Proteoglycans consisting of proteins linked to one or more CHONDROITIN SULFATE-containing oligosaccharide chains.
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.
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.
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)
A mucopolysaccharide constituent of chondrin. (Grant & Hackh's Chemical Dictionary, 5th ed)
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.-.
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 BRAIN-specific hyalectin that may play a role in terminally differentiating NEURONS. It is found highly overexpressed in primary BRAIN TUMORS and in experimental models of GLIOMA.
A heteropolysaccharide that is similar in structure to HEPARIN. It accumulates in individuals with MUCOPOLYSACCHARIDOSIS.
HYALURONAN-containing proteoglycans found in the EXTRACELLULAR MATRIX of a variety of tissues and organs. Several versican isoforms exist due to multiple ALTERNATIVE SPLICING of the versican MESSENGER RNA.
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.
A subclass of receptor-like protein tryosine phosphatases that contain an extracellular fibronectin III-like domain along with a carbonic anhydrase-like domain.
Large HYALURONAN-containing proteoglycans found in articular cartilage (CARTILAGE, ARTICULAR). They form into aggregates that provide tissues with the capacity to resist high compressive and tensile forces.
Inorganic salts of sulfuric acid.
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)
A hyalectin family member that is expressed in neuronal tissue and plays a role in neuronal CELL ADHESION.
A class of animal lectins that bind to carbohydrate in a calcium-dependent manner. They share a common carbohydrate-binding domain that is structurally distinct from other classes of lectins.
Macromolecular organic compounds that contain carbon, hydrogen, oxygen, nitrogen, and usually, sulfur. These macromolecules (proteins) form an intricate meshwork in which cells are embedded to construct tissues. Variations in the relative types of macromolecules and their organization determine the type of extracellular matrix, each adapted to the functional requirements of the tissue. The two main classes of macromolecules that form the extracellular matrix are: glycosaminoglycans, usually linked to proteins (proteoglycans), and fibrous proteins (e.g., COLLAGEN; ELASTIN; FIBRONECTINS; and LAMININ).
Cell surface receptors that bind to ACETYLGLUCOSAMINE.
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.
Renewal or physiological repair of damaged nerve tissue.
Nerve fibers that are capable of rapidly conducting impulses away from the neuron cell body.
Oligosaccharides containing two monosaccharide units linked by a glycosidic bond.
A highly acidic mucopolysaccharide formed of equal parts of sulfated D-glucosamine and D-glucuronic acid with sulfaminic bridges. The molecular weight ranges from six to twenty thousand. Heparin occurs in and is obtained from liver, lung, mast cells, etc., of vertebrates. Its function is unknown, but it is used to prevent blood clotting in vivo and vitro, in the form of many different salts.
A family of transmembrane glycoproteins that contain a short cytoplasmic domain, a single-span transmembrane domain, and an extracellular domain with heparin sulfate and CHONDROITIN SULFATE chains. Syndecans interact with a variety of heparin-binding INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS and may play a role in modulating cellular signaling during EMBRYONIC DEVELOPMENT, tumorigenesis, and angiogenesis.
A group of carbon-oxygen lyases. These enzymes catalyze the breakage of a carbon-oxygen bond in polysaccharides leading to an unsaturated product and the elimination of an alcohol. EC 4.2.2.
Hexameric extracellular matrix glycoprotein transiently expressed in many developing organs and often re-expressed in tumors. It is present in the central and peripheral nervous systems as well as in smooth muscle and tendons. (From Kreis & Vale, Guidebook to the Extracellular Matrix and Adhesion Proteins, 1993, p93)
An enzyme of the isomerase class that catalyzes the eliminative cleavage of polysaccharides containing 1,4-linked D-glucuronate or L-iduronate residues and 1,4-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends. (From Enzyme Nomenclature, 1992) EC 4.2.2.7.
Enzymes which transfer sulfate groups to various acceptor molecules. They are involved in posttranslational sulfation of proteins and sulfate conjugation of exogenous chemicals and bile acids. EC 2.8.2.
Penetrating and non-penetrating injuries to the spinal cord resulting from traumatic external forces (e.g., WOUNDS, GUNSHOT; WHIPLASH INJURIES; etc.).
A meshwork-like substance found within the extracellular space and in association with the basement membrane of the cell surface. It promotes cellular proliferation and provides a supporting structure to which cells or cell lysates in culture dishes adhere.
A natural high-viscosity mucopolysaccharide with alternating beta (1-3) glucuronide and beta (1-4) glucosaminidic bonds. It is found in the UMBILICAL CORD, in VITREOUS BODY and in SYNOVIAL FLUID. A high urinary level is found in PROGERIA.
In tissue culture, hairlike projections of neurons stimulated by growth factors and other molecules. These projections may go on to form a branched tree of dendrites or a single axon or they may be reabsorbed at a later stage of development. "Neurite" may refer to any filamentous or pointed outgrowth of an embryonal or tissue-culture neural cell.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
A non-vascular form of connective tissue composed of CHONDROCYTES embedded in a matrix that includes CHONDROITIN SULFATE and various types of FIBRILLAR COLLAGEN. There are three major types: HYALINE CARTILAGE; FIBROCARTILAGE; and ELASTIC CARTILAGE.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
Unstable isotopes of sulfur that decay or disintegrate spontaneously emitting radiation. S 29-31, 35, 37, and 38 are radioactive sulfur isotopes.
Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.
The fibrous tissue that replaces normal tissue during the process of WOUND HEALING.
A small leucine-rich proteoglycan that interacts with FIBRILLAR COLLAGENS and modifies the EXTRACELLULAR MATRIX structure of CONNECTIVE TISSUE. Decorin has also been shown to play additional roles in the regulation of cellular responses to GROWTH FACTORS. The protein contains a single glycosaminoglycan chain and is similar in structure to BIGLYCAN.
A ubiquitously expressed syndecan that is found in all stages of embryonic development and in most adult tissues. Syndecan-4 is found localized to focal adhesion sites in fibronectin-adherent cells and may play a role the process of CELL MIGRATION and CELL PROLIFERATION.
Glucosamine is a naturally occurring amino sugar that is often used in supplements to support joint health and reduce inflammation.
A small leucine-rich proteoglycan found in a variety of tissues including CAPILLARY ENDOTHELIUM; SKELETAL MUSCLE; CARTILAGE; BONE; and TENDONS. The protein contains two glycosaminoglycan chains and is similar in structure to DECORIN.
The developmental entity of a fertilized chicken egg (ZYGOTE). The developmental process begins about 24 h before the egg is laid at the BLASTODISC, a small whitish spot on the surface of the EGG YOLK. After 21 days of incubation, the embryo is fully developed before hatching.
Adherence of cells to surfaces or to other cells.
A class of large neuroglial (macroglial) cells in the central nervous system - the largest and most numerous neuroglial cells in the brain and spinal cord. Astrocytes (from "star" cells) are irregularly shaped with many long processes, including those with "end feet" which form the glial (limiting) membrane and directly and indirectly contribute to the BLOOD-BRAIN BARRIER. They regulate the extracellular ionic and chemical environment, and "reactive astrocytes" (along with MICROGLIA) respond to injury.
A syndecan that interacts with EXTRACELLULAR MATRIX PROTEINS and plays a role CELL PROLIFERATION and CELL MIGRATION.
Any compound that contains a constituent sugar, in which the hydroxyl group attached to the first carbon is substituted by an alcoholic, phenolic, or other group. They are named specifically for the sugar contained, such as glucoside (glucose), pentoside (pentose), fructoside (fructose), etc. Upon hydrolysis, a sugar and nonsugar component (aglycone) are formed. (From Dorland, 28th ed; From Miall's Dictionary of Chemistry, 5th ed)
An enzyme that catalyzes the random hydrolysis of 1,4-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate. (From Enzyme Nomenclature, 1992) There has been use as ANTINEOPLASTIC AGENTS to limit NEOPLASM METASTASIS.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Inorganic salts of chloric acid that contain the ClO3- ion.
A syndecan that is predominantly expressed during EMBRYONIC DEVELOPMENT. It may play a role in mediating cellular interactions with the EXTRACELLULAR MATRIX and may modulate the signaling activity of certain INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS.
A family of GLYCOSYLPHOSPHATIDYLINOSITOL-anchored, cell-surface heparan sulfate proteoglycans that may play a role in CELL GROWTH PROCESSES and CELL DIFFERENTIATION by modulating ligand-receptor interactions.
Nerve tissue proteins are the structural and functional components of neurons and glial cells that make up the nervous system.
Sensory ganglia located on the dorsal spinal roots within the vertebral column. The spinal ganglion cells are pseudounipolar. The single primary branch bifurcates sending a peripheral process to carry sensory information from the periphery and a central branch which relays that information to the spinal cord or brain.
Acids derived from monosaccharides by the oxidation of the terminal (-CH2OH) group farthest removed from the carbonyl group to a (-COOH) group. (From Stedmans, 26th ed)
A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.
The part of brain that lies behind the BRAIN STEM in the posterior base of skull (CRANIAL FOSSA, POSTERIOR). It is also known as the "little brain" with convolutions similar to those of CEREBRAL CORTEX, inner white matter, and deep cerebellar nuclei. Its function is to coordinate voluntary movements, maintain balance, and learn motor skills.
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.
A syndecan found at high levels in the developing LIMB BUDS. It may play a role in the regulation of MUSCULOSKELETAL DEVELOPMENT by modulating the effects of INTERCELLULAR SIGNALING PEPTIDES AND PROTEINS.
The basic cellular units of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the NERVOUS SYSTEM.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
Established cell cultures that have the potential to propagate indefinitely.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Nitrous acid (HNO2). A weak acid that exists only in solution. It can form water-soluble nitrites and stable esters. (From Merck Index, 11th ed)
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.
The sum of the weight of all the atoms in a molecule.
A group of elongate elasmobranchs. Sharks are mostly marine fish, with certain species large and voracious.
The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.
Test for tissue antigen using either a direct method, by conjugation of antibody with fluorescent dye (FLUORESCENT ANTIBODY TECHNIQUE, DIRECT) or an indirect method, by formation of antigen-antibody complex which is then labeled with fluorescein-conjugated anti-immunoglobulin antibody (FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT). The tissue is then examined by fluorescence microscopy.
Antibodies produced by a single clone of cells.
Glucuronidase is an enzyme that breaks down glucuronide conjugates, such as glucuronidated drugs and toxins, into their parent compounds.
Sulfatases are a group of enzymes that catalyze the hydrolysis of sulfate esters.
The N-acetyl derivative of galactosamine.
The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM.
Inorganic and organic derivatives of sulfuric acid (H2SO4). The salts and esters of sulfuric acid are known as SULFATES and SULFURIC ACID ESTERS respectively.
CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.
The movement of cells from one location to another. Distinguish from CYTOKINESIS which is the process of dividing the CYTOPLASM of a cell.
A slowly growing malignant neoplasm derived from cartilage cells, occurring most frequently in pelvic bones or near the ends of long bones, in middle-aged and old people. Most chondrosarcomas arise de novo, but some may develop in a preexisting benign cartilaginous lesion or in patients with ENCHONDROMATOSIS. (Stedman, 25th ed)
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Enzymes that catalyze the transfer of N-acetylgalactosamine from a nucleoside diphosphate N-acetylgalactosamine to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.
Refers to animals in the period of time just after birth.
A protective layer of firm, flexible cartilage over the articulating ends of bones. It provides a smooth surface for joint movement, protecting the ends of long bones from wear at points of contact.
The characteristic 3-dimensional shape of a carbohydrate.
Component of dermatan sulfate. Differs in configuration from glucuronic acid only at the C-5 position.
3'-Phosphoadenosine-5'-phosphosulfate. Key intermediate in the formation by living cells of sulfate esters of phenols, alcohols, steroids, sulfated polysaccharides, and simple esters, such as choline sulfate. It is formed from sulfate ion and ATP in a two-step process. This compound also is an important step in the process of sulfur fixation in plants and microorganisms.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
A polypeptide substance comprising about one third of the total protein in mammalian organisms. It is the main constituent of SKIN; CONNECTIVE TISSUE; and the organic substance of bones (BONE AND BONES) and teeth (TOOTH).
A darkly stained mat-like EXTRACELLULAR MATRIX (ECM) that separates cell layers, such as EPITHELIUM from ENDOTHELIUM or a layer of CONNECTIVE TISSUE. The ECM layer that supports an overlying EPITHELIUM or ENDOTHELIUM is called basal lamina. Basement membrane (BM) can be formed by the fusion of either two adjacent basal laminae or a basal lamina with an adjacent reticular lamina of connective tissue. BM, composed mainly of TYPE IV COLLAGEN; glycoprotein LAMININ; and PROTEOGLYCAN, provides barriers as well as channels between interacting cell layers.
A class of Echinodermata characterized by long, slender bodies.
The rate dynamics in chemical or physical systems.
The capacity of the NERVOUS SYSTEM to change its reactivity as the result of successive activations.
A cylindrical column of tissue that lies within the vertebral canal. It is composed of WHITE MATTER and GRAY MATTER.
A single-chain polypeptide growth factor that plays a significant role in the process of WOUND HEALING and is a potent inducer of PHYSIOLOGIC ANGIOGENESIS. Several different forms of the human protein exist ranging from 18-24 kDa in size due to the use of alternative start sites within the fgf-2 gene. It has a 55 percent amino acid residue identity to FIBROBLAST GROWTH FACTOR 1 and has potent heparin-binding activity. The growth factor is an extremely potent inducer of DNA synthesis in a variety of cell types from mesoderm and neuroectoderm lineages. It was originally named basic fibroblast growth factor based upon its chemical properties and to distinguish it from acidic fibroblast growth factor (FIBROBLAST GROWTH FACTOR 1).
A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Naturally occurring or experimentally induced animal diseases with pathological processes sufficiently similar to those of human diseases. They are used as study models for human diseases.
Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.
Hexosamines are a type of sugar found in the human body that are involved in the formation of glycosaminoglycans, which play a role in various biological processes such as cell signaling and inflammation.
Long-chain polymer of glucose containing 17-20% sulfur. It has been used as an anticoagulant and also has been shown to inhibit the binding of HIV-1 to CD4-POSITIVE T-LYMPHOCYTES. It is commonly used as both an experimental and clinical laboratory reagent and has been investigated for use as an antiviral agent, in the treatment of hypolipidemia, and for the prevention of free radical damage, among other applications.
Glycoproteins found on the membrane or surface of cells.
Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.
Glycoproteins found on the surfaces of cells, particularly in fibrillar structures. The proteins are lost or reduced when these cells undergo viral or chemical transformation. They are highly susceptible to proteolysis and are substrates for activated blood coagulation factor VIII. The forms present in plasma are called cold-insoluble globulins.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
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)
The head of a long bone that is separated from the shaft by the epiphyseal plate until bone growth stops. At that time, the plate disappears and the head and shaft are united.
A sugar acid formed by the oxidation of the C-6 carbon of GLUCOSE. In addition to being a key intermediate metabolite of the uronic acid pathway, glucuronic acid also plays a role in the detoxification of certain drugs and toxins by conjugating with them to form GLUCURONIDES.
Proteins prepared by recombinant DNA technology.
The nine cartilages of the larynx, including the cricoid, thyroid and epiglottic, and two each of arytenoid, corniculate and cuneiform.
Polysaccharides are complex carbohydrates composed of long chains of monosaccharide units, with important functions in the body including energy storage, structural support, and immune response.
Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.
Large, noncollagenous glycoprotein with antigenic properties. It is localized in the basement membrane lamina lucida and functions to bind epithelial cells to the basement membrane. Evidence suggests that the protein plays a role in tumor invasion.
Xylose is a type of sugar found in plants that is sometimes used as a dietary supplement for people with gut disorders.
Glycoside Hydrolases are enzymes that break down complex carbohydrates into simpler sugars.
An enzyme of the hydrolase class that catalyzes the reaction of triacylglycerol and water to yield diacylglycerol and a fatty acid anion. The enzyme hydrolyzes triacylglycerols in chylomicrons, very-low-density lipoproteins, low-density lipoproteins, and diacylglycerols. It occurs on capillary endothelial surfaces, especially in mammary, muscle, and adipose tissue. Genetic deficiency of the enzyme causes familial hyperlipoproteinemia Type I. (Dorland, 27th ed) EC 3.1.1.34.
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.
Stable sulfur atoms that have the same atomic number as the element sulfur, but differ in atomic weight. S-33, 34, and 36 are stable sulfur isotopes.
Separation of particles according to density by employing a gradient of varying densities. At equilibrium each particle settles in the gradient at a point equal to its density. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

