Glycosaminoglycans
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Glycosaminoglycans
Glycosaminoglycans (GAGs) or mucopolysaccharides are long, linear polysaccharides consisting of repeating disaccharide units (i.e. two-sugar units). The repeating two-sugar unit consists of a uronic acid, uronic sugar and an amino sugar, except in the case of the sulfated glycosaminoglycan keratan sulfate, keratan, where, in place of the uronic sugar there is a galactose unit. GAGs are found in vertebrates, invertebrates and bacteria. Because GAGs are highly polar molecules and attract water; the body uses them as lubricants or shock absorbers. Mucopolysaccharidosis, Mucopolysaccharidoses are a group of metabolic disorders in which abnormal accumulations of glycosaminoglycans occur due to enzyme deficiencies. Production Glycosaminoglycans vary greatly in molecular mass, disaccharide structure, and sulfation. This is because GAG synthesis is not template driven, as are proteins or nucleic acids, but constantly altered by processing enzymes. GAGs are classified into four groups, b ...
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Chondroitin Sulfate
Chondroitin sulfate is a sulfated glycosaminoglycan (GAG) composed of a chain of alternating sugars (N-Acetylgalactosamine, N-acetylgalactosamine and glucuronic acid). It is usually found attached to proteins as part of a proteoglycan. A chondroitin chain can have over 100 individual sugars, each of which can be sulfated in variable positions and quantities. Chondroitin sulfate is an important structural component of cartilage, and provides much of its resistance to compressive stress, compression. Along with glucosamine, chondroitin sulfate has become a widely used dietary supplement for treatment of osteoarthritis, although large clinical trials failed to demonstrate any symptomatic benefit of chondroitin. Fragments of chondroitin chains suspended in water elicit a fear response in many fishes, similar to schreckstoff, hypoxanthine-3N-oxide. Medical use Chondroitin is used in dietary supplements as an alternative medicine to treat osteoarthritis. It is also approved and regula ...
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Heparin
Heparin, also known as unfractionated heparin (UFH), is a medication and naturally occurring glycosaminoglycan. Heparin is a blood anticoagulant that increases the activity of antithrombin. It is used in the treatment of myocardial infarction, heart attacks and unstable angina. It can be given intravenously or by subcutaneous injection, injection under the skin. Its anticoagulant properties make it useful to prevent blood clotting in blood specimen test tubes and kidney dialysis machines. Common side effects include bleeding, pain at the injection site, and thrombocytopenia, low blood platelets. Serious side effects include heparin-induced thrombocytopenia. Greater care is needed in those with poor kidney function. Heparin is contraindicated for suspected cases of Post-vaccination embolic and thrombotic events, vaccine-induced pro-thrombotic immune thrombocytopenia (VIPIT) secondary to SARS-CoV-2 vaccination, as heparin may further increase the risk of bleeding in an anti-PF4 ...
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Chondroitin Sulfate Structure NTP
A chondroitin is a chondrin derivative. Types include: * Chondroitin sulfate * Dermatan sulfate Chondroitin as a supplement is now commonly used (often in combination with glucosamine) in treating the joint disease of osteoarthritis. In contrast to the symptomatic treatments, chondroitin can modify the progression of a disease process in the patient which it can be used as an alternative medicine. Chondroitin's effect toward the articular cartilage integrity as it is part of the proteoglycan Proteoglycans are proteins that are heavily glycosylated. The basic proteoglycan unit consists of a "core protein" with one or more covalently attached glycosaminoglycan (GAG) chain(s). The point of attachment is a serine (Ser) residue to w ... molecules. The cartilage proteoglycan synthesis can speed up as chondroitin is going through the pathway of the alimentary canal. Research has been conducted to show the effectiveness of chondroitin and results indicate that it helps to manage ...
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Hyaluronic Acid
Hyaluronic acid (; abbreviated HA; conjugate base hyaluronate), also called hyaluronan, is an anionic, nonsulfated glycosaminoglycan distributed widely throughout connective, epithelial, and neural tissues. It is unique among glycosaminoglycans as it is non-sulfated, forms in the plasma membrane instead of the Golgi apparatus, and can be very large: human synovial HA averages about per molecule, or about 20,000 disaccharide monomers, while other sources mention . Medically, hyaluronic acid is used to treat osteoarthritis of the knee and dry eye, for wound repair, and as a cosmetic filler. The average 70 kg (150 lb) person has roughly 15 grams of hyaluronan in the body, one third of which is turned over (i.e., degraded and synthesized) per day. As one of the chief components of the extracellular matrix, it contributes significantly to cell proliferation and migration, and is involved in the progression of many malignant tumors. Hyaluronic acid is also a ...
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Keratan Sulfate
Keratan sulfate (KS), also called keratosulfate, is any of several sulfated glycosaminoglycans (structural carbohydrates) that have been found especially in the cornea, cartilage, and bone. It is also synthesized in the central nervous system where it participates both in development and in the glial scar formation following an injury. Keratan sulfates are large, highly hydrated molecules which in joints can act as a cushion to absorb mechanical shock. Structure Like other glycosaminoglycans keratan sulfate is a linear polymer that consists of a repeating disaccharide unit. Keratan sulfate occurs as a proteoglycan (PG) in which KS chains are attached to cell-surface or extracellular matrix proteins, termed core proteins. KS core proteins include lumican, keratocan, mimecan, fibromodulin, PRELP, osteoadherin, and aggrecan. The basic repeating disaccharide unit within keratan sulfate is -3 Galβ1-4 GlcNAc6Sβ1-. This can be sulfated at carbon position 6 (C6) of either or bot ...
