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Glycosylation

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AGEs are responsible for many things. These molecules play an important role especially in nutrition, they are responsible for the brownish color and the aromas and flavors of some foods. It is demonstrated that cooking at high temperature results in various food products having high levels of AGEs.
971:, the body of the patient produces antibodies against the enzyme lymphocytes galactosyltransferase which inhibits the glycosylation of IgG. Therefore, the changes in the N-glycosylation produce the immunodeficiency involved in this illness. In this second group we can also find disorders caused by 553:
and Thr) in order for mannosylation to occur. Recently there has been a breakthrough in the technique of predicting whether or not the sequence will have a mannosylation site that provides an accuracy of 93% opposed to the 67% accuracy if we just consider the WXXW motif.
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All these diseases are difficult to diagnose because they do not only affect one organ, they affect many of them and in different ways. As a consequence, they are also hard to treat. However, thanks to the many advances that have been made in
953:-glycosylation, disorders of lipid glycosylation and disorders of other glycosylation pathways and of multiple glycosylation pathways. No effective treatment is known for any of these disorders. 80% of these affect the nervous system. 922:. One of the modulators that intervene in this process is the Fringe, a glycosyltransferase that modifies the O-fucose to activate or deactivate parts of the signalling, acting as a positive or negative regulator, respectively. 540:
and the second carbon of the tryptophan. However, not all the sequences that have this pattern are mannosylated. It has been established that, in fact, only two thirds are and that there is a clear preference for the second
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transmission of viruses. In addition, glycosylation is often used by viruses to shield the underlying viral protein from immune recognition. A significant example is the dense glycan shield of the envelope spike of the
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Overall, glycosylation needs to be understood by the likely evolutionary selection pressures that have shaped it. In one model, diversification can be considered purely as a result of endogenous functionality (such as
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There are three types of glycosylation disorders sorted by the type of alterations that are made to the glycosylation process: congenital alterations, acquired alterations and non-enzymatic acquired alterations.
232:-linked glycans mediate a critical quality control check point in glycoprotein folding in the endoplasmic reticulum. Glycosylation also plays a role in cell-to-cell adhesion (a mechanism employed by cells of the 505:, on the cell-surface laminin receptor alpha dystroglycan. It has been suggested this rare finding may be linked to the fact that alpha dystroglycan is highly conserved from lower vertebrates to mammals. 2393:
Razaghi A, Villacrés C, Jung V, Mashkour N, Butler M, Owens L, Heimann K (October 2017). "Improved therapeutic efficacy of mammalian expressed-recombinant interferon gamma against ovarian cancer cells".
647:-benzylidene) in order to achieve desired regioselectivity. The other challenge of chemical glycosylation is the stereoselectivity that each glycosidic linkage has two stereo-outcomes, α/β or 584:. In 2011, the first crystal structure of a protein containing this type of glycosylation was determined—that of human complement component 8. Currently it is established that 18% of human 209:. This modification serves various functions. For instance, some proteins do not fold correctly unless they are glycosylated. In other cases, proteins are not stable unless they contain 260:
are presented and hence what antibody specificities are exhibited. This immunological role may well have driven the diversification of glycan heterogeneity and creates a barrier to
659:-glycoside is more challenging to synthesis. New methods have been developed based on solvent participation or the formation of bicyclic sulfonium ions as chiral-auxiliary groups. 985:
Non-enzymatic disorders, are also acquired, but they are due to the lack of enzymes that attach oligosaccharides to the protein. In this group the illnesses that stand out are
396:-linked glycosylation is a very prevalent form of glycosylation and is important for the folding of many eukaryotic glycoproteins and for cell–cell and cell– 3235: 2750: 687:
of the protein. In this process the intervention of an enzyme is not needed. It takes place across and close to the water channels and the protruding tubules.
888:. This means it is crucial in embryonic development, to the point that it has been tested on mice that the removal of glycans in Notch proteins can result in 1158:
Jung ST, Kang TH, Kelton W, Georgiou G (December 2011). "Bypassing glycosylation: engineering aglycosylated full-length IgG antibodies for human therapy".
244:, which recognize specific carbohydrate moieties. Glycosylation is an important parameter in the optimization of many glycoprotein-based drugs such as 823:(from Streptococcus pneumoniae): cleaves all non-reducing terminal β-linked N-acetylglucosamine residues from complex carbohydrates and glycoproteins. 3210: 1968:Świa̧tecka, D.; Kostyra, H.; Świa̧tecki, A. (2010). "Impact of glycated pea proteins on the activity of free‐swimming and immobilised bacteria". 1243:
Dalziel M, Crispin M, Scanlan CN, Zitzmann N, Dwek RA (January 2014). "Emerging principles for the therapeutic exploitation of glycosylation".