Identification of the human melanoma-associated chondroitin sulfate proteoglycan antigen epitope recognized by the antitumor monoclonal antibody 763.74 from a peptide phage library. (1/1155)

To identify the epitope of the melanoma-associated chondroitin sulfate proteoglycan (MCSP) recognized by the monoclonal antibody (mAb) 763.74, we first expressed random DNA fragments obtained from the complete coding sequence of the MCSP core glycoproteins in phages and selected without success for binders to the murine mAb 763.74. We then used a library of random heptapeptides displayed at the surface of the filamentous M13 phage as fusion protein to the NH2-terminal portion of the minor coat protein III. After three rounds of selection on the bound mAb, several phages displaying related binding peptides were identified, yielding the consensus sequence Val-His-Leu-Asn-Tyr-Glu-His. Competitive ELISA experiments showed that this peptide can be specifically prevented from binding to mAb 763.74 by an anti-idiotypic MK2-23 mouse:human chimeric mAb and by A375 melanoma cells expressing the antigen MCSP. We screened the amino acid sequence of the MCSP molecule for a region of homology to the consensus sequence and found that the amino acid sequence Val-His-Ile-Asn-Ala-His spanning positions 289 and 294 has high homology. Synthetic linear peptides corresponding to the consensus sequence as well as to the MCSP-derived epitope inhibit the binding of mAb 763.74 to the phages displaying the consensus amino acid sequence. Finally, the biotinylated consensus peptide absorbed to streptavidin-microtiter plates can be used for the detection of mAb 763.74 in human serum. These results show clearly that the MCSP epitope defined by mAb 763.74 has been identified.  (+info)

Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon. (2/1155)

Fibromodulin is a member of a family of connective tissue glycoproteins/proteoglycans containing leucine-rich repeat motifs. Several members of this gene family bind to fibrillar collagens and are believed to function in the assembly of the collagen network in connective tissues. Here we show that mice lacking a functional fibromodulin gene exhibit an altered morphological phenotype in tail tendon with fewer and abnormal collagen fiber bundles. In fibromodulin-null animals virtually all collagen fiber bundles are disorganized and have an abnormal morphology. Also 10-20% of the bundles in heterozygous mice are similar to the abnormal bundles in fibromodulin-null tail tendon. Ultrastructural analysis of Achilles tendon from fibromodulin-null mice show collagen fibrils with irregular and rough outlines in cross-section. Morphometric analysis show that fibromodulin-null mice have on the average thinner fibrils than wild type animals as a result of a larger preponderance of very thin fibrils in an overall similar range of fibril diameters. Protein and RNA analyses show an approximately 4-fold increase in the content of lumican in fibromodulin-null as compared with wild type tail tendon, despite a decrease in lumican mRNA. These results demonstrate a role for fibromodulin in collagen fibrillogenesis and suggest that the orchestrated action of several leucine-rich repeat glycoproteins/proteoglycans influence the architecture of collagen matrices.  (+info)

Formation of hyaluronan- and versican-rich pericellular matrix is required for proliferation and migration of vascular smooth muscle cells. (3/1155)

The accumulation of hyaluronan (HA) and the HA-binding proteoglycan versican around smooth muscle cells in lesions of atherosclerosis suggests that together these molecules play an important role in the events of atherogenesis. In this study we have examined the formation of HA- and versican-rich pericellular matrices by human aortic smooth muscle cells in vitro, using a particle-exclusion assay, and the role of the pericellular matrix in cell proliferation and migration. The structural dependence of the pericellular matrix on HA can be demonstrated by the complete removal of the matrix with Streptomyces hyaluronidase. The presence of versican in the pericellular matrix was confirmed immunocytochemically. By electron microscopy, the cell coat was seen as a tangled network of hyaluronidase-sensitive filaments decorated with ruthenium red-positive proteoglycan granules. Ninety percent of migrating cells in wounded cultures, and virtually all mitotic cells, displayed abundant HA- and versican-rich coats. Time-lapse video imaging revealed that HA- and versican-rich pericellular matrix formation is dynamic and rapid, and coordinated specifically with cell detachment and mitotic cell rounding. HA oligosaccharides, which inhibit the binding of HA to the cell surface and prevent pericellular matrix formation, significantly reduced proliferation and migration in response to platelet-derived growth factor, whereas larger HA fragments and high molecular weight HA had no effect. Treatment with HA oligosaccharides also led to changes in cell shape from a typical fusiform morphology to a more spread and flattened appearance. These data suggest that organization of HA- and versican-rich pericellular matrices may facilitate migration and mitosis by diminishing cell surface adhesivity and affecting cell shape through steric exclusion and the viscous properties of HA proteoglycan gels.  (+info)

The proteoglycan lectin domain binds sulfated cell surface glycolipids and promotes cell adhesion. (4/1155)

The lecticans are a group of chondroitin sulfate proteoglycans characterized by the presence of C-type lectin domains. Despite the suggestion that their lectin domains interact with carbohydrate ligands, the identity of such ligands has not been elucidated. We previously showed that brevican, a nervous system-specific lectican, binds the surface of B28 glial cells (Yamada, H., Fredette, B., Shitara, K., Hagihara, K., Miura, R., Ranscht, B., Stallcup, W. B., and Yamaguchi, Y. (1997) J. Neurosci. 17, 7784-7795). In this paper, we demonstrate that two classes of sulfated glycolipids, sulfatides and HNK-1-reactive sulfoglucuronylglycolipids (SGGLs), act as cell surface receptors for brevican. The lectin domain of brevican binds sulfatides and SGGLs in a calcium-dependent manner as expected of a C-type lectin domain. Intact, full-length brevican also binds both sulfatides and SGGLs. The lectin domain immobilized as a substrate supports adhesion of cells expressing SGGLs or sulfatides, which was inhibited by monoclonal antibodies against these glycolipids or by treatment of the substrate with SGGLs or sulfatides. Our findings demonstrate that the interaction between the lectin domains of lecticans and sulfated glycolipids comprises a novel cell substrate recognition system, and suggest that lecticans in extracellular matrices serve as substrate for adhesion and migration of cells expressing these glycolipids in vivo.  (+info)

Resistance of small leucine-rich repeat proteoglycans to proteolytic degradation during interleukin-1-stimulated cartilage catabolism. (5/1155)

A bovine nasal-cartilage culture system has been utilized to analyse the catabolic events occurring in response to interleukin-1beta over a 14-day period. An early event following the start of interleukin-1 treatment was the release of glycosaminoglycan into the culture medium. This release was accompanied by the appearance in the tissue, and shortly thereafter also in the culture media, of a globular domain (G1)-containing aggrecan degradation product generated by the action of aggrecanase. Link protein was also released from the cartilage with a similar timeframe to that of the G1 fragment, although there was no evidence of its proteolytic degradation. By comparison with aggrecan, the small leucine-rich repeat proteoglycans decorin, biglycan and lumican showed a resistance to both proteolytic cleavage and release throughout the culture period. In contrast, fibromodulin exhibited a marked decrease in size after day 4, presumably due to proteolytic modification, but the major degradation product was retained throughout the culture period. Also in contrast with the early changes in the components of the proteoglycan aggregate, type II collagen did not display signs of extensive degradation until much later in the culture period. Collagen degradation products compatible with collagenase action first appeared in the medium by day 10 and increased thereafter. These data demonstrate that the leucine-rich repeat proteoglycans are resistant to proteolytic action during interleukin-1-stimulated cartilage catabolism, compared with aggrecan. This resistance and continued interaction with the surface of the collagen fibrils may help to stabilize the collagen fibrillar network and protect it from extensive proteolytic attack during the early phases of cartilage degeneration.  (+info)

Identification and characterization of ligands for L-selectin in the kidney. I. Versican, a large chondroitin sulfate proteoglycan, is a ligand for L-selectin. (6/1155)

Ligands for a leukocyte adhesion molecule, L-selectin, are expressed not only in the specific vascular endothelium in lymph nodes and Peyer's patches but also in the extravascular tissues such as the brain white matter, choroid plexus and the kidney distal straight tubuli. However, the biological significance of these extravascular ligands is currently unknown. We now report the purification and characterization of a novel extravascular ligand for L-selectin in the kidney using a tubule-derived cell line, ACHN. Binding of L-selectin-IgG chimera (LEC-IgG) to the isolated ligand was specifically blocked with either (i) anti-L-selectin mAb, (ii) EDTA, (iii) fucoidan, (iv) chondroitin sulfate (CS) B or CS E, or (v) treatment with chondroitinases. Partial amino acid sequencing, Western blotting and immunoprecipitation analyses showed that a major ligand for L-selectin in ACHN cells is versican of 1600 kDa. Histochemical as well as biochemical analyses verified that a versican subspecies in the kidney was indeed reactive with L-selectin. Studies with cell lines including those derived from the kidney indicated that a certain glycoform and/or splice form of versican is reactive with L-selectin. Under pathological conditions such as those induced by unilateral ureteral obstruction, versican was shed from the distal straight tubuli and became localized in the adjacent vascular bundles around which a substantial leukocyte infiltration was concomitantly observed. Possible involvement of versican in leukocyte trafficking into the kidney under diseased conditions is discussed.  (+info)

Dermatopontin expression is decreased in hypertrophic scar and systemic sclerosis skin fibroblasts and is regulated by transforming growth factor-beta1, interleukin-4, and matrix collagen. (7/1155)

Dermatopontin is a recently discovered extracellular matrix protein with proteoglycan and cell-binding properties and is assumed to play important roles in cell-matrix interactions and matrix assembly. In this study we examined the expression of dermatopontin mRNA and protein in skin fibroblast cultures from patients with hypertrophic scar and patients with systemic sclerosis. Dermatopontin mRNA and protein levels were reduced in fibroblast cultures from hypertrophic scar lesional skin compared with fibroblasts from normal skin of the same hypertrophic scar patient. Fibroblast cultures from systemic sclerosis patient involved skin also showed significantly reduced expression of dermatopontin compared with normal skin fibroblasts from healthy individuals. We also investigated the effects of cytokines and matrix collagen on dermatopontin expression in normal cultured fibroblasts. Transforming growth factor-beta1 increased dermatopontin mRNA and protein levels, while interleukin-4 reduced dermatopontin expression. Substrate coated with type I collagen reduced dermatopontin mRNA levels, the reduction being more prominent in three-dimensional collagen matrices. Our results suggest that the decreased expression of dermatopontin is associated with the pathogenesis of fibrosis in hypertrophic scar and systemic sclerosis, and that the effect of the cytokines and matrix collagen on dermatopontin may have important implications for skin fibrosis.  (+info)

DSD-1-proteoglycan is the mouse homolog of phosphacan and displays opposing effects on neurite outgrowth dependent on neuronal lineage. (8/1155)

DSD-1-PG is a chondroitin sulfate proteoglycan (CSPG) expressed by glial cells that can promote neurite outgrowth from rat embryonic mesencephalic (E14) and hippocampal (E18) neurons, an activity that is associated with the CS glycosaminoglycans (GAGs). Further characterization of DSD-1-PG has included sequencing of peptides from the core protein and the cloning of the corresponding cDNA using polyclonal antisera against DSD-1-PG to screen phage expression libraries. On the basis of these studies we have identified DSD-1-PG as the mouse homolog of phosphacan, a neural rat CSPG. Monoclonal antibodies 3H1 and 3F8 against carbohydrate residues on rat phosphacan recognize these epitopes on DSD-1-PG. The epitopes of the antibodies, L2/HNK-1 and L5/Lewis-X, which have been implicated in functional interactions, are also found on DSD-1-PG. Although DSD-1-PG has previously been shown to promote neurite outgrowth, its upregulation after stab wounding of the CNS and its localization in regions that are considered boundaries to axonal extension suggested that it may also have inhibitory functions. Neonatal dorsal root ganglion (DRG) explants grown on a rich supportive substrate (laminin) with and without DSD-1-PG were strikingly inhibited by the proteoglycan. The inhibitory effects of DSD-1-PG on the DRG explants were not relieved by removal of the CS GAGs, indicating that this activity is associated with the core glycoprotein. The neurite outgrowth from embryonic hippocampal neurons on laminin was not affected by the addition of DSD-1-PG. This indicates that DSD-1-PG/mouse phosphacan can have opposing effects on the process of neurite outgrowth dependent on neuronal lineage.  (+info)

Chondroitin sulfate proteoglycans (CSPGs) are a type of proteoglycan found in the extracellular matrix of connective tissues, including cartilage, bone, and the central nervous system. They are composed of a core protein to which multiple chains of chondroitin sulfate glycosaminoglycans (GAGs) are attached. CSPGs play important roles in various biological processes, including cell adhesion, migration, and differentiation, as well as in the development and maintenance of tissue structure and function. In the medical field, CSPGs are of interest for their potential roles in various diseases and conditions, including osteoarthritis, spinal cord injury, and cancer.

Chondroitin sulfates are a group of complex carbohydrates that are found in the extracellular matrix of connective tissues, including cartilage, bone, and blood vessels. They are composed of repeating disaccharide units of glucuronic acid and galactosamine, which are linked by a sulfate group. In the medical field, chondroitin sulfates are often used as dietary supplements to support joint health and reduce the symptoms of osteoarthritis. They are thought to work by inhibiting the activity of enzymes that break down cartilage, promoting the production of proteoglycans, and reducing inflammation in the joints. Chondroitin sulfates are also used in some medical treatments, such as the treatment of certain types of cancer and the prevention of blood clots. However, their effectiveness and safety in these applications are still being studied, and more research is needed to fully understand their potential benefits and risks.

