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Glycoproteins are proteins which contain oligosaccharide (sugar) chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation. Secreted extracellular proteins are often glycosylated.
In proteins that have segments extending extracellularly, the extracellular segments are also often glycosylated. Glycoproteins are also often important integral membrane proteins, where they play a role in cell–cell interactions. It is important to distinguish endoplasmic reticulum-based glycosylation of the secretory system from reversible cytosolic-nuclear glycosylation. Glycoproteins of the cytosol and nucleus can be modified through the reversible addition of a single GlcNAc residue that is considered reciprocal to phosphorylation and the functions of these are likely to be an additional regulatory mechanism that controls phosphorylation-based signalling.[2] In contrast, classical secretory glycosylation can be structurally essential. For example, inhibition of asparagine-linked, i.e. N-linked, glycosylation can prevent proper glycoprotein folding and full inhibition can be toxic to an individual cell. In contrast, perturbation of glycan processing (enzymatic removal/addition of carbohydrate residues to the glycan), which occurs in both the endoplasmic reticulum and Golgi apparatus, is dispensable for isolated cells (as evidenced by survival with glycosides inhibitors) but can lead to human disease (congenital disorders of glycosylation) and can be lethal in animal models. It is therefore likely that the fine processing of glycans is important for endogenous functionality, such as cell trafficking, but that this is likely to have been secondary to its role in host-pathogen interactions. A famous example of this latter effect is the ABO blood group system.
Though there are different types of glycoproteins, the most common are N-linked and O-linked glycoproteins.[3] These two types of glycoproteins are distinguished by structural differences that give them their names. Glycoproteins vary greatly in composition, making many different compounds such as antibodies or hormones.[4] Due to the wide array of functions within the body, interest in glycoprotein synthesis for medical use has increased.[5] There are now several methods to synthesize glycoproteins, including recombination and glycosylation of proteins.[5]
Glycosylation is also known to occur on nucleocytoplasmic proteins in the form of O-GlcNAc.[6]
- ^ Ruddock LW, Molinari M (November 2006). "N-glycan processing in ER quality control". Journal of Cell Science. 119 (Pt 21): 4373–4380. doi:10.1242/jcs.03225. PMID 17074831.
- ^ Funakoshi Y, Suzuki T (February 2009). "Glycobiology in the cytosol: the bitter side of a sweet world". Biochimica et Biophysica Acta (BBA) - General Subjects. 1790 (2): 81–94. doi:10.1016/j.bbagen.2008.09.009. PMID 18952151.
- ^ Picanco e Castro V, Swiech SH (2018). Recombinant Glycoprotein Production Methods and Protocols. Springer. ISBN 978-1-4939-7312-5. OCLC 1005519572.
- ^ Nelson DL, Cox MM, Hoskins AA, Lehninger AL (2013). Lehninger Principles of Biochemistry (Sixth ed.). Macmillan Learning. ISBN 978-1-319-38149-3. OCLC 1249676451.
- ^ a b Gamblin DP, Scanlan EM, Davis BG (January 2009). "Glycoprotein synthesis: an update". Chemical Reviews. 109 (1): 131–163. doi:10.1021/cr078291i. PMID 19093879.
- ^ Hart GW (27 October 2014). "Three Decades of Research on O-GlcNAcylation - A Major Nutrient Sensor That Regulates Signaling, Transcription and Cellular Metabolism". Frontiers in Endocrinology. 5: 183. doi:10.3389/fendo.2014.00183. PMC 4209869. PMID 25386167.