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Henle, Thomas; Duerasch, Anja; Weiz, Alexander; Ruck, Michael; Moeckel, Ulrike (1 November 2020). "Glycation Reactions of Casein Micelles".
1727:"Mutations in the Trp-Ser-X-Trp-Ser motif of the erythropoietin receptor abolish processing, ligand binding, and activation of the receptor" 72:. Glycans serve a variety of structural and functional roles in membrane and secreted proteins. The majority of proteins synthesized in the 2614: 939: 1458: 2535:-glycosylation sites in human proteins using artificial neural networks that examine the sequence context of Asn-Xaa-Ser/Thr sequons. 907:. The Notch proteins go through these organelles in their maturation process and can be subject to different types of glycosylation: 2512: 2289: 2187: 1100: 745:, heart damage... And, if they are present at a decreased level, skin elasticity is reduced which is an important symptom of aging. 1501:
Yoshida-Moriguchi T, Yu L, Stalnaker SH, Davis S, Kunz S, Madson M, Oldstone MB, Schachter H, Wells L, Campbell KP (January 2010).
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Having elevated levels of AGEs in the body has a direct impact on the development of many diseases. It has a direct implication in
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undergo the process of C-mannosylation. Numerous studies have shown that this process plays an important role in the secretion of
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modification. Aglycosylation is a feature of engineered antibodies to bypass glycosylation. Five classes of glycans are produced:
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attachment to terminal saccharide residues) and that diversity within the multicellular organism is then exploited endogenously.
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are one of the proteins most commonly modified in this way. However, there is another group of proteins that undergo
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which is the most glycated and structurally abundant protein, especially in humans. Also, some studies have shown
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is twofold. Firstly, the highly soluble glycans may have a direct physicochemical stabilisation effect. Secondly,
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Crispin M, Harvey DJ, Bitto D, Bonomelli C, Edgeworth M, Scrivens JH, Huiskonen JT, Bowden TA (March 2014).
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Varki A, Cummings RD, Esko JD, Freeze HH, Stanley P, Bertozzi CR, Hart GW, Etzler ME (2009). Varki A (ed.).
605: 2346:"Mitotic Intragenic Recombination:A Mechanism of Survivalfor Several Congenital Disorders of Glycosylation" 967:. In these cases, the changes in glycosylation are the cause of certain biological events. For example, in 3220: 3168: 3102: 2988: 2983: 2688: 1044: 986: 943: 912: 908: 432: 420:-linked glycans of a protein can modulate a protein's function, in some cases acting as an on/off switch. 388: 110: 65:(also 'non-enzymatic glycation' and 'non-enzymatic glycosylation') may refer to a non-enzymatic reaction. 27: 918:
All of the Notch proteins are modified by an O-fucose, because they share a common trait: O-fucosylation
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residue in the sequence W–X–X–W (W indicates tryptophan; X is any amino acid). A
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Gill, Vidhu; Kumar, Vijay; Singh, Kritanjali; Kumar, Ashok; Kim, Jong-Joo (17 December 2019).
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There are various mechanisms for glycosylation, although most share several common features:
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Covalent attachment and further modification of carbohydrate residues to a substrate molecule
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Lima, M.; Baynes, J.W. (2013). "Glycation". In Lennarz, William J.; Lane, M. Daniel (eds.).
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Ardejani, Maziar S.; Noodleman, Louis; Powers, Evan T.; Kelly, Jeffery W. (15 March 2021).
3029: 2911: 1583: 1288:"Structural plasticity of the Semliki Forest virus glycome upon interspecies transmission" 1010:
It has been reported that mammalian glycosylation can improve the therapeutic efficacy of
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At first, the reaction forms temporary molecules which later undergo different reactions (
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Glycosylation can also module the thermodynamic and kinetic stability of the proteins.
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Ihara, Yoshito. "C-Mannosylation: A Modification on Tryptophan in Cellular Proteins".
166:-linked glycans, a rare form of glycosylation where a sugar is added to a carbon on a 3204: 2665: 2314: 1272: 1193: 1019: 1002:, scientists can now understand better these disorders and have discovered new CDGs. 810: 676: 479: 233: 198: 146: 2592: 2423: 2141: 1807:-Glycosylation as the driving force of progress in synthetic carbohydrate chemistry" 2958: 2928: 2733: 2705: 2450:
platform for prediction of N-, O- and C-glycosites in eukaryotic protein sequences"
1625:"C-mannosylation supports folding and enhances stability of thrombospondin repeats" 1050: 792: 340:, is an enzymatic process. Indeed, glycosylation is thought to be the most complex 279: 225: 190: 38: 520:
The mannose molecule is attached to the C2 of the first tryptophan of the sequence
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of proteins meaning it alters their structure and biological activity. It is the
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have been reported in the literature. Fucose and GlcNAc have been found only in
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is a cell signalling pathway whose role is, among many others, to control the
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Crich D (August 2010). "Mechanism of a chemical glycosylation reaction".