Chondroitin ABC Lyase (CABCyL) is an enzyme that breaks down chondroitin sulfate, a complex carbohydrate found in cartilage, tendons, and other connective tissues. It is involved in the degradation of proteoglycans, which are large molecules composed of proteins and carbohydrates, and plays a role in the turnover of extracellular matrix in tissues. In the medical field, CABCyL has been studied for its potential therapeutic applications in various conditions, including osteoarthritis, a degenerative joint disease characterized by the breakdown of cartilage and the development of bone spurs. CABCyL has been shown to increase the turnover of cartilage matrix and promote the synthesis of new cartilage, which may help to slow down the progression of osteoarthritis. It has also been studied for its potential use in the treatment of other connective tissue disorders, such as intervertebral disc degeneration and fibrosis.

Proteoglycans are complex macromolecules that consist of a core protein to which one or more glycosaminoglycan chains are covalently attached. They are found in the extracellular matrix of connective tissues, including cartilage, bone, skin, and blood vessels, and play important roles in various biological processes, such as cell signaling, tissue development, and wound healing. Proteoglycans are involved in the regulation of cell growth and differentiation, as well as in the maintenance of tissue homeostasis. They also play a crucial role in the formation and function of the extracellular matrix, which provides structural support and helps to maintain tissue integrity. In the medical field, proteoglycans are of interest because they are involved in a number of diseases and disorders, including osteoarthritis, cancer, and cardiovascular disease. For example, changes in the composition and distribution of proteoglycans in the cartilage matrix have been implicated in the development of osteoarthritis, a degenerative joint disease characterized by the breakdown of cartilage and bone. Similarly, alterations in proteoglycan expression and function have been observed in various types of cancer, including breast, prostate, and colon cancer.

Heparan sulfate proteoglycans (HSPGs) are a family of complex molecules that are found in the extracellular matrix of many tissues in the human body. They are composed of a core protein, which is modified with heparan sulfate chains. HSPGs play important roles in a variety of biological processes, including cell signaling, cell adhesion, and the regulation of growth and development. They are also involved in the formation and function of blood vessels, and have been implicated in a number of diseases, including cancer, cardiovascular disease, and neurological disorders.

Chondroitin is a complex polysaccharide that is found in the extracellular matrix of connective tissues, particularly in cartilage. It is composed of repeating disaccharide units of glucuronic acid and N-acetylglucosamine, and it plays an important role in maintaining the structure and function of cartilage. In the medical field, chondroitin is often used as a dietary supplement to support joint health and reduce the symptoms of osteoarthritis. It is thought to work by inhibiting the activity of enzymes that break down cartilage, thereby slowing down the progression of joint damage. Chondroitin supplements are also sometimes used to treat other conditions, such as interstitial cystitis and high blood pressure. However, the effectiveness of chondroitin supplements for these conditions is not well-established, and more research is needed to confirm their benefits. Additionally, some studies have suggested that high doses of chondroitin may increase the risk of bleeding, so it is important to use caution when taking this supplement and to consult with a healthcare provider before starting any new supplement regimen.

Chondroitinases and chondroitin lyases are enzymes that break down chondroitin sulfate, a complex carbohydrate found in cartilage. These enzymes are used in medical research and treatment of various conditions, including osteoarthritis, spinal cord injury, and multiple sclerosis. Chondroitinases are a type of lyase that specifically cleave the glycosidic bond between the disaccharide units of chondroitin sulfate. This results in the release of smaller chondroitin sulfate fragments, which can be used for various purposes, such as studying the structure and function of cartilage, or developing new treatments for diseases that affect cartilage. Chondroitin lyases, on the other hand, are a broader category of enzymes that can cleave various types of glycosaminoglycans, including chondroitin sulfate, heparan sulfate, and dermatan sulfate. These enzymes are used in research to study the structure and function of glycosaminoglycans, and in clinical settings to treat conditions such as osteoarthritis and spinal cord injury. Overall, chondroitinases and chondroitin lyases play important roles in the medical field by providing tools for studying cartilage and developing new treatments for diseases that affect this tissue.

Glycosaminoglycans (GAGs) are a group of complex carbohydrates that are found in the extracellular matrix of connective tissues in the human body. They are composed of repeating disaccharide units of a sugar called glucose and another sugar called uronic acid, which are linked together by glycosidic bonds. GAGs play important roles in various biological processes, including cell signaling, tissue development, and wound healing. They are also involved in the regulation of inflammation, blood clotting, and the immune response. In the medical field, GAGs are often studied in relation to various diseases and conditions, such as osteoarthritis, rheumatoid arthritis, and cancer. They are also used as diagnostic markers and therapeutic targets in the treatment of these conditions. Additionally, GAGs are used in various medical applications, such as wound dressings, tissue engineering, and drug delivery systems.

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Heparitin Sulfate is a naturally occurring glycosaminoglycan found in the extracellular matrix of connective tissue. It is a linear polysaccharide composed of repeating disaccharide units of glucuronic acid and N-sulfated glucosamine. Heparitin Sulfate is known for its ability to bind and modulate the activity of various growth factors, cytokines, and other signaling molecules, making it an important component of the body's regulatory network. In the medical field, Heparitin Sulfate is used as a medication to treat a variety of conditions, including thrombosis, inflammation, and cancer. It is also used in research as a tool to study the interactions between proteins and carbohydrates.

In the medical field, "versican" refers to a large chondroitin sulfate proteoglycan that is expressed in various tissues, including cartilage, bone, and the central nervous system. Versican is a member of the aggrecan family of proteoglycans, which play important roles in the maintenance of tissue structure and function. In cartilage, versican is primarily found in the extracellular matrix and is involved in the regulation of cell behavior and matrix organization. In bone, versican is expressed by osteoblasts and is thought to play a role in bone formation and remodeling. In the central nervous system, versican is expressed by astrocytes and is involved in the regulation of cell migration and axon guidance. Abnormal expression or function of versican has been implicated in a number of diseases, including osteoarthritis, multiple sclerosis, and glioblastoma.

Chondroitin lyases are a group of enzymes that break down chondroitin sulfate, a complex carbohydrate found in cartilage and other connective tissues. These enzymes are important in the process of cartilage turnover and repair, as they help to break down old or damaged cartilage and replace it with new tissue. There are several different types of chondroitin lyases, each with a slightly different mechanism of action. Some chondroitin lyases are able to cleave the glycosidic bonds between the sugar molecules that make up chondroitin sulfate, while others are able to remove specific sulfate groups from the molecule. Chondroitin lyases have been the subject of extensive research in the medical field, as they have potential applications in the treatment of a variety of conditions that affect cartilage, including osteoarthritis, rheumatoid arthritis, and other forms of joint disease. Some studies have suggested that chondroitin lyases may be able to help stimulate the production of new cartilage tissue, or to reduce the inflammation and pain associated with joint disease. However, more research is needed to fully understand the potential therapeutic applications of chondroitin lyases, and to determine the most effective ways to use these enzymes in the treatment of cartilage-related conditions.

Receptor-like protein tyrosine phosphatases, class 5 (PTPRC5) are a group of proteins that are involved in cell signaling and communication. They are characterized by the presence of a tyrosine phosphatase domain, which is responsible for removing phosphate groups from tyrosine residues on other proteins. This activity can regulate the activity of these proteins and alter their function. PTPRC5 proteins are expressed in a variety of tissues and cell types, and they have been implicated in a number of biological processes, including cell adhesion, migration, and differentiation. Some members of this family have also been associated with diseases, such as cancer and autoimmune disorders. In the medical field, PTPRC5 proteins are of interest as potential therapeutic targets for the treatment of various conditions. For example, they may be targeted to modulate the activity of proteins involved in cell signaling pathways that are dysregulated in certain diseases. Additionally, PTPRC5 proteins may be used as diagnostic markers to identify individuals who are at risk for certain diseases or to monitor the progression of these diseases.

Aggrecans are a type of proteoglycan that are found in the extracellular matrix of connective tissues, including cartilage, bone, and tendon. They are large, complex molecules that consist of a core protein called aggrecan core protein, which is surrounded by a meshwork of negatively charged glycosaminoglycan chains. In the context of cartilage, aggrecans are the primary component of the proteoglycan matrix, which provides the tissue with its unique properties, such as its ability to resist compression and absorb shock. Aggrecans also play a role in regulating the growth and differentiation of chondrocytes, the cells that produce and maintain cartilage. In the medical field, aggrecans are often studied in relation to various diseases and conditions that affect cartilage, such as osteoarthritis, rheumatoid arthritis, and osteogenesis imperfecta. Changes in the levels or composition of aggrecans have been observed in these conditions, and they may contribute to the development and progression of cartilage damage.

In the medical field, sulfates refer to compounds that contain the sulfate ion (SO4^2-). Sulfates are commonly found in many minerals and are also produced by the body as a byproduct of metabolism. Sulfates are often used in medical treatments, particularly in the treatment of respiratory conditions such as asthma and chronic obstructive pulmonary disease (COPD). They work by helping to thin mucus in the lungs, making it easier to cough up and reducing the risk of infection. Sulfates are also used in the treatment of certain skin conditions, such as psoriasis and eczema, as well as in the treatment of gout, a type of arthritis caused by high levels of uric acid in the blood. In addition to their therapeutic uses, sulfates are also used in the production of a variety of industrial and commercial products, including detergents, fertilizers, and plastics.

Dermatan sulfate is a type of glycosaminoglycan, which is a complex carbohydrate found in the extracellular matrix of connective tissues in the body. It is a major component of the proteoglycans found in the skin, cartilage, and other connective tissues. Dermatan sulfate is synthesized by cells in the connective tissue and is involved in a variety of biological processes, including cell signaling, tissue development, and wound healing. It also plays a role in the regulation of inflammation and the immune response. In the medical field, dermatan sulfate is used as a diagnostic tool to help identify certain diseases and conditions, such as inflammatory bowel disease, osteoarthritis, and certain types of cancer. It is also used in the development of new drugs and therapies for these conditions.

Neurocan is a type of proteoglycan, which is a complex molecule made up of a protein core and chains of carbohydrates. It is a glycosaminoglycan that is found in the extracellular matrix of the central nervous system, including the brain and spinal cord. Neurocan is involved in the development and maintenance of the nervous system, and it plays a role in regulating cell growth and differentiation. It is also thought to be involved in the formation of synapses, which are the connections between neurons that allow them to communicate with each other. In the medical field, neurocan is being studied as a potential target for the treatment of neurological disorders such as multiple sclerosis and Alzheimer's disease.

Lectins, C-Type are a type of carbohydrate-binding proteins that are found in a variety of plants, animals, and microorganisms. They are characterized by the presence of a conserved cysteine residue in their carbohydrate recognition domain, which is responsible for their binding specificity to specific carbohydrate structures. C-Type lectins are involved in a wide range of biological processes, including immune response, cell adhesion, and cell signaling. They are also used in medical research and have potential therapeutic applications, such as in the treatment of cancer, infectious diseases, and inflammatory disorders. In the medical field, C-Type lectins are often studied for their ability to bind to specific carbohydrate structures on the surface of cells, which can be used to target and modulate cellular processes. They are also used as diagnostic tools to detect specific carbohydrate structures in biological samples, such as in the diagnosis of certain diseases or to monitor the progression of a disease.

Extracellular matrix (ECM) proteins are a diverse group of proteins that are secreted by cells and form a complex network within the extracellular space. These proteins provide structural support to cells and tissues, regulate cell behavior, and play a crucial role in tissue development, homeostasis, and repair. ECM proteins are found in all tissues and organs of the body and include collagens, elastin, fibronectin, laminins, proteoglycans, and many others. These proteins interact with each other and with cell surface receptors to form a dynamic and highly regulated ECM that provides a physical and chemical environment for cells to thrive. In the medical field, ECM proteins are important for understanding the development and progression of diseases such as cancer, fibrosis, and cardiovascular disease. They are also used in tissue engineering and regenerative medicine to create artificial ECMs that can support the growth and function of cells and tissues. Additionally, ECM proteins are used as diagnostic and prognostic markers in various diseases, and as targets for drug development.

Receptors, N-Acetylglucosamine (NAG) are a type of protein receptors found on the surface of cells in the immune system. These receptors are responsible for recognizing and binding to N-acetylglucosamine (NAG), a sugar molecule that is commonly found on the surface of bacteria and other microorganisms. When NAG receptors bind to NAG, it triggers a signaling cascade within the cell that leads to the activation of immune cells and the production of inflammatory molecules, which help to fight off the invading microorganisms. NAG receptors are also involved in the regulation of cell growth and differentiation, and have been implicated in the development of certain diseases, including cancer and autoimmune disorders.

Keratan sulfate (KS) is a type of glycosaminoglycan (GAG) that is found in the extracellular matrix of connective tissues throughout the body. It is particularly abundant in the cornea, skin, and joint cartilage. In the medical field, KS is important because it plays a role in the structure and function of many tissues. For example, in the cornea, KS helps to maintain its transparency and elasticity, while in joint cartilage, it helps to provide shock absorption and lubrication. Abnormalities in KS production or metabolism can lead to a variety of diseases and conditions, including corneal dystrophies, osteoarthritis, and certain types of cancer. Therefore, understanding the biology of KS and its role in health and disease is an important area of research in the medical field.

In the medical field, disaccharides are two monosaccharide units (simple sugars) that are joined together by a glycosidic bond. Disaccharides are commonly found in foods and are broken down by the body into their constituent monosaccharides during digestion. Some common examples of disaccharides include sucrose (table sugar), lactose (milk sugar), and maltose (malt sugar). Disaccharides are an important source of energy for the body and are also used in the production of various foods and beverages.

Heparin is a medication that is used to prevent and treat blood clots. It is a natural anticoagulant that works by inhibiting the activity of enzymes that are involved in the formation of blood clots. Heparin is typically administered intravenously, but it can also be given by injection or applied topically to the skin. It is commonly used to prevent blood clots in people who are at risk due to surgery, pregnancy, or other medical conditions. Heparin is also used to treat blood clots that have already formed, such as deep vein thrombosis (DVT) and pulmonary embolism (PE). It is important to note that heparin can have serious side effects, including bleeding, and should only be used under the supervision of a healthcare professional.

Syndecans are a family of transmembrane proteoglycans that are found on the surface of many different types of cells in the human body. They are involved in a variety of cellular processes, including cell adhesion, migration, and signaling. Syndecans are composed of a core protein that is linked to a glycosaminoglycan chain, which is a long chain of sugar molecules. The glycosaminoglycan chain is responsible for the interactions between syndecans and other molecules in the extracellular matrix, such as growth factors and matrix proteins. In the medical field, syndecans are being studied for their potential role in a variety of diseases, including cancer, cardiovascular disease, and inflammatory disorders.

