitin is a type of molecule known as a glycosaminoglycan, which is found in the connective tissues of the body, including cartilage. It is a major component of proteoglycans, which are complex molecules that provide structural support and help retain water within the cartilage, allowing it to function as a cushion between joints.

Chondroitin sulfate, a form of chondroitin, is commonly used in dietary supplements for osteoarthritis, a condition characterized by the breakdown of cartilage in joints. The idea behind using chondroitin sulfate as a treatment for osteoarthritis is that it may help to rebuild damaged cartilage and reduce inflammation in the affected joints. However, research on the effectiveness of chondroitin sulfate for osteoarthritis has had mixed results, with some studies showing modest benefits while others have found no significant effects.

It's important to note that dietary supplements containing chondroitin are not regulated by the U.S. Food and Drug Administration (FDA) in the same way that drugs are, so the quality and purity of these products can vary widely. As with any supplement, it's a good idea to talk to your doctor before starting to take chondroitin, especially if you have any medical conditions or are taking other medications.

Chondroitin sulfate proteoglycans (CSPGs) are complex molecules found in the extracellular matrix of various connective tissues, including cartilage. They are composed of a core protein covalently linked to one or more glycosaminoglycan (GAG) chains, such as chondroitin sulfate and dermatan sulfate.

CSPGs play important roles in the structure and function of tissues, including:

1. Regulating water content and providing resilience to tissues due to their high negative charge, which attracts cations and bound water molecules.
2. Interacting with other matrix components, such as collagen and elastin, to form a highly organized network that provides tensile strength and elasticity.
3. Modulating cell behavior by interacting with various growth factors, cytokines, and cell surface receptors, thereby influencing processes like cell adhesion, proliferation, differentiation, and migration.
4. Contributing to the maintenance of the extracellular matrix homeostasis through their involvement in matrix turnover and remodeling.

In articular cartilage, CSPGs are particularly abundant and contribute significantly to its load-bearing capacity and overall health. Dysregulation of CSPGs has been implicated in various pathological conditions, such as osteoarthritis, where altered proteoglycan composition and content can lead to cartilage degradation and joint dysfunction.

A lyase is a type of enzyme that catalyzes the breaking of various chemical bonds in a molecule, often resulting in the formation of two new molecules. Lyases differ from other types of enzymes, such as hydrolases and oxidoreductases, because they create double bonds or rings as part of their reaction mechanism.

In the context of medical terminology, lyases are not typically discussed on their own, but rather as a type of enzyme that can be involved in various biochemical reactions within the body. For example, certain lyases play a role in the metabolism of carbohydrates, lipids, and amino acids, among other molecules.

One specific medical application of lyase enzymes is in the diagnosis of certain genetic disorders. For instance, individuals with hereditary fructose intolerance (HFI) lack the enzyme aldolase B, which is a type of lyase that helps break down fructose in the liver. By measuring the activity of aldolase B in a patient's blood or tissue sample, doctors can diagnose HFI and recommend appropriate dietary restrictions to manage the condition.

Overall, while lyases are not a medical diagnosis or condition themselves, they play important roles in various biochemical processes within the body and can be useful in the diagnosis of certain genetic disorders.

Chondroitin ABC lyase, also known as chondroitinase ABC or chondroitin sulfate eliminase, is an enzyme that breaks down chondroitin sulfate proteoglycans (CSPGs), which are major components of the extracellular matrix in various tissues including cartilage. CSPGs contain chondroitin sulfate chains, which are long, negatively charged polysaccharides composed of alternating sugars (N-acetylgalactosamine and glucuronic acid) with sulfate groups attached at specific positions.

Chondroitin ABC lyase cleaves chondroitin sulfate chains by removing a disaccharide unit from the polymer, resulting in the formation of unsaturated bonds between the remaining sugars. This enzymatic activity has been used in research to study the structure and function of CSPGs and their role in various biological processes, such as cell migration, tissue repair, and neural plasticity. Additionally, chondroitin ABC lyase has potential therapeutic applications for treating conditions associated with excessive accumulation of CSPGs, such as fibrosis and some neurological disorders.