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on the enzymes that control the glycosylation of Notch proteins, such as
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residues. The influence of glycosylation on the folding and stability of
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Posttranslational Modification of Proteins: Expanding Nature's Inventory
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or non-enzymatic glycation. It is a spontaneous reaction and a type of
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Varki A, Cummings R, Esko J, Freeze H, Hart G, Marth J, eds. (1999).
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L. express aglycosylated monoclonal antibody with antitumor activity"
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of a reducing sugar (mainly glucose and fructose) and the amino acid
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is a special form of glycosylation that features the formation of a
2276:. Handbook of Clinical Neurology. Vol. 113. pp. 1737–43. 600:
if they do not undergo C-mannosylation This explains why a type of
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In this second group the main disorders are infectious diseases,
501:. Mannose has recently been reported in a vertebrate, the mouse, 440:-linked glycosylation is a form of glycosylation that occurs in 2596: 160:
Phosphoglycans linked through the phosphate of a phosphoserine.
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Some of the specific modulators that control this process are
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AGEs accumulate in long-lived extracellular proteins such as
1343:. Viral pathogenesis • Preventive and therapeutic vaccines. 370:). Therefore, glycosylation is a site-specific modification. 76:
undergo glycosylation. Glycosylation is also present in the
915:(more specifically: O-linked glucose and O-linked fucose). 572:-mannosylation is unusual because the sugar is linked to a 2315:"Alteraciones de la glicosilación en enfermedades humanas" 2272:
Jaeken J (2013). "Congenital disorders of glycosylation".
2056:"НЕФЕРМЕНТАТИВНОЕ ГЛИКИРОВАНИЕ БЕЛКОВ: ОТ ДИАБЕТА ДО РАКА" 1065: – Technology enabling rapid molecule diversification 344:, because of the large number of enzymatic steps involved. 2313:
Jiménez Martínez, María del Carmen (January–March 2002).
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and regulate and modify their receptor mechanisms at the
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in the lumen of the endoplasmic reticulum and widely in
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usually refers to an enzyme-catalysed reaction, whereas
1856:"Mechanism of Glycosylation of Anomeric Sulfonium Ions" 1129:(2nd ed.). Cold Spring Harbor Laboratories Press. 1040:
Pages displaying short descriptions of redirect targets
311:—the types of sugars that are linked to a given protein 2825:(amino acid→pyruvate, acetyl CoA, or TCA intermediate) 868:-linked oligosaccharides unless α1,3-core fucosylated. 639:
Glycosylation can also be effected using the tools of
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Lovelace LL, Cooper CL, Sodetz JM, Lebioda L (2011).
1087:(Second ed.). Academic Press. pp. 405–411. 721:
may trigger spontaneous non-enzymatic glycosylation.
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Additional information on glycosylation and figures
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Supplementary Material of the Book "The Sugar Code"
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Biochemical and Biophysical Research Communications