Polysaccharide lyases are a group of enzymes that break down complex carbohydrates, such as starch, glycogen, and cellulose, into simpler sugars. These enzymes are important in the human body for the digestion and absorption of carbohydrates, as well as in the production of certain types of bacteria and the breakdown of plant material. There are several different types of polysaccharide lyases, each of which targets a specific type of carbohydrate. For example, amylases break down starch into maltose and other simpler sugars, while cellulases break down cellulose into glucose. These enzymes are produced by the pancreas, salivary glands, and other organs in the digestive system, and are also found in certain types of bacteria. In the medical field, polysaccharide lyases are sometimes used to treat conditions related to carbohydrate metabolism, such as diabetes and malabsorption disorders. They may also be used in the production of certain types of biofuels and other industrial products.

Tenascin is a large extracellular matrix protein that is expressed in a variety of tissues during development, wound healing, and tissue repair. It is synthesized by fibroblasts and other cells in response to injury or tissue remodeling, and it plays a role in regulating cell migration, adhesion, and differentiation. In the medical field, tenascin is often studied in the context of cancer, where it is overexpressed in many types of tumors and is associated with poor prognosis. It is also involved in the development of fibrosis, a condition characterized by the excessive accumulation of scar tissue in organs and tissues. In addition, tenascin has been shown to play a role in the immune response, and it is involved in the regulation of angiogenesis, the formation of new blood vessels. Overall, tenascin is a complex and multifunctional protein that plays a critical role in many aspects of tissue biology and disease.

Heparin lyase is an enzyme that breaks down heparin, a type of polysaccharide that is commonly used as an anticoagulant medication. Heparin lyase is produced by certain bacteria and can cause heparin resistance, which can lead to increased bleeding and other complications in patients who are taking heparin. Heparin resistance can occur when bacteria in the body produce heparin lyase, which breaks down the heparin molecules, rendering them less effective at preventing blood clots. This condition is typically treated with alternative anticoagulant medications or by administering higher doses of heparin.

Sulfotransferases are a group of enzymes that transfer a sulfate group from a donor molecule to an acceptor molecule. These enzymes play important roles in the metabolism of many drugs, hormones, and other substances in the body. They are also involved in the detoxification of harmful substances, such as environmental pollutants and toxins. Sulfotransferases are found in many tissues throughout the body, including the liver, kidney, and brain. They are classified into different families based on their substrate specificity and mechanism of action. Some of the most well-known families of sulfotransferases include the cytosolic sulfotransferases (SULTs) and the membrane-bound sulfotransferases (SULTs). In the medical field, sulfotransferases are important for understanding the metabolism and pharmacology of drugs. They can affect the efficacy and toxicity of drugs by modifying their chemical structure and altering their interactions with receptors and enzymes. Sulfotransferases are also being studied as potential targets for the development of new drugs for the treatment of various diseases, including cancer, cardiovascular disease, and neurological disorders.

Spinal cord injuries (SCI) are a type of injury that occurs when the spinal cord is damaged or disrupted, usually as a result of trauma or disease. The spinal cord is a bundle of nerves that runs down the back of the neck and lower back, and it is responsible for transmitting signals between the brain and the rest of the body. When the spinal cord is injured, it can result in a range of symptoms, depending on the location and severity of the injury. These can include loss of sensation or movement in the affected area, difficulty with bladder or bowel control, and changes in sexual function. SCI can be caused by a variety of factors, including car accidents, falls, sports injuries, and acts of violence. Treatment for SCI typically involves a combination of medical and rehabilitative care, and the goal is to help individuals with SCI regain as much function as possible and improve their quality of life.

Hyaluronic acid is a naturally occurring glycosaminoglycan (GAG) found in the human body. It is a polysaccharide composed of repeating disaccharide units of glucuronic acid and N-acetylglucosamine. Hyaluronic acid is a major component of the extracellular matrix in connective tissues, including the skin, joint cartilage, and synovial fluid. In the medical field, hyaluronic acid is used in various therapeutic applications, including: 1. Joint injections: Hyaluronic acid is used as a viscosupplement to treat osteoarthritis in the knee, shoulder, and hip joints. It helps to lubricate the joint and reduce friction, thereby reducing pain and improving mobility. 2. Skin care: Hyaluronic acid is used in skincare products to hydrate and plump the skin, reduce the appearance of fine lines and wrinkles, and improve skin elasticity. 3. Wound healing: Hyaluronic acid is used in wound dressings to promote healing by providing a moist environment that supports the growth of new tissue. 4. Eye surgery: Hyaluronic acid is used in eye surgery to help maintain the shape of the cornea and prevent corneal swelling after surgery. Overall, hyaluronic acid has a wide range of medical applications due to its unique properties, including its ability to attract and retain water, its ability to modulate cell behavior, and its ability to promote tissue repair and regeneration.

Sulfur radioisotopes are radioactive isotopes of sulfur, which are used in various medical applications. These isotopes are typically produced by bombarding stable sulfur atoms with high-energy particles, such as protons or neutrons. One commonly used sulfur radioisotope in medicine is sulfur-35 (35S), which has a half-life of approximately 87 days. It is used in a variety of diagnostic and therapeutic applications, including: * Radiolabeling of biomolecules: 35S can be used to label proteins, peptides, and other biomolecules, allowing researchers to study their structure, function, and interactions with other molecules. * Imaging of tumors: 35S-labeled compounds can be used to image tumors in animals or humans, allowing doctors to monitor the growth and spread of tumors. * Radioimmunotherapy: 35S can be used to label antibodies, which can then be targeted to specific cells or tissues in the body, delivering a dose of radiation to kill cancer cells or other diseased cells. Other sulfur radioisotopes, such as sulfur-32 (32S) and sulfur-33 (33S), are also used in medical applications, although they are less commonly used than 35S.

In the medical field, a cicatrix is a scar that forms after the healing of a wound or injury. It is typically a raised, thickened area of skin that is usually pale or lighter in color than the surrounding skin. Cicatrices can be caused by a variety of factors, including surgery, burns, acne, and skin infections. They can range in size and appearance, and may be permanent or fade over time. In some cases, cicatrices may cause discomfort or interfere with the function of the affected area. Treatment options for cicatrices may include topical creams, laser therapy, or surgical procedures.

Decorin is a protein that is found in the extracellular matrix of connective tissues in the human body. It is a member of the small leucine-rich proteoglycan (SLRP) family of proteins, which are involved in the regulation of tissue structure and function. Decorin is primarily found in the skin, where it plays a role in maintaining the integrity of the dermis and preventing the excessive accumulation of collagen fibers. It is also found in other connective tissues, such as tendons, ligaments, and cartilage. In the medical field, decorin is of interest because it has been implicated in a number of diseases and conditions, including skin disorders, such as psoriasis and scleroderma, as well as joint disorders, such as osteoarthritis and rheumatoid arthritis. It is also being studied as a potential target for the development of new treatments for these conditions.

Syndecan-4 is a transmembrane protein that is expressed on the surface of many different types of cells, including epithelial cells, endothelial cells, and fibroblasts. It is a member of the syndecan family of proteoglycans, which are large, complex molecules that are composed of a core protein and a variety of attached carbohydrates. Syndecan-4 plays a number of important roles in the body. One of its main functions is to serve as a receptor for various growth factors and other signaling molecules, which can bind to the protein and trigger a variety of cellular responses. It is also involved in the regulation of cell adhesion and migration, and has been implicated in a number of different diseases and conditions, including cancer, cardiovascular disease, and inflammatory disorders. In the medical field, syndecan-4 is the subject of ongoing research, and there is interest in developing drugs and therapies that target the protein in order to treat various diseases and conditions.

Glucosamine is a naturally occurring amino sugar that is found in the shells of crustaceans and in the cartilage of animals. It is also synthesized in the human body from the amino acid glutamine and the sugar glucose. In the medical field, glucosamine is often used as a dietary supplement to support joint health and reduce the symptoms of osteoarthritis, a degenerative joint disease that affects millions of people worldwide. It is believed to work by stimulating the production of proteoglycans, which are essential components of cartilage that help to cushion and lubricate joints. There is some evidence to suggest that glucosamine may be effective in reducing joint pain and stiffness, improving joint function, and slowing the progression of osteoarthritis. However, more research is needed to confirm these effects and to determine the optimal dosage and duration of treatment. It is important to note that glucosamine supplements are not regulated by the FDA and may contain varying amounts of the active ingredient. Therefore, it is important to choose a high-quality supplement from a reputable manufacturer and to consult with a healthcare provider before starting any new supplement regimen.

Biglycan is a proteoglycan, which is a complex molecule made up of proteins and carbohydrates. It is a type of small leucine-rich proteoglycan (SLRP) that is found in the extracellular matrix of connective tissues in the body. In the medical field, biglycan is known to play a role in the regulation of cell growth and differentiation, as well as in the formation and maintenance of tissues such as cartilage, bone, and blood vessels. It has also been implicated in various diseases, including osteoarthritis, atherosclerosis, and certain types of cancer.

Syndecan-1 is a type of cell surface proteoglycan that plays a role in cell adhesion, migration, and signaling. It is expressed on the surface of many different types of cells, including epithelial cells, endothelial cells, and fibroblasts. Syndecan-1 is composed of a core protein and a number of covalently attached glycosaminoglycan chains, which give it a complex and dynamic structure. In the medical field, syndecan-1 is of interest because it is involved in a number of different diseases and conditions, including cancer, cardiovascular disease, and inflammatory disorders. It is also being studied as a potential therapeutic target for the treatment of these conditions.

Glycosides are a class of organic compounds that are formed by the attachment of a sugar molecule (a glycosyl group) to a non-sugar molecule (a aglycone). In the medical field, glycosides are often found in plants and are used for a variety of therapeutic purposes, including as heart medications, diuretics, and anti-inflammatory agents. One of the most well-known examples of a glycoside is digitalis, which is derived from the foxglove plant and is used to treat heart failure and atrial fibrillation. Digitalis works by slowing down the heart rate and strengthening the contractions of the heart muscle, which can help to improve blood flow and reduce symptoms of heart failure. Other examples of glycosides used in medicine include strophanthin, which is used as a heart medication, and glycyrrhizin, which is used as an anti-inflammatory agent and to treat liver disease. Glycosides can be synthesized in the laboratory or obtained from natural sources, and they are often used in combination with other medications to enhance their therapeutic effects or to reduce their side effects. However, glycosides can also have toxic effects if they are not used properly, so they must be prescribed and monitored carefully by a healthcare professional.

Hyaluronoglucosaminidase (also known as hyaluronidase) is an enzyme that breaks down hyaluronic acid, a complex carbohydrate found in the extracellular matrix of connective tissue. It is primarily produced by cells in the immune system, such as neutrophils and macrophages, and is involved in the process of inflammation. In the medical field, hyaluronoglucosaminidase is used as a diagnostic tool to detect and monitor certain diseases, such as cancer, rheumatoid arthritis, and osteoarthritis. It is also used in certain medical procedures, such as tissue repair and wound healing, to break down hyaluronic acid and facilitate the migration of cells to the site of injury. In addition, hyaluronoglucosaminidase has been studied for its potential therapeutic applications in various diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. However, more research is needed to fully understand its role in these conditions and to develop effective treatments.

Chlorates are a class of inorganic salts that contain the chlorate ion (ClO3-). They are typically white or colorless solids that are soluble in water. Chlorates are used in a variety of applications, including as oxidizing agents, water treatment chemicals, and as ingredients in some medications. In the medical field, chlorates are sometimes used as a treatment for certain types of heart rhythm disorders, such as atrial fibrillation. They work by slowing down the electrical activity in the heart, which can help to regulate the heart's rhythm. Chlorates are also used as a source of chlorine in the production of certain medications, such as chloramphenicol. However, it is important to note that chlorates can also have toxic effects on the body, particularly on the thyroid gland. High levels of chlorate exposure can lead to hypothyroidism, which is a condition in which the thyroid gland does not produce enough thyroid hormones. As a result, chlorates are typically used with caution in medical settings, and their use is closely monitored by healthcare professionals.

Syndecan-2 is a type of cell surface proteoglycan that plays a role in cell adhesion, migration, and signaling. It is expressed on the surface of many different types of cells, including epithelial cells, endothelial cells, and fibroblasts. Syndecan-2 is composed of a core protein and a number of covalently attached glycosaminoglycan chains, which give it a complex and dynamic structure. In the medical field, syndecan-2 is of interest because it has been implicated in a number of different diseases and conditions, including cancer, cardiovascular disease, and inflammatory disorders. For example, changes in the expression or function of syndecan-2 have been observed in many types of cancer, and it is thought to play a role in the progression and metastasis of these diseases. Additionally, syndecan-2 has been shown to be involved in the regulation of blood vessel formation, which is important for the development of cardiovascular disease. Overall, syndecan-2 is an important molecule that plays a role in many different cellular processes, and its study is of great interest in the medical field.

Glypicans are a family of proteoglycans that are found in the extracellular matrix of animals. They are composed of a core protein with attached glycosaminoglycan chains, which give them their unique properties. Glypicans play important roles in a variety of biological processes, including cell signaling, cell adhesion, and tissue development. They are also involved in the regulation of growth and differentiation, and have been implicated in a number of diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. In the medical field, glypicans are being studied as potential targets for the development of new therapies for these and other diseases.

Nerve tissue proteins are proteins that are found in nerve cells, also known as neurons. These proteins play important roles in the structure and function of neurons, including the transmission of electrical signals along the length of the neuron and the communication between neurons. There are many different types of nerve tissue proteins, each with its own specific function. Some examples of nerve tissue proteins include neurofilaments, which provide structural support for the neuron; microtubules, which help to maintain the shape of the neuron and transport materials within the neuron; and neurofilament light chain, which is involved in the formation of neurofibrillary tangles, which are a hallmark of certain neurodegenerative diseases such as Alzheimer's disease. Nerve tissue proteins are important for the proper functioning of the nervous system and any disruption in their production or function can lead to neurological disorders.

Uronic acids are a type of carbohydrate that are found in the human body. They are composed of a uronic acid residue, which is a type of carboxylic acid, and a sugar residue. Uronic acids are important components of the extracellular matrix, which is the network of proteins and carbohydrates that surrounds cells in the body. They are also found in the cell walls of plants and bacteria. There are two main types of uronic acids: glucuronic acid and galacturonic acid. Glucuronic acid is the most common type and is found in many different types of molecules, including glycosaminoglycans, proteoglycans, and certain types of lipids. Galacturonic acid is found in pectin, a type of carbohydrate that is found in the cell walls of plants. Uronic acids play important roles in many different biological processes, including cell signaling, inflammation, and the formation and maintenance of tissues. They are also involved in the metabolism of certain drugs and toxins.