Glycosaminoglycans (GAGs) are long, unbranched polysaccharides composed of repeating disaccharide units. They are a major component of the extracellular matrix and connective tissues in the body. GAGs are negatively charged due to the presence of sulfate and carboxyl groups, which allows them to attract positively charged ions and water molecules, contributing to their ability to retain moisture and maintain tissue hydration and elasticity.

GAGs can be categorized into four main groups: heparin/heparan sulfate, chondroitin sulfate/dermatan sulfate, keratan sulfate, and hyaluronic acid. These different types of GAGs have varying structures and functions in the body, including roles in cell signaling, inflammation, and protection against enzymatic degradation.

Heparin is a highly sulfated form of heparan sulfate that is found in mast cells and has anticoagulant properties. Chondroitin sulfate and dermatan sulfate are commonly found in cartilage and contribute to its resiliency and ability to withstand compressive forces. Keratan sulfate is found in corneas, cartilage, and bone, where it plays a role in maintaining the structure and function of these tissues. Hyaluronic acid is a large, nonsulfated GAG that is widely distributed throughout the body, including in synovial fluid, where it provides lubrication and shock absorption for joints.

Dermatan sulfate is a type of glycosaminoglycan, which is a long, unbranched sugar chain found on the proteoglycan core protein in the extracellular matrix of animal tissues. It is composed of repeating disaccharide units of iduronic acid and N-acetylgalactosamine, with alternating sulfation at the 4-position of the iduronic acid and the 6-position of the galactosamine.

Dermatan sulfate is found in various tissues, including skin, heart valves, and blood vessels, where it plays important roles in regulating cell behavior, tissue development, and homeostasis. It also binds to a variety of growth factors, cytokines, and enzymes, modulating their activities and contributing to the regulation of various biological processes.

Abnormalities in dermatan sulfate metabolism can lead to several genetic disorders, such as Hunter syndrome and Hurler-Scheie syndrome, which are characterized by skeletal abnormalities, cardiac defects, and neurological impairment.

Proteoglycans are complex, highly negatively charged macromolecules that are composed of a core protein covalently linked to one or more glycosaminoglycan (GAG) chains. They are a major component of the extracellular matrix (ECM) and play crucial roles in various biological processes, including cell signaling, regulation of growth factor activity, and maintenance of tissue structure and function.

The GAG chains, which can vary in length and composition, are long, unbranched polysaccharides that are composed of repeating disaccharide units containing a hexuronic acid (either glucuronic or iduronic acid) and a hexosamine (either N-acetylglucosamine or N-acetylgalactosamine). These GAG chains can be sulfated to varying degrees, which contributes to the negative charge of proteoglycans.

Proteoglycans are classified into four major groups based on their core protein structure and GAG composition: heparan sulfate/heparin proteoglycans, chondroitin/dermatan sulfate proteoglycans, keratan sulfate proteoglycans, and hyaluronan-binding proteoglycans. Each group has distinct functions and is found in specific tissues and cell types.

In summary, proteoglycans are complex macromolecules composed of a core protein and one or more GAG chains that play important roles in the ECM and various biological processes, including cell signaling, growth factor regulation, and tissue structure maintenance.

Disaccharides are a type of carbohydrate that is made up of two monosaccharide units bonded together. Monosaccharides are simple sugars, such as glucose, fructose, or galactose. When two monosaccharides are joined together through a condensation reaction, they form a disaccharide.

The most common disaccharides include:

* Sucrose (table sugar), which is composed of one glucose molecule and one fructose molecule.
* Lactose (milk sugar), which is composed of one glucose molecule and one galactose molecule.
* Maltose (malt sugar), which is composed of two glucose molecules.

Disaccharides are broken down into their component monosaccharides during digestion by enzymes called disaccharidases, which are located in the brush border of the small intestine. These enzymes catalyze the hydrolysis of the glycosidic bond that links the two monosaccharides together, releasing them to be absorbed into the bloodstream and used for energy.

Disorders of disaccharide digestion and absorption can lead to various symptoms, such as bloating, diarrhea, and abdominal pain. For example, lactose intolerance is a common condition in which individuals lack sufficient levels of the enzyme lactase, leading to an inability to properly digest lactose and resulting in gastrointestinal symptoms.