1059: – Attachment of a sugar to a protein or lipid 1014:. For example, therapeutic efficacy of recombinant 805:): releases only β1,4-linked, nonreducing terminal 2225:"Significance of glycosylation in Notch signaling" 1047: – Reaction of a glycosyl donor and acceptor 892:or malformations of vital organs like the heart. 667:The non-enzymatic glycosylation is also known as 174:is one of the few naturally occurring substances. 116:requires participation of a special lipid called 68:Glycosylation is a form of co-translational and 317:—can be unbranched or branched chains of sugars 1854:Fang T, Gu Y, Huang W, Boons GJ (March 2016). 1219:(2nd ed.). Oxford University Press, USA. 1022:platform, was improved against drug-resistant 596:containing proteins which are retained in the 2608: 1453:. Roberts and Co. Publishers, Englewood, CO. 737:that can lead to many complications such as: 323:—can be short- or long-chain oligosaccharides 153:side-chains, or to oxygens on lipids such as 8: 57:. In biology (but not always in chemistry), 2164:"Roles of glycosylation in Notch signaling" 3090: 3007: 2900: 2893: 2805: 2781: 2672: 2615: 2601: 2593: 2162:Stanley, Pamela; Okajima, Tetsuya (2010). 2110:"Glycosylation regulates Notch signalling" 1905:Journal of Agricultural and Food Chemistry 706:...) and form permanent residues known as 536:is formed between the first carbon of the 2575: 2483: 2473: 2369: 2248: 2071: 2030: 2020: 1879: 1830: 1742: 1701: 1691: 1650: 1640: 1599: 1538: 1425: 1360: 1311: 354:The process is non-templated (unlike DNA 347:The donor molecule is often an activated 294:Glycosylation increases diversity in the 252:system. It is the presence or absence of 2054:Ansari, N.A.; Rasheed, Z. (March 2010). 1860:Journal of the American Chemical Society 404:-linked glycosylation process occurs in 189:Glycosylation is the process by which a 2550:Emanual Maverakis; et al. (2015). 2531:NetNGlyc: The NetNglyc server predicts 2507:. Cold Spring Harbor Laboratory Press. 2168:Current Topics in Developmental Biology 1118: 1116: 1114: 1112: 1075: 2444:Chauhan JS, Rao A, Raghava GP (2013). 2350:The American Journal of Human Genetics 2223:Hideyuki, Takeuchi (17 October 2014). 2114:Nature Reviews. Molecular Cell Biology 1801:Nigudkar SS, Demchenko AV (May 2015). 3236:Congenital disorders of glycosylation 2526:-glycosylation of proteins on the web 2218: 2216: 2214: 2103: 2101: 2099: 1938: 1936: 1934: 1577: 1575: 1573: 940:congenital disorders of glycosylation 748:They are also the precursors of many 616:Formation of GPI anchors (glypiation) 7: 2725:Electron acceptors other than oxygen 1945:Encyclopedia of Biological Chemistry 1238: 1236: 1085:Encyclopedia of Biological Chemistry 850:-glycosylation. This enzyme cleaves 612:if it lacked C-mannosylation sites. 576:rather than a reactive atom such as 1731:The Journal of Biological Chemistry 1335:Crispin M, Doores KJ (April 2015). 983:Non-enzymatic acquired alterations: 858:-linked unsubstituted Galβ1,3GalNAc 248:. Glycosylation also underpins the 2344:S. Kane, Megan (4 February 2016). 2282:10.1016/B978-0-444-59565-2.00044-7 1564:Glycoscience: Biology and Medicine 1480:. Nova Publishers. pp. 45ff. 1093:10.1016/B978-0-12-378630-2.00120-1 545:to be one of the polar ones (Ser, 14: 1623:Aleksandra, Shcherbakova (2019). 256:which dictates which blood group 1943:Baynes, J. W.; Lima, M. (2013). 1477:Biotechnology and Bioengineering 1160:Current Opinion in Biotechnology 126:-linked glycans attached to the 3211:Post-translational modification 2746:Substrate-level phosphorylation 2108:Haines, Nicole (October 2003). 1215:Drickamer K, Taylor ME (2006). 