Oligosaccharides are short chains of sugar molecules that are composed of three to ten monosaccharide units. They are also known as "oligos" or "short-chain carbohydrates." In the medical field, oligosaccharides have been studied for their potential health benefits, including their ability to improve gut health, boost the immune system, and reduce the risk of chronic diseases such as diabetes and obesity. Some specific types of oligosaccharides that have been studied in the medical field include: 1. Prebiotics: These are oligosaccharides that selectively stimulate the growth of beneficial bacteria in the gut, such as Bifidobacteria and Lactobacilli. 2. Galactooligosaccharides (GOS): These are oligosaccharides that are found naturally in breast milk and have been shown to improve gut health and immune function in infants. 3. Fructooligosaccharides (FOS): These are oligosaccharides that are found in many fruits and vegetables and have been shown to improve gut health and reduce the risk of chronic diseases. Overall, oligosaccharides are an important class of carbohydrates that have potential health benefits and are being studied in the medical field for their potential therapeutic applications.

Syndecan-3 is a type of transmembrane proteoglycan that is expressed on the surface of many different types of cells, including epithelial cells, endothelial cells, and fibroblasts. It is a member of the syndecan family of cell surface proteoglycans, which are involved in a variety of cellular processes, including cell adhesion, migration, and signaling. In the medical field, syndecan-3 is of interest because it has been implicated in a number of different diseases and conditions. For example, it has been shown to play a role in the development of certain types of cancer, including breast cancer and colon cancer. It is also involved in the regulation of the immune system and has been implicated in the development of autoimmune diseases such as rheumatoid arthritis. In addition to its role in disease, syndecan-3 is also being studied for its potential therapeutic applications. For example, it has been shown to have anti-inflammatory properties and is being investigated as a potential treatment for inflammatory diseases such as rheumatoid arthritis and inflammatory bowel disease. It is also being studied as a potential target for cancer therapy, as it is overexpressed in many types of cancer cells.

In the medical field, Nitrous Acid (also known as Nitric Oxide Dioxide or Nitrous Dioxide) is a chemical compound with the formula HNO2. It is a colorless gas that is highly reactive and can be produced by the reaction of nitric oxide (NO) with oxygen (O2) in the presence of water (H2O). Nitrous Acid is not commonly used in medicine, but it has been studied for its potential therapeutic effects. It has been shown to have anti-inflammatory and analgesic properties, and it has been used in the treatment of certain types of cancer and inflammatory bowel disease. However, Nitrous Acid is also a toxic gas that can cause respiratory distress and other health problems if inhaled in high concentrations. Therefore, its use in medicine is carefully regulated and monitored to ensure its safe and effective use.

Monoclonal antibodies (mAbs) are laboratory-made proteins that can mimic the immune system's ability to fight off harmful pathogens, such as viruses and bacteria. They are produced by genetically engineering cells to produce large quantities of a single type of antibody, which is specific to a particular antigen (a molecule that triggers an immune response). In the medical field, monoclonal antibodies are used to treat a variety of conditions, including cancer, autoimmune diseases, and infectious diseases. They can be administered intravenously, intramuscularly, or subcutaneously, depending on the condition being treated. Monoclonal antibodies work by binding to specific antigens on the surface of cells or pathogens, marking them for destruction by the immune system. They can also block the activity of specific molecules involved in disease processes, such as enzymes or receptors. Overall, monoclonal antibodies have revolutionized the treatment of many diseases, offering targeted and effective therapies with fewer side effects than traditional treatments.

Glucuronidase is an enzyme that breaks down glucuronides, which are conjugated forms of various substances, including drugs, hormones, and toxins. In the medical field, glucuronidase is often used as a diagnostic tool to detect the presence of specific substances in the body. For example, in the field of forensic toxicology, glucuronidase can be used to detect the presence of drugs such as cocaine, amphetamines, and opioids in biological samples, such as urine or blood. This is because these drugs are often metabolized in the body by conjugation with glucuronic acid, forming glucuronides. By measuring the levels of glucuronides in a sample, forensic toxicologists can determine whether a person has recently used these drugs. In addition to its use in forensic toxicology, glucuronidase is also used in the treatment of certain medical conditions. For example, in the treatment of certain types of cancer, glucuronidase can be used to break down conjugated toxins that have accumulated in the body, potentially reducing their toxicity and improving patient outcomes.

Sulfatases are a group of enzymes that catalyze the hydrolysis of sulfate esters. In the medical field, sulfatases are important because they play a role in the metabolism of various compounds, including hormones, lipids, and carbohydrates. There are several types of sulfatases, each with its own specific substrate and function. For example, arylsulfatase A is involved in the metabolism of glycosaminoglycans, which are important components of connective tissue. Deficiency of arylsulfatase A can lead to a rare genetic disorder called metachromatic leukodystrophy. Another example is heparan sulfate sulfatase, which is involved in the degradation of heparan sulfate proteoglycans, which are important for cell signaling and tissue development. Deficiency of heparan sulfate sulfatase can lead to a rare genetic disorder called mucopolysaccharidosis type VII. Sulfatases are also important in the treatment of certain diseases. For example, the enzyme heparanase is involved in the degradation of heparan sulfate proteoglycans, which can promote tumor growth and metastasis. Inhibitors of heparanase are being developed as potential cancer therapies. Overall, sulfatases play a critical role in many biological processes and are important targets for research and therapy in the medical field.

Acetylgalactosamine (GalNAc) is a type of sugar molecule that is found in the human body. It is a component of many glycoproteins and glycolipids, which are complex carbohydrates that are attached to proteins and lipids, respectively. GalNAc is also a building block of the polysaccharide chondroitin sulfate, which is found in the extracellular matrix of many tissues, including cartilage and the brain. In the medical field, GalNAc is used as a substrate for the synthesis of certain drugs, such as those used to treat viral infections and cancer. It is also being studied as a potential target for the development of new therapies for a variety of diseases, including diabetes, obesity, and neurodegenerative disorders.

Sulfuric acid is a strong acid that is commonly used in the medical field for various purposes. It is a colorless, odorless, and corrosive liquid that is highly soluble in water. In the medical field, sulfuric acid is used as a chemical reagent in various laboratory procedures, such as the preparation of buffers, the extraction of proteins, and the analysis of biological samples. It is also used as a component in some medications, such as certain antacids and laxatives. However, sulfuric acid is highly caustic and can cause severe burns and tissue damage if it comes into contact with the skin or eyes. Therefore, it is important to handle sulfuric acid with extreme caution and to follow proper safety protocols when working with it.

Chondrosarcoma is a type of cancer that arises from cartilage cells in the body. It is a rare cancer that typically affects adults, although it can occur in children as well. Chondrosarcoma can develop in any part of the body where cartilage is present, but it most commonly occurs in the bones of the pelvis, shoulder, and thigh. Chondrosarcoma is classified into different grades based on how aggressive the cancer is and how quickly it grows. Grade I chondrosarcomas are slow-growing and have a good prognosis, while grade II and III chondrosarcomas are more aggressive and have a poorer prognosis. Treatment for chondrosarcoma typically involves surgery to remove the tumor, followed by radiation therapy or chemotherapy to kill any remaining cancer cells. The prognosis for chondrosarcoma depends on the grade of the cancer, the location of the tumor, and the patient's overall health.

N-Acetylgalactosaminyltransferases (NAGT) are a family of enzymes that transfer the N-acetylgalactosamine (GalNAc) residue from UDP-GalNAc to specific acceptor molecules, such as glycoproteins and glycolipids. These enzymes play a crucial role in the biosynthesis of complex carbohydrates, also known as glycans, which are essential for many cellular processes, including cell-cell recognition, signaling, and immune function. In the medical field, NAGTs are of particular interest because defects in these enzymes can lead to a group of rare genetic disorders known as mucopolysaccharidoses (MPSs). MPSs are characterized by the accumulation of undegraded glycosaminoglycans (GAGs) in the lysosomes of cells, leading to a range of symptoms, including skeletal abnormalities, intellectual disability, and organ dysfunction. NAGT deficiencies are responsible for several forms of MPS, including MPS I, MPS II, and MPS VII. In addition to their role in MPSs, NAGTs are also being studied for their potential therapeutic applications in other diseases, such as cancer and neurodegenerative disorders. For example, some researchers are exploring the use of NAGT inhibitors as targeted therapies for cancer, as these enzymes are often upregulated in cancer cells and are involved in processes such as cell proliferation and invasion.

Iduronic acid is a naturally occurring uronic acid that is found in the glycosaminoglycan chains of proteoglycans in connective tissue. It is a derivative of glucuronic acid, which is a common component of many polysaccharides in the body. Iduronic acid is involved in the formation and maintenance of connective tissue, and it plays a role in the regulation of cell signaling and the immune response. In the medical field, iduronic acid is sometimes used as a diagnostic tool to study the structure and function of connective tissue, and it may also be used as a therapeutic agent to treat certain conditions that affect the connective tissue, such as osteoarthritis and rheumatoid arthritis.

Phosphoadenosine phosphosulfate (PAPS) is a molecule that plays a crucial role in the metabolism of sulfur-containing amino acids and other sulfur-containing compounds in the body. It is synthesized from adenosine triphosphate (ATP) and sulfate, and is involved in the formation of various sulfur-containing molecules, such as glutathione, coenzyme A, and sulfated glycosaminoglycans. In the medical field, PAPS is often studied in the context of various diseases and disorders, including cystic fibrosis, where it is involved in the metabolism of the amino acid cysteine. PAPS is also involved in the metabolism of drugs and xenobiotics, and its levels can be used as a biomarker for certain diseases, such as liver disease and cancer. Additionally, PAPS is a target for the development of new drugs for the treatment of various diseases, including cancer and inflammatory disorders.

Collagen is a protein that is found in the extracellular matrix of connective tissues throughout the body. It is the most abundant protein in the human body and is responsible for providing strength and support to tissues such as skin, bones, tendons, ligaments, and cartilage. In the medical field, collagen is often used in various medical treatments and therapies. For example, it is used in dermal fillers to plump up wrinkles and improve skin texture, and it is also used in wound healing to promote tissue regeneration and reduce scarring. Collagen-based products are also used in orthopedic and dental applications, such as in the production of artificial joints and dental implants. In addition, collagen is an important biomarker for various medical conditions, including osteoporosis, rheumatoid arthritis, and liver disease. It is also used in research to study the mechanisms of tissue repair and regeneration, as well as to develop new treatments for various diseases and conditions.

Fibroblast Growth Factor 2 (FGF2) is a protein that plays a crucial role in the growth and development of various tissues in the human body. It is a member of the fibroblast growth factor family of proteins, which are involved in a wide range of biological processes, including cell proliferation, differentiation, migration, and survival. In the medical field, FGF2 is often studied in relation to various diseases and conditions, including cancer, cardiovascular disease, and neurological disorders. For example, FGF2 has been shown to promote the growth and survival of cancer cells, making it a potential target for cancer therapy. It has also been implicated in the development of cardiovascular disease, as it can stimulate the growth of blood vessels and contribute to the formation of atherosclerotic plaques. In addition, FGF2 plays a role in the development and maintenance of the nervous system, and has been implicated in various neurological disorders, including Alzheimer's disease, Parkinson's disease, and multiple sclerosis. It is also involved in the regulation of bone growth and remodeling, and has been studied in the context of osteoporosis and other bone diseases. Overall, FGF2 is a complex and multifaceted protein that plays a critical role in many different biological processes, and its function and regulation are the subject of ongoing research in the medical field.

In the medical field, "Disease Models, Animal" refers to the use of animals to study and understand human diseases. These models are created by introducing a disease or condition into an animal, either naturally or through experimental manipulation, in order to study its progression, symptoms, and potential treatments. Animal models are used in medical research because they allow scientists to study diseases in a controlled environment and to test potential treatments before they are tested in humans. They can also provide insights into the underlying mechanisms of a disease and help to identify new therapeutic targets. There are many different types of animal models used in medical research, including mice, rats, rabbits, dogs, and monkeys. Each type of animal has its own advantages and disadvantages, and the choice of model depends on the specific disease being studied and the research question being addressed.

Hexosamines are a type of sugar molecule that are found in the human body. They are composed of a hexose (a sugar with six carbon atoms) and an amine group. Hexosamines are important components of the glycosaminoglycan (GAG) molecules that are found in the extracellular matrix of connective tissue. GAGs are complex carbohydrates that play a variety of roles in the body, including providing structural support to tissues, regulating cell signaling, and participating in the immune response. Hexosamines are also found in other types of molecules, such as glycoproteins and proteoglycans. In the medical field, hexosamines are of interest because they have been implicated in a number of diseases, including cancer, diabetes, and inflammatory disorders.

Dextran sulfate is a polysaccharide compound that is derived from the bacterial fermentation of cornstarch. It is used in a variety of medical applications, including as a diagnostic tool for detecting blood clots, as an anticoagulant to prevent blood clots from forming, and as a component of certain types of chemotherapy drugs. Dextran sulfate is also used in the treatment of certain types of liver disease, such as cirrhosis, by helping to reduce the buildup of scar tissue in the liver. In addition, it has been studied for its potential use in the treatment of certain types of cancer, such as colon cancer, by helping to stimulate the immune system to attack cancer cells.

Membrane glycoproteins are proteins that are attached to the cell membrane through a glycosyl group, which is a complex carbohydrate. These proteins play important roles in cell signaling, cell adhesion, and cell recognition. They are involved in a wide range of biological processes, including immune response, cell growth and differentiation, and nerve transmission. Membrane glycoproteins can be classified into two main types: transmembrane glycoproteins, which span the entire cell membrane, and peripheral glycoproteins, which are located on one side of the membrane.

Glycoproteins are a type of protein that contains one or more carbohydrate chains covalently attached to the protein molecule. These carbohydrate chains are made up of sugars and are often referred to as glycans. Glycoproteins play important roles in many biological processes, including cell signaling, cell adhesion, and immune response. They are found in many different types of cells and tissues throughout the body, and are often used as markers for various diseases and conditions. In the medical field, glycoproteins are often studied as potential targets for the development of new drugs and therapies.

Fibronectins are a family of large, soluble glycoproteins that are found in the extracellular matrix of connective tissues. They are synthesized by a variety of cells, including fibroblasts, endothelial cells, and epithelial cells, and are involved in a wide range of cellular processes, including cell adhesion, migration, and differentiation. Fibronectins are composed of two large subunits, each containing three distinct domains: an N-terminal domain, a central domain, and a C-terminal domain. The central domain contains a high-affinity binding site for fibronectin receptors on the surface of cells, which allows cells to adhere to the extracellular matrix and migrate through it. Fibronectins play a critical role in the development and maintenance of tissues, and are involved in a variety of pathological processes, including wound healing, tissue fibrosis, and cancer. They are also important in the immune response, as they can bind to and activate immune cells, and can modulate the activity of various cytokines and growth factors.