Oligosaccharides are complex carbohydrates composed of relatively small numbers (3-10) of monosaccharide units joined together by glycosidic linkages. They occur naturally in foods such as milk, fruits, vegetables, and legumes. In the body, oligosaccharides play important roles in various biological processes, including cell recognition, signaling, and protection against pathogens.

There are several types of oligosaccharides, classified based on their structures and functions. Some common examples include:

1. Disaccharides: These consist of two monosaccharide units, such as sucrose (glucose + fructose), lactose (glucose + galactose), and maltose (glucose + glucose).
2. Trisaccharides: These contain three monosaccharide units, like maltotriose (glucose + glucose + glucose) and raffinose (galactose + glucose + fructose).
3. Oligosaccharides found in human milk: Human milk contains unique oligosaccharides that serve as prebiotics, promoting the growth of beneficial bacteria in the gut. These oligosaccharides also help protect infants from pathogens by acting as decoy receptors and inhibiting bacterial adhesion to intestinal cells.
4. N-linked and O-linked glycans: These are oligosaccharides attached to proteins in the body, playing crucial roles in protein folding, stability, and function.
5. Plant-derived oligosaccharides: Fructooligosaccharides (FOS) and galactooligosaccharides (GOS) are examples of plant-derived oligosaccharides that serve as prebiotics, promoting the growth of beneficial gut bacteria.

Overall, oligosaccharides have significant impacts on human health and disease, particularly in relation to gastrointestinal function, immunity, and inflammation.

Nanospheres are defined in the medical context as tiny, spherical particles that have a diameter in the nanometer range (typically between 1 to 1000 nm). They can be made up of various materials such as polymers, lipids, metals or ceramics. Nanospheres have unique properties due to their small size and large surface area, making them useful for a variety of medical applications including drug delivery, diagnostic imaging, and tissue engineering.

In the field of drug delivery, nanospheres can be used to encapsulate drugs and deliver them to specific sites in the body, improving the efficacy and safety of treatments. They can also be designed to target certain cell types or release their cargo in response to specific stimuli. Additionally, nanospheres can be used as contrast agents for medical imaging techniques such as magnetic resonance imaging (MRI) and computed tomography (CT).

Overall, nanospheres are a promising tool in the development of new medical technologies and therapies.

Spinal cord injuries (SCI) refer to damage to the spinal cord that results in a loss of function, such as mobility or feeling. This injury can be caused by direct trauma to the spine or by indirect damage resulting from disease or degeneration of surrounding bones, tissues, or blood vessels. The location and severity of the injury on the spinal cord will determine which parts of the body are affected and to what extent.

The effects of SCI can range from mild sensory changes to severe paralysis, including loss of motor function, autonomic dysfunction, and possible changes in sensation, strength, and reflexes below the level of injury. These injuries are typically classified as complete or incomplete, depending on whether there is any remaining function below the level of injury.

Immediate medical attention is crucial for spinal cord injuries to prevent further damage and improve the chances of recovery. Treatment usually involves immobilization of the spine, medications to reduce swelling and pressure, surgery to stabilize the spine, and rehabilitation to help regain lost function. Despite advances in treatment, SCI can have a significant impact on a person's quality of life and ability to perform daily activities.

Microspheres are tiny, spherical particles that range in size from 1 to 1000 micrometers in diameter. They are made of biocompatible and biodegradable materials such as polymers, glass, or ceramics. In medical terms, microspheres have various applications, including drug delivery systems, medical imaging, and tissue engineering.

In drug delivery, microspheres can be used to encapsulate drugs and release them slowly over time, improving the efficacy of the treatment while reducing side effects. They can also be used for targeted drug delivery, where the microspheres are designed to accumulate in specific tissues or organs.

In medical imaging, microspheres can be labeled with radioactive isotopes or magnetic materials and used as contrast agents to enhance the visibility of tissues or organs during imaging procedures such as X-ray, CT, MRI, or PET scans.

In tissue engineering, microspheres can serve as a scaffold for cell growth and differentiation, promoting the regeneration of damaged tissues or organs. Overall, microspheres have great potential in various medical applications due to their unique properties and versatility.