1006:Effects on therapeutic efficacy 809:from complex carbohydrates and 708:Advanced Glycation end-products 673:post-translational modification 342:post-translational modification 70:post-translational modification 873:Regulation of Notch signalling 94:-linked glycans attached to a 1: 3149:Reverse cholesterol transport 2180:10.1016/S0070-2153(10)92004-8 1768:Accounts of Chemical Research 1744:10.1016/S0021-9258(19)49956-0 1036:Advanced glycation endproduct 2801:(protein→peptide→amino acid) 2475:10.1371/journal.pone.0067008 2274:Pediatric Neurology Part III 1582:Julenius, Karin (May 2007). 1353:10.1016/j.coviro.2015.02.002 1292:Journal of Proteome Research 1217:Introduction to Glycobiology 1172:10.1016/j.copbio.2011.03.002 528:sugar is added to the first 267:human immunodeficiency virus 2408:10.1016/j.yexcr.2017.08.014 1341:Current Opinion in Virology 776:or remove some part of the 663:Non-enzymatic glycosylation 641:synthetic organic chemistry 460:Phosphoserine glycosylation 305:—the site of glycan linkage 74:rough endoplasmic reticulum 37:is the reaction in which a 3252: 3186:Phospagen system (ATP-PCr) 2656:Primary nutritional groups 2568:10.1016/j.jaut.2014.12.002 2504:Essentials of Glycobiology 2396:Experimental Cell Research 2362:10.1016/j.ajhg.2015.12.007 2241:10.1016/j.bbrc.2014.05.115 1410:10.1038/s41557-021-00646-w 1126:Essentials of Glycobiology 1000:next-generation sequencing 430: 386: 25: 18: 3048: 3020:Anoxygenic photosynthesis 3010: 2974: 2942:Pentose phosphate pathway 2937: 2920: 2903: 2697:Oxidative phosphorylation 2319:Rev Inst Nal Enf Resp Mex 969:Rheumatoid Arthritis (RA) 3040:Entner-Doudoroff pathway 2702:electron transport chain 2689:Pyruvate decarboxylation 2073:10.18097/pbmc20105602168 2060:Biomeditsinskaya Khimiya 1917:10.1021/acs.jafc.6b00472 843:Streptococcus pneumoniae 834:-Acetylgalactosaminidase 803:Streptococcus pneumoniae 789:Arthrobacter ureafaciens 785:α2-3,6,8,9-Neuraminidase 735:diabetes mellitus type 2 487:Dictyostelium discoideum 19:Not to be confused with 3134:Sphingolipid metabolism 3035:DeLey-Doudoroff pathway 2883:carbohydrate catabolism 2878:Carbohydrate metabolism 2864:Purine nucleotide cycle 2556:Journal of Autoimmunity 1725:Yoshimura (June 1992). 1693:10.1074/jbc.M111.219766 1531:10.1126/science.1180512 1257:10.1126/science.1235681 949:, disorders of protein 936:Congenital alterations: 679:attachment between the 655:. Generally, the α- or 606:erythropoietin receptor 564:-mannosylation, type I 3226:Carbohydrate chemistry 3103:Fatty acid degradation 2823:Amino acid degradation 1202:Biotecnologia Aplicada 1194:"Transgenic plants of 1045:Chemical glycosylation 1016:human interferon gamma 913:O-linked glycosylation 909:N-linked glycosylation 884:process in equivalent 821:-Acetylglucosaminidase 692:Amadori rearrangements 635:Chemical glycosylation 521: 433:O-linked glycosylation 389:N-linked glycosylation 336:Glycosylation, unlike 290:Glycoprotein diversity 238:sugar-binding proteins 28:Chemical glycosylation 3139:Eicosanoid metabolism 3095:Fatty acid metabolism 2859:Pyrimidine metabolism 2718:Anaerobic respiration 1601:10.1093/glycob/cwm050 957:Acquired alterations: 901:endoplasmic reticulum 610:endoplasmic reticulum 598:endoplasmic reticulum 519: 448:, but also occurs in 427:-linked glycosylation 412:, but very rarely in 383:-linked glycosylation 364:endoplasmic reticulum 246:monoclonal antibodies 197:attached to a target 114:-linked glycosylation 53:) in order to form a 3113:Fatty acid synthesis 2818:Amino acid synthesis 1947:. pp. 405–411. 1872:10.1021/jacs.5b08436 961:autoimmune illnesses 897:glycosyltransferases 882:cell differentiation 764:There are different 594:Trombospondin type 1 398:extracellular matrix 254:glycosyltransferases 2677:Aerobic respiration 2522:GlyProt: In-silico 2466:2013PLoSO...867008C 2022:10.3390/biom9120888 1686:(20): 17585–17592. 