Glucuronic acid is a naturally occurring organic acid that is produced by the liver as a byproduct of the metabolism of carbohydrates. It is a key component of the glycoprotein molecule hyaluronic acid, which is found in the extracellular matrix of connective tissue throughout the body. In the medical field, glucuronic acid is often used as a precursor in the synthesis of other important molecules, such as bile acids and some hormones. It is also used in the treatment of certain medical conditions, such as hyperuricemia (high levels of uric acid in the blood), where it is used to convert excess uric acid into a more water-soluble form that can be excreted from the body. In addition, glucuronic acid is used in the production of certain drugs and dietary supplements, and it has been shown to have potential anti-inflammatory and anti-cancer effects in laboratory studies. However, more research is needed to fully understand the therapeutic potential of glucuronic acid in the treatment of human diseases.

Recombinant proteins are proteins that are produced by genetically engineering bacteria, yeast, or other organisms to express a specific gene. These proteins are typically used in medical research and drug development because they can be produced in large quantities and are often more pure and consistent than proteins that are extracted from natural sources. Recombinant proteins can be used for a variety of purposes in medicine, including as diagnostic tools, therapeutic agents, and research tools. For example, recombinant versions of human proteins such as insulin, growth hormones, and clotting factors are used to treat a variety of medical conditions. Recombinant proteins can also be used to study the function of specific genes and proteins, which can help researchers understand the underlying causes of diseases and develop new treatments.

Polysaccharides are complex carbohydrates that are composed of long chains of monosaccharide units linked together by glycosidic bonds. They are found in many different types of biological materials, including plant cell walls, animal tissues, and microorganisms. In the medical field, polysaccharides are often used as drugs or therapeutic agents, due to their ability to modulate immune responses, promote wound healing, and provide other beneficial effects. Some examples of polysaccharides that are used in medicine include hyaluronic acid, chondroitin sulfate, heparin, and dextran.

Laminin is a type of protein that is found in the basement membrane, which is a thin layer of extracellular matrix that separates tissues and organs in the body. It is a major component of the extracellular matrix and plays a crucial role in maintaining the structural integrity of tissues and organs. Laminin is a large, complex protein that is composed of several subunits. It is synthesized by cells in the basement membrane and is secreted into the extracellular space, where it forms a network that provides support and stability to cells. In the medical field, laminin is of great interest because it is involved in a number of important biological processes, including cell adhesion, migration, and differentiation. It is also involved in the development and maintenance of many different types of tissues, including the nervous system, skeletal muscle, and the cardiovascular system. Laminin has been the subject of extensive research in the medical field, and its role in various diseases and conditions is being increasingly understood. For example, laminin has been implicated in the development of certain types of cancer, as well as in the progression of neurodegenerative diseases such as Alzheimer's and Parkinson's. As a result, laminin is a potential target for the development of new therapies for these and other diseases.

Xylose is a type of sugar that is found in the cell walls of plants. It is a monosaccharide, which means it is a simple sugar made up of one molecule of carbon, hydrogen, and oxygen. In the medical field, xylose is sometimes used as a diagnostic tool to test for certain conditions, such as celiac disease or malabsorption syndromes. In these tests, a person is given a solution containing xylose and then their blood is tested to see how well their body is able to absorb it. If the body is not able to absorb xylose properly, it may be a sign of an underlying medical condition.

Glycoside hydrolases are a group of enzymes that catalyze the hydrolysis of glycosidic bonds in carbohydrates. These enzymes are involved in a wide range of biological processes, including digestion, metabolism, and signaling. In the medical field, glycoside hydrolases are often used as diagnostic tools to study carbohydrate metabolism and to develop new treatments for diseases related to carbohydrate metabolism, such as diabetes and obesity. They are also used in the production of biofuels and other industrial products.

Lipoprotein lipase (LPL) is an enzyme that plays a crucial role in the metabolism of lipids (fats) in the human body. It is primarily found in the capillary endothelial cells of adipose tissue (fat tissue) and muscle tissue, where it is responsible for hydrolyzing triglycerides (fatty acids) from circulating lipoproteins, such as chylomicrons and very low-density lipoproteins (VLDL). The hydrolysis of triglycerides by LPL releases free fatty acids, which can then be taken up by adipose tissue and muscle cells for energy production or storage. LPL also plays a role in the metabolism of high-density lipoproteins (HDL), the "good" cholesterol, by hydrolyzing triglycerides in HDL particles. Abnormalities in LPL activity can lead to a variety of metabolic disorders, including hypertriglyceridemia (elevated levels of triglycerides in the blood), familial chylomicronemia syndrome, and lipemia retinalis. In addition, LPL has been implicated in the development of atherosclerosis, a condition characterized by the buildup of plaque in the arteries, which can lead to heart attack and stroke.

Sulfur isotopes are atoms of sulfur that have different numbers of neutrons in their nuclei, resulting in different atomic masses. In the medical field, sulfur isotopes are often used in diagnostic imaging techniques, such as positron emission tomography (PET) scans. For example, sulfur-35 (35S) and sulfur-75 (75S) are commonly used as tracers to study the metabolism of sulfur-containing compounds in the body, such as amino acids and neurotransmitters. These isotopes can be administered to a patient in the form of a radiolabeled compound, and the distribution and metabolism of the compound can be monitored using PET imaging. This information can be used to diagnose and monitor a variety of medical conditions, including neurological disorders, cancer, and cardiovascular disease.