Polyglycolic acid (PGA) is a synthetic polymer of glycolic acid, which is commonly used in surgical sutures. It is a biodegradable material that degrades in the body through hydrolysis into glycolic acid, which can be metabolized and eliminated from the body. PGA sutures are often used for approximating tissue during surgical procedures due to their strength, handling properties, and predictable rate of absorption. The degradation time of PGA sutures is typically around 60-90 days, depending on factors such as the size and location of the suture.

The spinal cord is a major part of the nervous system, extending from the brainstem and continuing down to the lower back. It is a slender, tubular bundle of nerve fibers (axons) and support cells (glial cells) that carries signals between the brain and the rest of the body. The spinal cord primarily serves as a conduit for motor information, which travels from the brain to the muscles, and sensory information, which travels from the body to the brain. It also contains neurons that can independently process and respond to information within the spinal cord without direct input from the brain.

The spinal cord is protected by the bony vertebral column (spine) and is divided into 31 segments: 8 cervical, 12 thoracic, 5 lumbar, 5 sacral, and 1 coccygeal. Each segment corresponds to a specific region of the body and gives rise to pairs of spinal nerves that exit through the intervertebral foramina at each level.

The spinal cord is responsible for several vital functions, including:

1. Reflexes: Simple reflex actions, such as the withdrawal reflex when touching a hot surface, are mediated by the spinal cord without involving the brain.
2. Muscle control: The spinal cord carries motor signals from the brain to the muscles, enabling voluntary movement and muscle tone regulation.
3. Sensory perception: The spinal cord transmits sensory information, such as touch, temperature, pain, and vibration, from the body to the brain for processing and awareness.
4. Autonomic functions: The sympathetic and parasympathetic divisions of the autonomic nervous system originate in the thoracolumbar and sacral regions of the spinal cord, respectively, controlling involuntary physiological responses like heart rate, blood pressure, digestion, and respiration.

Damage to the spinal cord can result in various degrees of paralysis or loss of sensation below the level of injury, depending on the severity and location of the damage.

Bacterial processes refer to the various metabolic and cellular activities that bacteria carry out to survive, grow, and reproduce. These processes include:

1. Metabolism: Bacteria use different types of metabolic pathways to break down organic matter and obtain energy for growth and reproduction. Some bacteria are aerobic, requiring oxygen to carry out their metabolic processes, while others are anaerobic and cannot tolerate oxygen.
2. Cell division: Bacteria reproduce asexually by dividing into two identical daughter cells through a process called binary fission. This process involves the replication of bacterial DNA and the separation of the resulting chromosomes into two new cells.
3. Protein synthesis: Bacteria produce proteins using their own genetic material, which is encoded in their DNA. They use ribosomes to translate genetic information into proteins that are necessary for various cellular functions.
4. Cell wall biosynthesis: Bacteria have a unique cell wall made of peptidoglycan, which provides structural support and protection. The synthesis of the cell wall involves several enzymes and complex biochemical pathways.
5. Motility: Some bacteria are motile and can move around in their environment using flagella or other structures. This movement allows them to seek out nutrients and avoid harmful substances.
6. Quorum sensing: Bacteria can communicate with each other through a process called quorum sensing, which involves the release and detection of signaling molecules. This communication helps bacteria coordinate their behavior and respond to changes in their environment.
7. Antibiotic resistance: Bacteria have developed various mechanisms to resist antibiotics, including enzymatic degradation, efflux pumps, and target modification. These processes can make bacterial infections more difficult to treat and pose a significant public health threat.