1642:10.7554/eLife.52978 1523:2010Sci...327...88Y 1402:2021NatCh..13..480A 987:Alzheimer's disease 920:consensus sequences 492:Leishmania mexicana 80:and nucleus as the 3181:Ethanol metabolism 3129:Steroid metabolism 2854:Nucleotide salvage 2786:Protein metabolism 1970:J. Sci. Food Agric 1823:10.1039/c5sc00280j 1474:Flynne WG (2008). 1063:Glycorandomization 840:-glycosidase from 799:β1,4-Galactosidase 700:Maillard reactions 602:cytokine receptors 566:cytokine receptors 522: 309:Glycan composition 118:dolichol phosphate 3216:Organic reactions 3198: 3197: 3194: 3193: 3157: 3156: 3070: 3069: 3066: 3065: 3053:Xylose metabolism 2999: 2998: 2872: 2871: 2849:Purine metabolism 2794:Protein synthesis 2771: 2770: 2693:Citric acid cycle 2651:Metabolic network 2646:Metabolic pathway 1982:10.1002/jsfa.4022 1976:(11): 1837–1845. 1954:978-0-12-378631-9 1911:(14): 2953–2961. 1780:10.1021/ar100035r 1487:978-1-60456-067-1 1304:10.1021/pr401162k 1251:(6166): 1235681. 1226:978-0-19-928278-4 1196:Nicotiana tabacum 1136:978-0-87969-770-9 977:Alagille syndrome 498:Trypanosoma cruzi 51:glycosyl acceptor 3243: 3169:Metal metabolism 3091: 3076:Lipid metabolism 3008: 2901: 2894: 2806: 2782: 2708: 2673: 2617: 2610: 2603: 2594: 2589: 2579: 2518: 2497: 2487: 2477: 2428: 2427: 2390: 2384: 2383: 2373: 2341: 2335: 2334: 2332: 2330: 2310: 2304: 2303: 2269: 2263: 2262: 2252: 2220: 2209: 2208: 2206: 2204: 2159: 2153: 2152: 2150: 2148: 2105: 2094: 2093: 2075: 2051: 2045: 2044: 2034: 2024: 2000: 1994: 1993: 1965: 1959: 1958: 1940: 1929: 1928: 1900: 1894: 1893: 1883: 1851: 1845: 1844: 1834: 1817:(5): 2687–2704. 1811:Chemical Science 1798: 1792: 1791: 1763: 1757: 1756: 1746: 1737:(16): 11619–25. 1722: 1716: 1715: 1705: 1695: 1671: 1665: 1664: 1654: 1644: 1620: 1614: 1613: 1603: 1579: 1568: 1567: 1559: 1553: 1552: 1542: 1498: 1492: 1491: 1471: 1465: 1464: 1449:Walsh C (2006). 1446: 1440: 1439: 1429: 1390:Nature Chemistry 1381: 1375: 1374: 1364: 1332: 1326: 1325: 1315: 1283: 1277: 1276: 1240: 1231: 1230: 1212: 1206: 1205: 1190: 1184: 1183: 1155: 1149: 1148: 1120: 1107: 1106: 1080: 1041: 878:Notch signalling 608:remained in the 495:, and xylose in 400:attachment. The 349:nucleotide sugar 315:Glycan structure 275:cell trafficking 211:oligosaccharides 3251: 3250: 3246: 3245: 3244: 3242: 3241: 3240: 3201: 3200: 3199: 3190: 3174:Iron metabolism 3153: 3117: 3078: 3062: 3044: 3030:Carbon fixation 2995: 2970: 2933: 2916: 2912:Gluconeogenesis 2885: 2880: 2868: 2840: 2833: 2804: 2777: 2767: 2728: 2712: 2700: 2667: 2660: 2634: 2621: 2549: 2515: 2500: 2443: 2437: 2432: 2431: 2392: 2391: 2387: 2343: 2342: 2338: 2328: 2326: 2312: 2311: 2307: 2292: 2271: 2270: 2266: 2222: 2221: 2212: 2202: 2200: 2190: 2161: 2160: 2156: 2146: 2144: 2126:10.1038/nrm1228 2120:(10): 786–797. 2107: 2106: 2097: 2053: 2052: 2048: 2002: 2001: 1997: 1967: 1966: 1962: 1955: 1942: 1941: 1932: 1902: 1901: 1897: 1853: 1852: 1848: 1800: 1799: 1795: 1765: 1764: 1760: 1724: 1723: 1719: 1673: 1672: 1668: 1622: 1621: 1617: 1581: 1580: 1571: 1561: 1560: 1556: 1517:(5961): 88–92. 