Chondroitin sulfate proteoglycans (CSPGs) are proteoglycans consisting of a protein core and a chondroitin sulfate side chain. ... Chondroitin sulfate proteoglycans are composed of a core protein and a sugar side chain. The core protein is generally a ... Chondroitin sulfate proteoglycans have been implicated in Alzheimer's disease, stroke, and epilepsy. The two primary markers of ... Galtrey, C. M.; Fawcett, J. W. (2007). "The role of chondroitin sulfate proteoglycans in regeneration and plasticity in the ...
"Biosynthesis of the chondroitin sulfate proteoglycan. Purification and properties of xylosyltransferase". J. Biol. Chem. 247 ( ... This enzyme participates in the biosynthesis of chondroitin sulfate and glycan structures. XYLT1 XYLT2 Xylosyltransferase ... proteoglycan core protein beta-d-xylosyltransferase and its first isoform XT-II". J. Mol. Biol. 304 (4): 517-28. doi:10.1006/ ... proteoglycan core protein beta-D-xylosyltransferase, UDP-xylose-core protein beta-D-xylosyltransferase, uridine diphosphoxylose ...
Chondroitin sulfate proteoglycan 4, also known as melanoma-associated chondroitin sulfate proteoglycan (MCSP) or neuron-glial ... "Entrez Gene: CSPG4 chondroitin sulfate proteoglycan 4". Nishiyama A, Dahlin KJ, Prince JT, Johnstone SR, Stallcup WB (July 1991 ... Iida J, Pei D, Kang T, Simpson MA, Herlyn M, Furcht LT, McCarthy JB (June 2001). "Melanoma chondroitin sulfate proteoglycan ... Legg J, Jensen UB, Broad S, Leigh I, Watt FM (December 2003). "Role of melanoma chondroitin sulphate proteoglycan in patterning ...
PMID 14501214 Levine JM, Nishiyama A. "The NG2 chondroitin sulfate proteoglycan: a multifunctional proteoglycan associated with ... "Chondroitin sulphate proteoglycans: inhibitory components of the glial scar." Prog Brain Res. 2001;132:611-9. PMID 11545024. ... "NG2 is a major chondroitin sulfate proteoglycan produced after spinal cord injury and is expressed by macrophages and ... "Increased expression of the NG2 chondroitin-sulfate proteoglycan after brain injury." J. Neurosci. 1994 Aug;14(8):4716-30. PMID ...
One of the many inhibitory cues includes chondroitin sulfate proteoglycans (CSPGs). Neurons growing in culture become more able ... Jain A, Brady-Kalnay SM, Bellamkonda RV (2004). "Modulation of Rho GTPase activity alleviates chondroitin sulfate proteoglycan- ...
PNNs are composed of a condensed matrix of chondroitin sulfate proteoglycans, molecules that consist of a core protein and a ... Extracellular matrix Chondroitin sulfate proteoglycans Critical period Synaptic plasticity Flores, CE; Méndez, P (2014). " ... Galtrey, C. M.; Fawcett, J. W. (2007). "The role of chondroitin sulfate proteoglycans in regeneration and plasticity in the ... They are largely negatively charged and composed of chondroitin sulfate proteoglycans, molecules that play a key role in ...
This enzyme is also called chondroitin glucuronyltransferase II. This enzyme participates in chondroitin sulfate biosynthesis ... "Molecular cloning and characterization of a novel chondroitin sulfate glucuronyltransferase that transfers glucuronic acid to N ... In enzymology, a N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase (EC 2.4.1.226) is an enzyme that catalyzes ... DeAngelis PL, Padgett-McCue AJ (2000). "Identification and molecular cloning of a chondroitin synthase from Pasteurella ...
... has been shown to interact with: chondroitin sulphate proteoglycans, PTPRD, glial-derived and liprin-alpha-1. NME2. ... "NME2 associates with PTPσ to transduce signals from chondroitin sulfate proteoglycans". Biochemical and Biophysical Research ... "Modulation of the proteoglycan receptor PTPσ promotes recovery after spinal cord injury". Nature. 518 (7539): 404-8. doi: ...
It also cleaves chondroitin sulfate, heparan sulfate and proteoglycans of the basal membrane. Cathepsin S plays an active role ...
The most common GAGs are chondroitin sulfate and keratin sulfate. Proteoglycans attach to a central chain, usually hyaluronic ... Proteoglycans: Proteoglycans are the second most abundant macromolecule in the ECM of cartilage. Proteoglycans consist of a ... Proteoglycans are hydrophilic and therefore attract and restrain water molecules. This provides cartilage with its intrinsic ... Each type of cartilage has varying concentrations of components such as proteoglycans, collagen and water which determine its ...
"Myosin II activity regulates neurite outgrowth and guidance in response to chondroitin sulfate proteoglycans". Journal of ...
Chondroitin sulfate proteoglycan 5 is a protein that in humans is encoded by the CSPG5 gene. CSPG5 has been shown to interact ... "Entrez Gene: CSPG5 chondroitin sulfate proteoglycan 5 (neuroglycan C)". Hassel, Burkhard; Schreff Matthias; Stube Eva-Maria; ... a transmembrane chondroitin sulfate proteoglycan, in the human brain". J. Neurosci. Res. 83 (1): 110-8. doi:10.1002/jnr.20698. ... a neural transmembrane chondroitin sulfate proteoglycan with an EGF module". Neurosci Res. 32 (4): 313-22. doi:10.1016/S0168- ...
Iida J, Pei D, Kang T (2001). "Melanoma chondroitin sulfate proteoglycan regulates matrix metalloproteinase-dependent human ...
Like the chondroitin sulfate proteoglycans, keratan sulfate proteoglycan (KSPG) production is up regulated in reactive ... Chondroitin sulfate proteoglycans (CSPGs) have been shown to be up regulated in the central nervous system (CNS) following ... In response to scar-inducing factors, astrocytes up regulate the production of chondroitin sulfate proteoglycans. Astrocytes ... It is also 6-sulfated. This sulfation is crucial to the elongation of the keratan sulfate chain. A study was done using N- ...
Chondroitin and glucosamine are also used in veterinary medicine for osteoarthritis. Proteoglycan Heparin sulfate - a ... "Chondroitin sulfate B" is an old name for dermatan sulfate, and it is no longer classified as a form of chondroitin sulfate. ... Although the name "chondroitin sulfate" suggests a salt with a sulfate counter-anion, this is not the case, as sulfate is ... Furthermore, marine chondroitin sulfate chains tend to be longer, with molecular weight of up to 70 kDa in chondroitin sulfate ...
... (ACAN), also known as cartilage-specific proteoglycan core protein (CSPCP) or chondroitin sulfate proteoglycan 1, is a ... proteoglycan. It exhibits a bottlebrush structure, in which chondroitin sulfate and keratan sulfate glycosaminoglycan (GAG) ... This gene is a member of the lectican (chondroitin sulfate proteoglycan) family. The encoded protein is an integral part of the ... Kirschfink M, Blase L, Engelmann S, Schwartz-Albiez R (1997). "Secreted chondroitin sulfate proteoglycan of human B cell lines ...
... and chondroitin sulfate. With the exception of hyaluronic acid, GAGs are bound to proteins called proteoglycans. Glycoproteins ... Important GAGs found in ground substance include hyaluronic acid, heparan sulfate, dermatan sulfate, ... Link proteins such as vinculin, spectrin and actomyosin stabilize the proteoglycans and organize elastic fibers in the ECM. ... Ground substance is primarily composed of water and large organic molecules, such as glycosaminoglycans (GAGs), proteoglycans, ...
The chondroitin sulfate functions as a component of proteoglycans, which helps to form the extracellular matrix. Integra can be ... Integra, originally used to only treat burns, consists of a collagen matrix and chondroitin sulfate that can be used as a skin ... "Chondroitin sulfate is a component of Integra® Dermal Regeneration Template". fdocuments.us. Retrieved 5 December 2020. " ...
1997). "A family of activity-dependent neuronal cell-surface chondroitin sulfate proteoglycans in cat visual cortex." Journal ... Jones LL, Margolis RU, Tuszynski MH (August 2003). "The chondroitin sulfate proteoglycans neurocan, brevican, phosphacan, and ... Particularly, extracellular matrix protein deposition (laminin, fibronectin, and chondroitin sulfate proteoglycans) was closer ... Moreover, reduced astrocyte proliferation decreases expression of chondroitin sulfate proteoglycans (CSPGs), major ...
Legg J, Jensen UB, Broad S, Leigh I, Watt FM (December 2003). "Role of melanoma chondroitin sulphate proteoglycan in patterning ... May 2006). "Lack of expression of the chondroitin sulphate proteoglycan neuron-glial antigen 2 on candidate stem cell ...
2000). "Melanoma chondroitin sulphate proteoglycan regulates cell spreading through Cdc42, Ack-1 and p130cas". Nat. Cell Biol. ...
Ye Q, Miao QL (August 2013). "Experience-dependent development of perineuronal nets and chondroitin sulfate proteoglycan ... Perineuronal nets (PNNs) are structures in the extracellular matrix formed by chondroitin sulfate proteoglycans, hyaluronan, ...
... chondroitin sulfate proteoglycan protein families and consists of neurocan core protein and chondroitin sulfate. It is thought ... "The neuronal chondroitin sulfate proteoglycan neurocan binds to the neural cell adhesion molecules Ng-CAM/L1/NILE and N-CAM, ... aggregating chondroitin sulfate proteoglycan of brain". J Biol Chem. 267 (27): 19536-47. doi:10.1016/S0021-9258(18)41808-X. ...
... is also known as chondroitin sulfate proteoglycan core protein 2 or chondroitin sulfate proteoglycan 2 (CSPG2), and PG ... Versican is a large chondroitin sulfate proteoglycan with an apparent molecular mass of more than 1000kDa. In 1989, Zimmermann ... Krusius T, Gehlsen KR, Ruoslahti E (1987). "A fibroblast chondroitin sulfate proteoglycan core protein contains lectin-like and ... Because of their negatively charged sulfates or carboxyl groups, chondroitin sulfate chains are attracted to various positively ...
"Basement membrane zone type XV collagen is a disulfide-bonded chondroitin sulfate proteoglycan in human tissues and cultured ...
... is capable of cleaving all the large chondroitin sulfate hyaluronan-binding proteoglycans (CSPGs), including aggrecan, ... It can degrade aggrecan, a major proteoglycan of cartilage, brevican, a brain-specific extracellular matrix protein, neurocan ... ADAMTS4 (and ADAMTS5) are the major proteinases responsible for the degradation of proteoglycans in articular cartilage in ...
This gene encodes the protein core of a seminal plasma proteoglycan containing chondroitin- and heparan-sulfate chains. The ... "Entrez Gene: SPOCK1 sparc/osteonectin, cwcv and kazal-like domains proteoglycan (testican) 1". Périn JP, Alliel PM, Jollès P, ... Kohfeldt E, Maurer P, Vannahme C, Timpl R (1997). "Properties of the extracellular calcium binding module of the proteoglycan ... Alliel PM, Perin JP, Jollès P, Bonnet FJ (1993). "Testican, a multidomain testicular proteoglycan resembling modulators of cell ...
... a chondroitin sulfate proteoglycan of rat brain, occurs as secreted and cell surface glycosylphosphatidylinositol-anchored ... a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of ... Olin AI, Mörgelin M, Sasaki T, Timpl R, Heinegård D, Aspberg A (Jan 2001). "The proteoglycans aggrecan and Versican form ... Hu B, Kong LL, Matthews RT, Viapiano MS (Sep 2008). "The proteoglycan brevican binds to fibronectin after proteolytic cleavage ...
Chondroitin sulfate proteoglycans suppress the extension of axons over the glial scar, a barrier which develops after lesioning ... Cuellar K, Chuong H, Hubbell SM, Hinsdale ME (2007). "Biosynthesis of chondroitin and heparan sulfate in chinese hamster ovary ... Proteoglycans consist of one relatively small protein core and attached large glycosaminoglycan side chains. To block the very ... Grimpe B, Pressman Y, Lupa MD, Horn KP, Bunge MB, Silver J (2005). "The role of proteoglycans in Schwann cell/astrocyte ...
"Constitutive and TNF-inducible expression of chondroitin sulfate proteoglycan 4 in glioblastoma and neurospheres:Implications ... the studies have shown how the sulfate Proteoglycan 4 (CSPG4) in GBM is critical for tumor progression and metastasis. There is ...
Synonyms: Chondroitin sulfate proteoglycan 4, Chondroitin sulfate proteoglycan NG2, HMW-MAA, MCSP, MCSPG, ... ... Role of melanoma chondroitin sulphate proteoglycan in patterning stem cells in human interfollicular epidermis. Legg, J., ... Melanoma chondroitin sulfate proteoglycan enhances FAK and ERK activation by distinct mechanisms. Yang, J., Price, M.A., ... Melanoma chondroitin sulphate proteoglycan regulates cell spreading through Cdc42, Ack-1 and p130cas. Eisenmann, K.M., McCarthy ...
Hyaluronan and chondroitin sulfate proteoglycans in the supramolecular organization of the mammalian vitreous body. Connect ... Versican is a type of protein known as a proteoglycan, which means it has several sugar molecules attached to it. Versican is ... Versican: a versatile extracellular matrix proteoglycan in cell biology. Curr Opin Cell Biol. 2002 Oct;14(5):617-23. doi: ...
The murine Ia-associated chondroitin sulfate proteoglycan (CSPG) was studied both biochemically and immunochemically to ... Proteoglycans in cell-mediated cytotoxicity. Identification, localization, and exocytosis of a chondroitin sulfate proteoglycan ... Invariant chain is the core protein of the Ia-associated chondroitin sulfate proteoglycan. A J Sant, A J Sant ... The murine Ia-associated chondroitin sulfate proteoglycan (CSPG) was studied both biochemically and immunochemically to ...
Proteoglycans: Proteoglycans include heparin and chondroitin sulfate. The role of the latter is unknown; heparin seems to be ...
Chondroitin Sulfate Proteoglycan Immunoreactivity Increases Following Spinal Cord Injury and Transplantation (1999). ... Inhibiting Extracellular Matrix Molecule, Chondroitin Sulfate Proteoglycan, In Vivo. 1996 - 1997.. Professional Affiliations. ... potential role of chondroitin sulfate proteoglycans, specifically aggrecan.". Undergraduate Courses Taught. Principles of ... M.L. Lemons, J.D. Sandy, D.K. Anderson and D.R. Howland (2003). Intact aggrecan and chondroitin-sulfate depleted aggrecan ...
It consists of the core backbone glycan hyaluronic acid that attaches chondroitin sulfate proteoglycans and other proteins1,2. ... Semaphorin 3A binds to the perineuronal nets via chondroitin sulfate type E motifs in rodent brains. J. Biol. Chem. 288, 27384- ... Frischknecht, R. & Seidenbecher, C. I. Brevican: a key proteoglycan in the perisynaptic extracellular matrix of the brain. Int ...
Antibody-Mediated Inhibition of Infected Erythrocyte Adherence to Chondroitin Sulfate Proteoglycan. For an inhibition of ... intervillous space and on the villous surface of human placenta by binding to the low-sulfated chondroitin sulfate proteoglycan ... chondroitin sulfate proteoglycan [CSPG]; Sigma, St. Louis, MO, USA) and blocked with 3% BSA in PBS for 30 min. Late-stage FCR3 ... Dahlbäck M, Jørgensen LM, Nielsen MA, Clausen TM, Ditlev SB, Resende M, The chondroitin sulfate A-binding site of the VAR2CSA ...
Shark Cartilage is a source of Chondroitin Sulfate. It drives the Glucosamine and provide maximum absorption. Also, in many ... It stimulates the production of glycosaminoglycans and proteoglycans, two essential building blocks of cartilage. ... Chondroitin Sulfate reduces inflammation and assists the Glucosamine in protecting against future cartilage degeneration. ... Bovine Trachea can also be used as a source of Chondroitin, however, there is a risk of BSE (Mad Cow Disease). ...
Cultured astrocytes express biglycan, a chondroitin/dermatan sulfate proteoglycan supporting the survival of neocortical ...
These modified E. coli are capable of complete, essentially one-step biosynthesis of chondroitin sulfate at a variety of ... This is a major advantage over current production methods that depend on the natural distribution of chondroitin sulfate types ... The recombinant microorganisms are able produce all three components identified for chondroitin sulfate production - ... In order to produce chondroitin sulfate in an animal-free manner, engineered E. coli host cells were modified so as to reduce ...
Aggrecan belongs to the chondroitin sulfate (CS) proteoglycan family, which also includes Versican, Brevican, and Neurocan. ... It is the most abundant proteoglycan in cartilage, and contributes to the load-bearing capacity of this tissue. ... Each Aggrecan molecule contains approximately 100 and 30 keratan sulfate and glycosaminoglycan (GAG) sidechains, respectively. ...
Includes vegan glucosamine sulfate, chondroitin, and NAG, as well as vital... ... Vegan formula to support synthesis of elastin, glycosaminoglycans, hyaluronic acid, proteoglycans, and synovial fluid.* ...
Adany R, Heimer R, Caterson B, Sorrell JM and Iozzo RV: Altered expression of chondroitin sulfate proteoglycan in the stroma of ... In CRC, the components rich in connective tissues were found to have an accumulation of chondroitin sulphate proteoglycan. The ... Adany R and Iozzo RV: Hypomethylation of the decorin proteoglycan gene in human colon cancer. Biochem J. 276:301-306. 1991. ... Adany R and Iozzo RV: Altered methylation of versican proteoglycan gene in human colon carcinoma. Biochem Biophys Res Commun. ...
... including chondroitin sulfate proteoglycans (CSPGs), hyaluronic acid, and tenascins. They are detectable by various ... including chondroitin sulfate proteoglycans (CSPGs), hyaluronic acid, and tenascins. They are detectable by various ...
Sulfated polysaccharide. Sulfated lipids. Cadherins. Lens of Time: Velvet Worms-Secret of the Slime. Mesoglea. Mesohyl. ... also known as melanoma-associated chondroitin sulfate proteoglycan (MCSP), Mouse AN2, and Sea urchin ECM3.[2] This single-pass ... Sulfated proteoglycans. Sulfated polysaccharide. Sulfated lipids. Cadherins. Lens of Time: Velvet Worms-Secret of the Slime. ... Heparan sulfate - Wikipedia. Faculty. mIRN21 - Wikipedia. Chondroitin and Keratin Sulfate - Wheeless Textbook of Orthopaedics ...
M. Wagner, Universität Erlangen-Nürnberg, Germany); NG2 chondroitin sulfate proteoglycan (1:200 for IHC; CHEMICON ...
Loss of chondroitin sulfate is detrimental to the health of the disc as well as cells and nerves. Discat Plus Enhanced offers ... 57) Lower GAG accompanies disc degeneration and disc disorders (disc protrusion and extrusion). (58) Low proteoglycan (CS/GAG) ... Loss of Chondroitin Sulfate Is Detrimental. The loss of Chondroitin Sulfate (CS) is detrimental. CS is the glycosaminoglycan ( ... Chondroitin sulfate and disc herniation and degeneration is a large topic to study. Dr. Cox wrote another short article on ...
Consequently, supplemental glucosamine sulfate and chondroitin sulfate have been popular for years for the purpose of reducing ... Joint space loss as we age is known to be caused by a loss of proteoglycans, secondary to chronic inflammation and ...
It combines most popular anti-inflammatory agents such as Glucosamine, Chondroitin, MSM, vitamin, mineral and some Chinese ... Chondroitin Sulfate is part of a large protein molecule (proteoglycan) that gives cartilage elasticity. ... Glucosamine 1000 mg and Chondroitin Sulfate 134 mg are substances found naturally in the body. Glucosamine is a form of amino ... Studies have shown that a combination of Glucosamine and Chondroitin Sulfate reports pain relief at a level similar to that of ...
... chondroitin, and MSM in Pure Encapsulations Glucosamine with MSM. ... Chondroitin sulfate is responsible for building the ground ... Chondroitin sulfate is responsible for building the ground substance of cartilage, molecules known as proteogly-cans. Studies ... In addition, chondroitin sulfate may maintain healthy enzyme activity. An important role of sulfur from MSM is to enhance the ... Joint Motility and Function: Several studies indicate that the combination of glucosamine HCl and chondroitin sulfate has ...
... such as chondroitin sulfate B. Since these glycoproteins are present all over the cell membrane, they make the cell membrane ... Initially the CPPs and the cell membrane interact via electrostatic linkage to proteoglycans called as glycosaminoglycans (GAGs ...