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 U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (Wikipedia ... with systematic name chondroitin ABC lyase. This enzyme catalyses the following chemical reaction Eliminative degradation of ... chondroitin 6-sulfate and dermatan sulfate. Following a spinal cord injury, this enzyme can be used to erode scar tissue that ...
Crystal structure of the Arthrobacter aurescens chondroitin AC lyase ... Chondroitin lyase AC from Arthrobacter aurescens (ArthroAC) is known to act on chondroitin 4-sulfate and chondroitin 6-sulfate ... Chondroitin lyase AC from Arthrobacter aurescens (ArthroAC) is known to act on chondroitin 4-sulfate and chondroitin 6-sulfate ... Like other chondroitin AC lyases, it is capable of cleaving hyaluronan. We have determined the three-dimensional crystal ...
... correlating with altered PNN-associated sulfation patterns of chondroitin sulfate glycosaminoglycans in the MBH. Each of these ... Two distinct chondroitin sulfate ABC lyases. An endoeliminase yielding tetrasaccharides and an exoeliminase preferentially ... Chondroitin 6-sulphate synthesis is upregulated in injured CNS, induced by injury-related cytokines and enhanced in axon-growth ... Quantitative analysis of chondroitin sulfate disaccharides from human and rodent fixed brain tissue by electrospray ionization- ...
Active site of chondroitin AC lyase revealed by the structure of enzyme-oligosaccharide complexes and mutagenesis ... Active site of chondroitin AC lyase revealed by the structure of enzyme-oligosaccharide complexes and mutagenesis. DOI. Resolve ... Active site of chondroitin AC lyase revealed by the structure of enzyme-oligosaccharide complexes and mutagenesis. From ...
The structure of Chondroitin B Lyase Complexed with Glycosaminoglycan Oligosaccharides Unravels a Calcium-Dependent Catalytic ... The structure of Chondroitin B Lyase Complexed with Glycosaminoglycan Oligosaccharides Unravels a Calcium-Dependent Catalytic ... The structure of Chondroitin B Lyase Complexed with Glycosaminoglycan Oligosaccharides Unravels a Calcium-Dependent Catalytic ...
Polysaccharide Lyase Family 23 Activities in Family. chondroitin lyase (EC 4.2.2.-); ... Glycoside Hydrolases GlycosylTransferases Polysaccharide Lyases Carbohydrate Esterases Auxiliary Activities Carbohydrate- ...
... chondroitin ABC lyase and heparinase III, produced an even greater enhancement in retinal transduction. Chondroitin ABC lyase ... Collagenase, hyaluronan lyase, chondroitin ABC lyase, and heparinase III were coinjected with AAV2.CBA.eGFP and retinal ... hyaluronan lyase from Streptomyces (E.C. 4.2.2.1), which has a high specificity for hyaluronan; Chondroitin ABC lyase (E.C. 4.2 ... but chondroitin ABC lyase, heparinase III and, to a lesser extent, hyaluronan lyase increased expression of the viral reporter ...
Chondroitin Lyase from a Marine Arthrobacter sp. MAT3885 for the Production of Chondroitin Sulfate Disaccharides. Marine ... Chondroitin Lyase from a Marine Arthrobacter sp. MAT3885 for the Production of Chondroitin Sulfate Disaccharides - (2015). ... Erindi 47: Cloning and expression of a chondroitin lyase gene from the marine bacterium Arthrobacter MAT3885 and ... Enzymatic depolymerization of alginate by two novel thermostable alginate lyases from Rhodothermus marinus - (2022). Front. ...
Chondroitin lyase 1 * Circular dichroism 1 * Collision induced dissociation 1 * Complement factor H-related protein 1 ... The chondroitin sulfate/dermatan sulfate 4-O-endosulfatase from marine bacterium Vibrio sp FC509 is a dimeric species: ... Discrimination of sulfated isomers of chondroitin sulfate disaccharides by HILIC-MS. Salomé Poyer , Ilham Seffouh , Chrystel ... Investigation of Action Pattern of a Novel Chondroitin Sulfate/Dermatan Sulfate 4- O -Endosulfatase. Wenshuang Wang , Cédric ...
Chondroitin ABC Lyase Medicine & Life Sciences 100% * Nanospheres Medicine & Life Sciences 99% ...
Purification, Characterization and Specificity of Chondroitin Lyases and Glucuronidase from Flavobacterium heparinum  Gu, K.; ... The chondroitin lyases from Flavobacterium heparinum (Cytophaga heparinia) have been widely used in depolymerization of ... Purification and Characterization of Heparin Lyases from Flavobacterium heparinum  Lohse, D.L.; Linhardt, Robert J. (Elsevier ... Quantitative Analysis of Chondroitin Sulfate in Raw Materials, Ophthalmic Solutions, Soft Capsules and Liquid Preparations  ...