1500: 1499: 1495: 1488: 1473: 1472: 1468: 1461: 1448: 1447: 1443: 1383: 1382: 1378: 1334: 1333: 1329: 1285: 1284: 1280: 1242: 1241: 1234: 1227: 1214: 1213: 1209: 1192: 1191: 1187: 1157: 1156: 1152: 1137: 1122: 1121: 1110: 1103: 1082: 1081: 1077: 1072: 1039: 1032: 1018:, expressed in 1012:biotherapeutics 1008: 928: 905:Golgi apparatus 899:located in the 890:embryonic death 886:precursor cells 875: 762: 760:Deglycosylation 727: 665: 637: 618: 588:, secreted and 558:Thrombospondins 514: 462: 446:Golgi apparatus 435: 429: 391: 385: 377: 368:Golgi apparatus 366:, cisternae in 330: 303:Glycosidic bond 292: 250:ABO blood group 187: 30: 24: 17: 12: 11: 5: 3249: 3247: 3239: 3238: 3233: 3228: 3223: 3218: 3213: 3203: 3202: 3196: 3195: 3192: 3191: 3189: 3188: 3183: 3178: 3177: 3176: 3165: 3163: 3159: 3158: 3155: 3154: 3152: 3151: 3146: 3141: 3136: 3131: 3125: 3123: 3119: 3118: 3116: 3115: 3110: 3107:Beta oxidation 3099: 3097: 3088: 3072: 3071: 3068: 3067: 3064: 3063: 3061: 3060: 3055: 3049: 3046: 3045: 3043: 3042: 3037: 3032: 3027: 3025:Chemosynthesis 3022: 3017: 3015:Photosynthesis 3011: 3005: 3001: 3000: 2997: 2996: 2994: 2993: 2992: 2991: 2986: 2975: 2972: 2971: 2969: 2968: 2967: 2966: 2964:Leloir pathway 2956: 2955: 2954: 2952:Polyol pathway 2944: 2938: 2935: 2934: 2932: 2931: 2925:Glycogenolysis 2921: 2918: 2917: 2915: 2914: 2904: 2898: 2891: 2874: 2873: 2870: 2869: 2867: 2866: 2861: 2856: 2851: 2845: 2843: 2835: 2834: 2832: 2831: 2826: 2820: 2814: 2812: 2803: 2802: 2796: 2790: 2788: 2779: 2773: 2772: 2769: 2768: 2766: 2765: 2764: 2763: 2758: 2753: 2738: 2736: 2730: 2729: 2727: 2726: 2722: 2720: 2714: 2713: 2711: 2710: 2681: 2679: 2670: 2662: 2661: 2659: 2658: 2653: 2648: 2642: 2640: 2636: 2635: 2622: 2620: 2619: 2612: 2605: 2597: 2591: 2590: 2547: 2542: 2537: 2528: 2519: 2513: 2498: 2436: 2435:External links 2433: 2430: 2429: 2385: 2336: 2305: 2290: 2264: 2210: 2188: 2154: 2095: 2066:(2): 168–178. 2062:(in Russian). 2046: 1995: 1960: 1953: 1930: 1895: 1866:(9): 3002–11. 1846: 1793: 1774:(8): 1144–53. 1758: 1717: 1666: 1615: 1594:(8): 868–876. 1569: 1554: 1493: 1486: 1466: 1460:978-0974707730 1459: 1441: 1396:(5): 480–487. 1376: 1327: 1298:(3): 1702–12. 1278: 1232: 1225: 1207: 1185: 1150: 1135: 1108: 1101: 1074: 1073: 1071: 1068: 1067: 1066: 1060: 1054: 1048: 1042: 1031: 1028: 1024:ovarian cancer 1007: 1004: 995: 994: 980: 954: 947:-glycosylation 927: 924: 874: 871: 870: 869: 859: 824: 814: 796: 768:to remove the 761: 758: 726: 723: 681:carbonil group 664: 661: 636: 633: 617: 614: 513: 512:-mannosylation 507: 461: 458: 431:Main article: 428: 422: 387:Main article: 384: 378: 376: 373: 372: 371: 352: 345: 329: 326: 325: 324: 318: 312: 306: 291: 288: 213:linked at the 186: 183: 182: 181: 175: 161: 158: 151:hydroxyproline 121: 55:glycoconjugate 47:glycosyl donor 15: 13: 10: 9: 6: 4: 3: 2: 3248: 3237: 3234: 3232: 3229: 3227: 3224: 3222: 3221:Carbohydrates 3219: 3217: 3214: 3212: 3209: 3208: 3206: 3187: 3184: 3182: 3179: 3175: 3172: 3171: 3170: 3167: 3166: 3164: 3160: 3150: 3147: 3145: 3142: 3140: 3137: 3135: 3132: 3130: 3127: 3126: 3124: 3120: 3114: 3111: 3108: 3104: 3101: 3100: 3098: 3096: 3092: 3089: 3086: 3082: 3077: 3073: 3059: 3058:Radiotrophism 3056: 3054: 3051: 3050: 3047: 3041: 3038: 3036: 3033: 3031: 3028: 3026: 3023: 3021: 3018: 3016: 3013: 3012: 3009: 3006: 3002: 2990: 2987: 2985: 2982: 2981: 2980: 2979:Glycosylation 2977: 2976: 2973: 2965: 2962: 2961: 2960: 2957: 2953: 2950: 2949: 2948: 2945: 2943: 2940: 2939: 2936: 2930: 2926: 2923: 2922: 2919: 2913: 2909: 2906: 2905: 2902: 2899: 2895: 2892: 2889: 2884: 2879: 2875: 2865: 2862: 2860: 2857: 2855: 2852: 2850: 2847: 2846: 2844: 2842: 2836: 2830: 2827: 2824: 2821: 2819: 2816: 2815: 2813: 2811: 2807: 2800: 2797: 2795: 2792: 2791: 2789: 2787: 2783: 2780: 2774: 2762: 2759: 2757: 2754: 2752: 2749: 2748: 2747: 2743: 2740: 2739: 2737: 2735: 2731: 2724: 2723: 2721: 2719: 2715: 2707: 2703: 2698: 2694: 2690: 2686: 2683: 2682: 2680: 2678: 2674: 2671: 2669: 2663: 2657: 2654: 2652: 2649: 2647: 2644: 2643: 2641: 2637: 2633: 2629: 2625: 2618: 2613: 2611: 2606: 2604: 2599: 2598: 2595: 2587: 2583: 2578: 2573: 2569: 2565: 2561: 2557: 2553: 2548: 2546: 2543: 2541: 2538: 2536: 2534: 2529: 2527: 2525: 2520: 2516: 2514:0-87969-559-5 2510: 2506: 2505: 2499: 2495: 2491: 2486: 2481: 2476: 2471: 2467: 2463: 2460:(6): e67008. 