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Dermatan Sulfate
Dermatan sulfate is a glycosaminoglycan (formerly called a mucopolysaccharide) found mostly in skin, but also in blood vessels, heart valves, tendons, and lungs. It is also referred to as chondroitin sulfate B, although it is no longer classified as a form of chondroitin sulfate by most sources. The formula is C14H21NO15S. This carbohydrate is composed of linear polymers of disaccharide units that contain, N-acetyl galactosamine (GalNAc) and iduronic acid (IdoA). These repeating units are sulfated at a variety of positions. Dermatan sulfate is a component of the compound sulodexide. Function Dermatan sulfate may have roles in coagulation, cardiovascular disease, carcinogenesis, infection, wound repair, maintaining the shape of galactosamine 4-sulfate, skin, and fibrosis. Pathology Dermatan sulfate accumulates abnormally in several of the mucopolysaccharidosis disorders. An excess of dermatan sulfate in the mitral valve is characteristic of myxomatous degeneration of the ...
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Keratan Sulfate
Keratan sulfate (KS), also called keratosulfate, is any of several sulfated glycosaminoglycans (structural carbohydrates) that have been found especially in the cornea, cartilage, and bone. It is also synthesized in the central nervous system where it participates both in development and in the glial scar formation following an injury. Keratan sulfates are large, highly hydrated molecules which in joints can act as a cushion to absorb mechanical shock. Structure Like other glycosaminoglycans keratan sulfate is a linear polymer that consists of a repeating disaccharide unit. Keratan sulfate occurs as a proteoglycan (PG) in which KS chains are attached to cell-surface or extracellular matrix proteins, termed core proteins. KS core proteins include lumican, keratocan, mimecan, fibromodulin, PRELP, osteoadherin, and aggrecan. The basic repeating disaccharide unit within keratan sulfate is -3 Galβ1-4 GlcNAc6Sβ1-. This can be sulfated at carbon position 6 (C6) of either or bot ...
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Golgi Apparatus
The Golgi apparatus (), also known as the Golgi complex, Golgi body, or simply the Golgi, is an organelle found in most eukaryotic Cell (biology), cells. Part of the endomembrane system in the cytoplasm, it protein targeting, packages proteins into membrane-bound Vesicle (biology and chemistry), vesicles inside the cell before the vesicles are sent to their destination. It resides at the intersection of the secretory, lysosomal, and Endocytosis, endocytic pathways. It is of particular importance in processing proteins for secretion, containing a set of glycosylation enzymes that attach various sugar monomers to proteins as the proteins move through the apparatus. The Golgi apparatus was identified in 1898 by the Italian biologist and pathologist Camillo Golgi. The organelle was later named after him in the 1910s. Discovery Because of its large size and distinctive structure, the Golgi apparatus was one of the first organelles to be discovered and observed in detail. It was d ...
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Proteoglycan
Proteoglycans are proteins that are heavily glycosylated. The basic proteoglycan unit consists of a "core protein" with one or more covalently attached glycosaminoglycan (GAG) chain(s). The point of attachment is a serine (Ser) residue to which the glycosaminoglycan is joined through a tetrasaccharide bridge (e.g. chondroitin sulfate- GlcA- Gal-Gal- Xyl-PROTEIN). The Ser residue is generally in the sequence -Ser- Gly-X-Gly- (where X can be any amino acid residue but proline), although not every protein with this sequence has an attached glycosaminoglycan. The chains are long, linear carbohydrate polymers that are negatively charged under physiological conditions due to the occurrence of sulfate and uronic acid groups. Proteoglycans occur in connective tissue. Types Proteoglycans are categorized by their relative size (large and small) and the nature of their glycosaminoglycan chains. Types include: Certain members are considered members of the "small leucine-rich pr ...
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O-linked Glycosylation
''O''-linked glycosylation is the attachment of a sugar molecule to the oxygen atom of serine (Ser) or threonine (Thr) residues in a protein. ''O''-glycosylation is a post-translational modification that occurs after the protein has been synthesised. In eukaryotes, it occurs in the endoplasmic reticulum, Golgi apparatus and occasionally in the cytoplasm; in prokaryotes, it occurs in the cytoplasm. Several different sugars can be added to the serine or threonine, and they affect the protein in different ways by changing protein stability and regulating protein activity. O-glycans, which are the sugars added to the serine or threonine, have numerous functions throughout the body, including trafficking of cells in the immune system, allowing recognition of foreign material, controlling cell metabolism and providing cartilage and tendon flexibility. Because of the many functions they have, changes in O-glycosylation are important in many diseases including cancer, diabetes and Alzheime ...
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NDST1
Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1 is an enzyme. In humans, it is encoded by the ''NDST1'' gene In biology, the word gene has two meanings. The Mendelian gene is a basic unit of heredity. The molecular gene is a sequence of nucleotides in DNA that is transcribed to produce a functional RNA. There are two types of molecular genes: protei .... References Further reading * * * * * * * * * * Human proteins {{gene-5-stub ...
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N-linked Glycosylation
''N''-linked glycosylation is the attachment of an oligosaccharide, a carbohydrate consisting of several sugar molecules, sometimes also referred to as glycan, to a nitrogen atom (the amide nitrogen of an asparagine (Asn) residue of a protein), in a process called ''N''-glycosylation, studied in biochemistry. The resulting protein is called an N-linked glycan, or simply an N-glycan. This type of linkage is important for both the structure and function of many eukaryotic proteins. The ''N''-linked glycosylation process occurs in eukaryotes and widely in archaea, but very rarely in bacteria. The nature of ''N''-linked glycans attached to a glycoprotein is determined by the protein and the cell in which it is expressed. It also varies across species. Different species synthesize different types of ''N''-linked glycans. Energetics of bond formation There are two types of bonds involved in a glycoprotein: bonds between the saccharides residues in the glycan and the linkage between ...
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