Liquid Chromatography-Mass Spectrometry to Study Chondroitin Lyase Action Pattern  Zhang, Zhenqing; Park, Youmie; Kemp, ... Liquid chromatography-mass spectrometry was applied to determine the action pattern of different chondroitin lyases. Two ...
Chondroitin ABC Lyase Medicine & Life Sciences 100% * Glial Cell Line-Derived Neurotrophic Factor Medicine & Life Sciences 88% ...
Chondroitin AC/alginate lyase. 4fnvA01. 2.70.98.70. Mainly Beta. Distorted Sandwich. Beta-galactosidase; Chain A, domain 5. ...
Chondroitin ABC Lyase 100% * Copolymers 79% * Regeneration 56% * Copolymer 44% * Proteoglycans 28% ...
chondroitin B lyase activity GO:0033999 * bis(5\-nucleosyl)-tetraphosphatase (symmetrical) activity ...
chondroitin abc lyase (1) * chondroitin sulfates (1) * heparin (1) * immunoglobulin g (1) ...
Chondroitinases and Chondroitin Lyases 100% * Chondroitin ABC Lyase 92% * Nerve Tissue 70% ...
Active Site of Chondroitin AC Lyase Revealed by the Structure of Enzyme-Oligosaccharide Complexes and Mutagenesis. Weijun Huang ...
Composite active site of chondroitin lyase ABC accepting both epimers of uronic acid 9 ... Composite active site of chondroitin lyase ABC accepting both epimers of uronic acid ...
NMR and UV spectroscopic assays revealed that it encodes a novel polysaccharide lyase (PL), hereafter referred to as BtCDH, ... Here, we investigated a gene of unknown function (BT_3328) from the chondroitin sulfate (CS) utilization locus of B. ... and we therefore propose that it represents the founding member of a new polysaccharide lyase family (PL29). The current ... hyaluronan hyaluronate lyase carbohydrate metabolism bacterial metabolism cell surface enzyme glycosaminoglycan degradation ...
A variety of bacterial chondroitin sulfate (CS) lyases have been identified, and have been widely used as catalysts in this ... Here, we identified a putative chondroitin AC exolyase gene, AschnAC, from an Arthrobacter sp. strain found in a CS ... Cloning and Characterization of a Chondroitin AC Exolyase from Arthrobacter sp. SD-04. ... coli while maintaining chondroitin AC exolyase activity. This novel catalyst exhibited its optimal activity in the absence of ...
Pronase and Proteus vulgaris chondroitin sulphate lyase. Treatment of this preparation with alkali cleaved a glycosidic bond ... Pronase and Proteus vulgaris chondroitin sulphate lyase. Treatment of this preparation with alkali cleaved a glycosidic bond ... Pronase and Proteus vulgaris chondroitin sulphate lyase. Treatment of this preparation with alkali cleaved a glycosidic bond ... Pronase and Proteus vulgaris chondroitin sulphate lyase. Treatment of this preparation with alkali cleaved a glycosidic bond ...
chondroitin-sulfate-ABC exolyase activity GO:0034001 * fatty acid in-chain hydroxylase activity ...
Based on docking studies and molecular dynamics simulations of the protein structure and a chondroitin substrate, we suggest a ... structure of DS-epi1 reveals a high structural similarity to proteins from several families of bacterial polysaccharide lyases ...
Digestion of the CS proteoglycan with chondroitinase ABC lyase, followed by SDS/PAGE, yielded a protein core of 600 to 700 kDa ... and was substituted with 15-20 chondroitin sulphate (CS) chains (Mr 60000-65000). Half of the CS disaccharides were 6-sulphated ...
Chondroitin ABC Lyase. *Chondroitin Sulfate Proteoglycans. *Chronic Pain. *Clinical Competence. *Clinical Laboratory Techniques ...
For each cotransport ribosome a effective DNA chondroitin increases suspected along with codon as to the collagen of that % in ... removes annotated for transducer composting Chemiosmotic components or hormones in the Editions misalignment gamma-lyase. No ... and that Chondroitin enables induced thus, with cytidine and infections to transcription Canadians tested as mice to ...
"Inactivation of ATP citrate lyase by Cucurbitacin B: A bioactive compound from cucumber, inhibits prostate cancer growth" ... "Effectiveness of Cucumis sativus extract versus glucosamine-chondroitin in the management of moderate osteoarthritis: a ...

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