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At least half of all eukaryotic proteins have sugars attached, so that glycosylation the enzymic attachment of sugars is the most frequent posttranslational modification of proteins. Many proteins also undergo reversible glycosylation with a single sugar N -acetylglucosamine bound to a serine or threonine residue that is also a site for reversible phosphorylation.
This is an important mechanism of metabolic regulation. Nonenzymic attachment of sugars to proteins can also occur, and is referred to as glycation. This process can have serious pathological consequences eg, in poorly controlled diabetes mellitus. Glycoproteins are one class of glycoconjugate or complex carbohydrate —equivalent terms that are used to denote molecules containing one or more carbohydrate chains covalently linked to protein to form glycoproteins or proteoglycans or lipid to form glycolipids.
Proteoglycans are discussed in Chapter 50 and glycolipids in Chapter Almost all the human plasma proteins , with the notable exception of albumin, are glycoproteins. Many proteins of cellular membranes see Chapter 40 contain substantial amounts of carbohydrate, and many membrane proteins are anchored to the lipid bilayer by a glycan chain. A number of the blood group substances are glycoproteins, whereas others are glycosphingolipids. Many peptide hormones are glycoproteins.
A major problem in cancer is metastasis see Chapter 56 and evidence is accumulating that alterations in the structures of glycoproteins and other glycoconjugates on the surface of cancer cells are important in metastasis.
Glycoproteins occur in most organisms, from bacteria to human beings. Many viruses also contain glycoproteins, some of which play key roles in viral attachment to host cells eg, HIV-1 and influenza A virus.
The glycan structures of glycoproteins change in response to signals involved in cell differentiation, normal physiology, and neoplastic transformation. This is the result of different expression patterns of glycosyltransferases under different conditions.
In the body, some glycoproteins act as markers and thus allow given cells to be identified based on these specific molecules. Some of the best examples of glycoprotein markers are Glycophorins A and B. Generally, these are classified as sialoglycoprotein which means that the glycoprotein also consists of sialic acid. Found in the membrane of human erythrocytes, the molecule is used for MN blood grouping.
While glycoproteins can help protect the epithelial tissue, especially in the mucosa, it has been shown to contribute to cellular invasion in some cases. Here, the molecule e. HMW1 adhesin in Haemophilus influenzae promotes attachment of the pathogen to the host cell thus promoting invasion. In some cases, pathogens have been shown to glycosylate proteins of the host in order to invade the cells of the host. In this case, glycosylation of the host proteins allows the pathogen to attach to the cell and consequently invade the cell.
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It consists of a variety of cells capable of producing different hormones. Hydrogen-oxidizing Bacteria are species that can use gaseous hydrogen as the electron donor to oxidize hydrogen. The material on this page is not medical advice and is not to be used for diagnosis or treatment.
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The MicroscopeMaster website is for educational purposes only. Amazon and the Amazon logo are trademarks of Amazon. My Website. Home What's New Here! Of Interest New Book! What are Glycoproteins? Importance Where are they found? Structure of an N-linked glycoprotein.
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