They are divided in four groups: hyaluronic acid, keratan sulfate, chondroitin/dermatan sulfate, andheparan sulfate. ... The diversity of proteoglycans and their high interaction with growth factors and their receptors provides structural basis for ...
Now they are known as proteoglycans. My doctoral dissertation had to do with the biosynthesis of chondroitin sulfate, which is ... I think people who would be getting degrees and studying proteoglycans today are more likely to go onto postdocs in a related ... with embryonic chick cartilage looking at incorporation of radioactive precursors into the large polymer of chondroitin sulfate ... one of the proteoglycans, found prominently in cartilages, so the studies we did were ...
... heparan sulfate proteoglycan perlecan (Mertens et al., 1992), and chondroitin/dermatan sulfate proteoglycan biglycan (Whinna et ... Mertens, G., Cassiman, J.J., Van den Berghe, H., Vermylen, J. and David, G. (1992): Cell surface heparan sulfate proteoglycans ... sodium dodecyl sulfate, 150 mM NaCl, and 1 mM EDTA) supplemented with protease inhibitors (cOmplete™ ULTRA Tablets, Mini; Roche ... Arsenite but not arsenate inhibits general proteoglycan synthesis in cultured arterial smooth muscle cells. J. Toxicol. Sci., ...
In the present study, we showed that skin DCN and bone DCN (chondroitin sulfate-rich proteoglycan) were quantitatively ... Skin decorin (DCN) is an antiadhesive dermatan sulfate-rich proteoglycan that interacts with thrombospondin-1 (TSP) and ... In addition, heparan sulfate drastically inhibited [125I]DCN binding to solid-phase adsorbed TSP (80% inhibition), suggesting ...
... to the core tetrasaccharide linker and to elongating chondroitin sulfate chains in proteoglycans. Knockout of the orthologous ... chondroitin sulfate N-acetylgalactosaminyltransferase 1. Description. From NCBI Gene: This gene encodes an enzyme that ...
Proteochondroitin Sulfates. Chondroitin Sulfate Proteoglycans. D12 - Amino Acids, Peptides, and Proteins. Amyloid beta-Protein ... Proteochondroitin Sulfates. Chondroitin Sulfate Proteoglycans. Thiopronine. Tiopronin. D20 - Complex Mixtures. Nectar. Plant ...
  • As chemically specialized forms of the extracellular matrix in the central nervous system, polyanionic perineuronal nets (PNs) contain diverse constituents, including chondroitin sulfate proteoglycans (CSPGs), hyaluronic acid, and tenascins. (nih.gov)
  • They are divided in four groups: hyaluronic acid, keratan sulfate, chondroitin/dermatan sulfate, andheparan sulfate. (premiumbeautynews.com)
  • Chondroitinase ABC or chondroitinase AC treatment of the CSPG digested the chondroitin sulfate glycosaminoglycan, yielding a core protein that migrated with an apparent molecular weight of 38,000. (silverchair.com)
  • Each Aggrecan molecule contains approximately 100 and 30 keratan sulfate and glycosaminoglycan (GAG) sidechains, respectively. (rndsystems.com)
  • Glucosamine promotes the synthesis of the glycosaminoglycan chondroitin sulfate. (drvitaminsolutions.com)
  • Skin decorin (DCN) is an antiadhesive dermatan sulfate-rich proteoglycan that interacts with thrombospondin-1 (TSP) and inhibits fibroblast adhesion to TSP [Winnemoller et al. (embl.de)
  • Iduronate sulfatase deficiency leads to the subsequent GAG accumulation of heparan sulfate and chondroitin sulfate B (dermatan sulfate) in the body. (medscape.com)
  • Other than water, the mesoglea is composed of several substances including fibrous proteins like collagen and heparan sulphate proteoglycans. (pearltrees.com)
  • Binding is mediated by VAR2CSA, a parasite antigen coded by the var gene, which interacts with chondroitin sulfate A (CSA). (cdc.gov)
  • From NCBI Gene: This gene encodes an enzyme that transfers N-acetylglucosamine (GalNAc) to the core tetrasaccharide linker and to elongating chondroitin sulfate chains in proteoglycans. (nih.gov)
  • Pure Encapsulations Glucosamine and Chondroitin with MSM offers highly purified constituents for healthy cartilage formation and joint movement ease. (drvitaminsolutions.com)
  • Ph.D. dissertation title: "Inhibition of regeneration in the injured, adult spinal cord: potential role of chondroitin sulfate proteoglycans, specifically aggrecan. (assumption.edu)
  • Intact aggrecan and chondroitin-sulfate depleted aggrecan inhibit axon growth in the adult rat spinal cord. (assumption.edu)
  • Proteoglycan synthesis decreases, which decreases the osmotic swelling and the traffic of oxygen and nutrients to the disk. (medscape.com)
  • Aggrecan belongs to the chondroitin sulfate (CS) proteoglycan family, which also includes Versican, Brevican, and Neurocan. (rndsystems.com)
  • Adaptation of sensory neurons to hyalectin and decorin proteoglycans. (assumption.edu)
  • Versican is a type of protein known as a proteoglycan, which means it has several sugar molecules attached to it. (medlineplus.gov)
  • Versican: a versatile extracellular matrix proteoglycan in cell biology. (medlineplus.gov)
  • The murine Ia-associated chondroitin sulfate proteoglycan (CSPG) was studied both biochemically and immunochemically to determine the nature of its core protein. (silverchair.com)
  • Biochemically, aging increases the ratio of keratin sulfate to chondroitin sulfate, and it also changes the proportion of chondroitin-4-sulfate to chondroitin-6-sulfate, with a parallel decrease in water content. (medscape.com)
  • 2] Aging and degeneration have in common decreased water and proteoglycan content in the disks, combined with increased collagen. (medscape.com)
  • Chondroitin Sulfate reduces inflammation and assists the Glucosamine in protecting against future cartilage degeneration. (healthynewage.com)
  • It combines most popular anti-inflammatory agents such as Glucosamine, Chondroitin, MSM, vitamin, mineral and some Chinese herbal medicine, such as Corydalis Yanhusuo, to help control the joints inflammation, repair the cartilage, and relieve the pain. (merryclinic.com)
  • Glucosamine 1000 mg and Chondroitin Sulfate 134 mg are substances found naturally in the body. (merryclinic.com)
  • Various studies have indicated the combination of glucosamine, chondroitin, and MSM in Pure Encapsulations Glucosamine with MSM provides the needed nutrients for optimal cartilage composition, connective tissue strength, and joint mobility & function. (drvitaminsolutions.com)
  • Sulfur-containing methylsulfonylmethane (MSM) is included in this glucosamine and chondroitin combination to provide an enhanced spectrum of nutrients for optimal cartilage matrix composition, connective tissue strength, and joint comfort. (drvitaminsolutions.com)
  • Several studies indicate that the combination of glucosamine HCl and chondroitin sulfate has positive effects on joint mobility and comfort. (drvitaminsolutions.com)
  • Chondroitin sulfate is responsible for building the ground substance of cartilage, molecules known as proteoglycans. (drvitaminsolutions.com)
  • 58) Low proteoglycan (CS/GAG) concentrations in all the discs of a spine precede disc degeneration. (coxtechnic.com)
  • In 1976, the enzyme deficiency in Morquio syndrome type IVA (galactosamine-6-sulfatase deficiency [ie, N -acetyl-galactosamine-6-sulfate sulfatase deficiency]) was identified. (medscape.com)
  • Chondroitin sulfate and disc herniation and degeneration is a large topic to study. (coxtechnic.com)
  • An important role of sulfur from MSM is to enhance the structure and integrity of proteoglycans. (drvitaminsolutions.com)
  • Glycosaminoglycans (GAGs) are oligosaccharide components of proteoglycans (macromolecules that provide structural integrity and function to connective tissues). (medscape.com)
  • Invariant chain is the core protein of the Ia-associated chondroitin sulfate proteoglycan. (silverchair.com)
  • Chondroitin Sulfate is part of a large protein molecule (proteoglycan) that gives cartilage elasticity. (merryclinic.com)
  • It stimulates the production of glycosaminoglycans and proteoglycans, two essential building blocks of cartilage. (healthynewage.com)
  • The diversity of proteoglycans and their high interaction with growth factors and their receptors provides structural basis for a multitude of biological functions. (premiumbeautynews.com)
  • In particular, chondroitin sulfate proteoglycans (CSPGs) have been found to be involved in almost every aspect of this well-orchestrated yet delicate process. (nih.gov)
  • In the adult mammalian CNS, chondroitin sulfate proteoglycans (CSPGs) and myelin-associated inhibitors (MAIs) stabilize neuronal structure and restrict compensatory sprouting following injury. (nih.gov)
  • Chondroitin sulfate proteoglycans (CSPGs) act as potent inhibitors of axonal growth and neuroplasticity after spinal cord injury (SCI). (bvsalud.org)
  • The barrier to their regrowth is largely due to chemicals called chondroitin sulphate proteoglycans (CSPGs). (nih.gov)
  • however, proteins called chondroitin sulfate proteoglycans (CSPGs) that appear at sites of injury prevent these cells from re-growing and reconnecting their axons to appropriate targets. (nih.gov)
  • Axon regrowth after spinal cord injury (SCI) is inhibited by several types of inhibitory extracellular molecules in the central nervous system (CNS), including chondroitin sulfate proteoglycans (CSPGs), which also are components of perineuronal nets (PNNs). (nsf.gov)
  • Versican: a versatile extracellular matrix proteoglycan in cell biology. (medlineplus.gov)
  • Proteoglycans are found throughout the human body, forming the intricate extracellular matrix. (nih.gov)
  • The scar is comprised of astrocytes which increase their expression of extracellular matrix molecules, especially chondroitin sulfate proteoglycans. (nih.gov)
  • Hyaluronic acid (HA) and proteoglycans (such as dermatan sulphate (DS) and chondroitin sulphate (CS)) are the main components of the extracellular matrix of the skin, along with collagen and elastin. (mdpi.com)
  • Cells comprising human tissues are embedded in, and supported by, extracellular matrices composed of collagens, proteoglycans, and associated proteins. (nih.gov)
  • GAGs are carbohydrate polymers and are usually attached to extracellular matix proteins to form proteoglycans (hyaluronic acid is a notable exception, see below). (wikidoc.org)
  • Described below are the different types of proteoglycan found within the extracellular matrix. (wikidoc.org)
  • It occurs as a proteoglycan (PG) in which two or three HS chains are attached in close proximity to cell suface or extracellular matrix proteins. (wikidoc.org)
  • In the extracellular matrix, especially basement membranes , the multi-domain proteins perlecan , agrin and collagen XVIII are the main proteins to which heparan sulfate is attached. (wikidoc.org)
  • Chondroitin sulfate proteoglycans are the foremost component of the extracellular matrix in the central nervous system . (satterwhitechiropractic.com)
  • 6. Surfen-mediated blockade of extratumoral chondroitin sulfate glycosaminoglycans inhibits glioblastoma invasion. (nih.gov)
  • Both chondroitin sulfate and heparan sulfate interact with two families of receptors: the LAR family, which includes Receptor Protein Tyrosine Phosphatase RPTP) σ RPTP-δ and the Leukocyte Common Antigen Receptor (LAR), and two members of the Nogo Receptor familiy, NgR1 and NgR3. (nih.gov)
  • Heparan sulfate (HS) is a linear polysaccharide found in all animal tissues. (wikidoc.org)
  • But curiously, PTPσ also binds to heparin sulfate proteoglycans (HSPGs), molecules that promote axonal growth. (nih.gov)
  • CSPG4 represents an integral membrane chondroitin sulfate proteoglycan expressed by human malignant melanoma cells. (nih.gov)
  • Chondroitin sulfate shows benefits in treating central nervous system diseases such as multiple sclerosis . (satterwhitechiropractic.com)
  • Glucosamine is an essential building block for the formation of glycosaminoglycans GAGs and proteoglycans, the main components of cartilage tissue. (vitaminlife.com)
  • There are several reports showing that taking chondroitin with glucosamine increases the effects of warfarin. (nih.gov)
  • Taking chondroitin sulfate together with glucosamine hydrochloride might reduce blood levels of glucosamine. (nih.gov)
  • It's also not clear if this interaction occurs with other forms of glucosamine, such as glucosamine sulfate. (nih.gov)
  • Used with glucosamine, chondroitin sulfate alleviates pain and inflammation from osteoarthritis and reportedly has a beneficial effect on degenerated joints. (nih.gov)
  • Thus dietary supplements containing glucosamine and chondroitin sulfate have a potential market of tens of millions of Americans who suffer from osteoarthritis, athletes and dancers who may have joint overuse, and aging baby boomers interested in maintaining their joints. (nih.gov)
  • Glucosamine and chondroitin provide structural building blocks for macromolecules, such as proteoglycans, which support healthy joint cartilage. (acuatlanta.net)
  • SynovX™ Recovery features methylsulfonylmethane (MSM) blended with naturally occurring, clinically researched glucosamine sulfate and chondroitin sulfate. (myvillagegreen.com)
  • NOW Extra Strength Glucosamine & Chondroitin combines two well-known joint support ingredients in their sulfate forms. (vitaminlife.com)
  • Glucosamine, an amino sugar naturally present in the body, is a form of glucosamine sulfate. (thesupplementswiki.com)
  • Chondroitin and glucosamine are often combined to make glucosamine a powerful component for joint problems because of its anti-inflammatory properties. (thesupplementswiki.com)
  • Chondroitin sulfate and glucosamine sulfate are particularly important nutrients to the disc. (satterwhitechiropractic.com)
  • Chondroitin sulfate proteoglycans inhibit regeneration, neuroprotection, and plasticity following spinal cord injury. (cam.ac.uk)
  • 3. Chondroitin sulfate proteoglycans potently inhibit invasion and serve as a central organizer of the brain tumor microenvironment. (nih.gov)
  • An injectable solution containing chondroitin sulfate and sodium hyaluronate is approved by the FDA to protect the eye during cataract surgery. (nih.gov)
  • The sodium salt of chondroitin sulfate, which is the commercially available form, has a different Chemical Abstracts Services number [CAS No. 9082-07-9]. (nih.gov)
  • We have establihed that all of these interactions depend upon sulfation: HS and highly sulfated CS bind with high affinity to all five of these receptors. (nih.gov)
  • Current research is directed at understanding the structural features of these receptors that mediate their interactions with proteoglycan GAG chains. (nih.gov)
  • 4. Perturbing chondroitin sulfate proteoglycan signaling through LAR and PTPσ receptors promotes a beneficial inflammatory response following spinal cord injury. (nih.gov)
  • Chondroitin sulfate is a chemical found in human and animal cartilage. (nih.gov)
  • Chondroitin sulfate is one of the building blocks of cartilage. (nih.gov)
  • Salmon skin, a rich source of collagen, contains cartilage proteoglycan, which modulates healthy inflammatory response function in joints responding to exercise-related stress, thus promoting comfort. (acuatlanta.net)
  • Proteoglycans contribute to structural resilience by trapping water in the cartilage matrix. (acuatlanta.net)
  • Chondroitin sulfates contribute to the tensile strength of cartilage, tendons , ligaments and walls of the aorta . (wikidoc.org)
  • Patients with conditions like osteoarthritis - a result of wear and tear on cartilage and joints which many of us Oxford back pain sufferers experience as we age - may benefit from chondroitin sulfate. (satterwhitechiropractic.com)
  • Hyaluronan and chondroitin sulfate proteoglycans in the supramolecular organization of the mammalian vitreous body. (medlineplus.gov)
  • It consists of an extended protein core to which many chondroitin sulfate and keratan sulfate (linear sulfated polysaccharide) chains are attached. (nih.gov)
  • Oral consumption of chondroitin, sulfate has a positive impact on the osteoarthritic joints. (thesupplementswiki.com)
  • Sequestration of infected erythrocytes in the placenta is mediated by VAR2CSA, the P. falciparum erythrocyte membrane protein 1 variant that binds to chondroitin sulfate A (CSA) on the syncytiotrophoblast ( 11 , 12 ). (cdc.gov)
  • Technical Products and Impurities: Chondroitin sulfate [CAS No. 9007-28-7] is a mixture of derivatives of chondroitin which have a sulfate moiety esterified to the galactosamine moiety of chondroitin. (nih.gov)
  • Some of the GlcA residues are epimerized to IdoA, while either of the two sugars in a disaccharide pair can be sulfate on any of several positions. (nih.gov)
  • Chondroitin sulfate is possibly safe when used together with other ingredients in an eye drop. (nih.gov)
  • Chondroitin sulfate proteoglycans prevent immune cell phenotypic conversion and inflammation resolution via TLR4 in rodent models of spinal cord injury. (bvsalud.org)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rat Chondroitin Sulfate Proteoglycan 5 (CSPG5) in Tissue homogenates, cell lysates and other biological fluids. (clinical-trial-logistics.com)
  • 5. Chondroitin Sulfate Proteoglycans Negatively Modulate Spinal Cord Neural Precursor Cells by Signaling Through LAR and RPTPσ and Modulation of the Rho/ROCK Pathway. (nih.gov)
  • 14. Chondroitin sulfate content and decorin expression in glioblastoma are associated with proliferative activity of glioma cells and disease prognosis. (nih.gov)
  • Description: A sandwich ELISA kit for detection of Chondroitin Sulfate Proteoglycan 5 from Rat in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (clinical-trial-logistics.com)
  • Keratan sulfates have a variable sulfate content and unlike many other GAGs, does not contain uronic acid . (wikidoc.org)
  • Aggrecan is a bottlebrush shaped high molecular weight proteoglycan. (nih.gov)
  • Oxford chiropractic patients can feel this care on each visit…and hear the latest information like the following about chondroitin sulfate and its benefit for your matrices! (satterwhitechiropractic.com)
  • It is covalently attached to the core protein to form a proteoglycan. (labex-gral.fr)
  • Chondroitin sulfate is brought to the attention of the Chemical Selection Working Group because it is widely used in dietary supplement that would be consumed over a period of many years to maximize potential beneficial effects. (nih.gov)
  • We have identified diifferences in the interaction of the LAR family members with proteoglycans which may explain their differential actions on neurons. (nih.gov)
  • Chondroitin sulfate is used for osteoarthritis and cataracts. (nih.gov)
  • Taking chondroitin sulfate by mouth seems to provide some relief from osteoarthritis pain and improve function. (nih.gov)
  • Research has shown that chondroitin sulfate reduces arthritic pain, improves joint function and reduces joint swelling and stiffness. (satterwhitechiropractic.com)
  • However, until more is known, do not take chondroitin sulfate if you have prostate cancer or are at high risk for developing it (you have a brother or father with prostate cancer). (nih.gov)
  • Virtually no information on the potential toxicity of chondroitin sulfate was found in the available literature. (nih.gov)
  • Description: A competitive ELISA for quantitative measurement of Canine Chondroitin Sulfate Proteoglycan 5 (CSPG5) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (clinical-trial-logistics.com)
  • This effect has not been shown with chondroitin sulfate supplements. (nih.gov)
  • Early research suggests that chondroitin might cause the spread or recurrence of prostate cancer. (nih.gov)