2459: 2455: 2451: 2449: 2442: 2439: 2438: 2434: 2425: 2421: 2417: 2413: 2409: 2405: 2401: 2397: 2389: 2386: 2381: 2377: 2372: 2367: 2363: 2359: 2356:(2): 339–46. 2355: 2351: 2347: 2340: 2337: 2324: 2320: 2316: 2309: 2306: 2301: 2297: 2293: 2291:9780444595652 2287: 2283: 2279: 2275: 2268: 2265: 2260: 2256: 2251: 2246: 2242: 2238: 2235:(2): 235–42. 2234: 2230: 2226: 2219: 2217: 2215: 2211: 2199: 2195: 2191: 2189:9780123809148 2185: 2181: 2177: 2173: 2169: 2165: 2158: 2155: 2143: 2139: 2135: 2131: 2127: 2123: 2119: 2115: 2111: 2104: 2102: 2100: 2096: 2091: 2087: 2083: 2079: 2074: 2069: 2065: 2061: 2057: 2050: 2047: 2042: 2038: 2033: 2028: 2023: 2018: 2014: 2010: 2006: 1999: 1996: 1991: 1987: 1983: 1979: 1975: 1971: 1964: 1961: 1956: 1950: 1946: 1939: 1937: 1935: 1931: 1926: 1922: 1918: 1914: 1910: 1906: 1899: 1896: 1891: 1887: 1882: 1877: 1873: 1869: 1865: 1861: 1857: 1850: 1847: 1842: 1838: 1833: 1828: 1824: 1820: 1816: 1812: 1808: 1806: 1797: 1794: 1789: 1785: 1781: 1777: 1773: 1769: 1762: 1759: 1754: 1750: 1745: 1740: 1736: 1732: 1728: 1721: 1718: 1713: 1709: 1704: 1699: 1694: 1689: 1685: 1681: 1677: 1670: 1667: 1662: 1658: 1653: 1648: 1643: 1638: 1634: 1630: 1626: 1619: 1616: 1611: 1607: 1602: 1597: 1593: 1589: 1585: 1578: 1576: 1574: 1570: 1565: 1558: 1555: 1550: 1546: 1541: 1536: 1532: 1528: 1524: 1520: 1516: 1512: 1508: 1506: 1497: 1494: 1489: 1483: 1479: 1478: 1470: 1467: 1462: 1456: 1452: 1445: 1442: 1437: 1433: 1428: 1423: 1419: 1415: 1411: 1407: 1403: 1399: 1395: 1391: 1387: 1380: 1377: 1372: 1368: 1363: 1358: 1354: 1350: 1346: 1342: 1338: 1331: 1328: 1323: 1319: 1314: 1309: 1305: 1301: 1297: 1293: 1289: 1282: 1279: 1274: 1270: 1266: 1262: 1258: 1254: 1250: 1246: 1239: 1237: 1233: 1228: 1222: 1218: 1211: 1208: 1203: 1199: 1197: 1189: 1186: 1181: 1177: 1173: 1169: 1166:(6): 858–67. 1165: 1161: 1154: 1151: 1146: 1142: 1138: 1132: 1128: 1127: 1119: 1117: 1115: 1113: 1109: 1104: 1102:9780123786319 1098: 1094: 1090: 1086: 1079: 1076: 1069: 1064: 1061: 1058: 1055: 1052: 1049: 1046: 1043: 1037: 1034: 1033: 1029: 1027: 1025: 1021: 1017: 1013: 1005: 1003: 1001: 992: 988: 984: 981: 978: 974: 970: 966: 962: 958: 955: 952: 948: 946: 941: 937: 934: 933: 932: 925: 923: 921: 916: 914: 910: 906: 902: 898: 893: 891: 887: 883: 879: 872: 867: 863: 860: 857: 853: 849: 845: 844: 839: 835: 833: 829: 825: 822: 820: 815: 812: 811:glycoproteins 808: 804: 800: 797: 794: 790: 786: 783: 782: 781: 779: 775: 771: 767: 759: 757: 755: 751: 746: 744: 743:renal failure 740: 736: 731: 724: 722: 720: 716: 711: 709: 705: 704:crosslinkings 701: 697: 693: 688: 686: 682: 678: 674: 670: 662: 660: 658: 654: 650: 646: 642: 634: 632: 630: 626: 622: 615: 613: 611: 607: 603: 599: 595: 591: 590:transmembrane 587: 583: 579: 575: 571: 567: 563: 559: 555: 552: 548: 544: 539: 538:alpha-mannose 535: 531: 527: 518: 511: 508: 506: 504: 500: 499: 494: 493: 489:, mannose in 488: 484: 481: 480:phosphoserine 478: 474: 470: 466: 459: 457: 455: 451: 447: 443: 439: 434: 426: 423: 421: 419: 415: 411: 407: 403: 399: 395: 390: 382: 379: 374: 369: 365: 361: 357: 356:transcription 353: 350: 346: 343: 339: 335: 334: 333: 327: 322: 321:Glycan length 319: 316: 313: 310: 307: 304: 301: 300: 299: 297: 289: 287: 284: 282: 281: 276: 270: 268: 263: 259: 255: 251: 247: 243: 239: 235: 234:immune system 231: 227: 223: 219: 216: 212: 208: 204: 200: 199:macromolecule 196: 192: 184: 179: 176: 173: 169: 165: 162: 159: 156: 152: 148: 147:hydroxylysine 144: 140: 136: 132: 129: 125: 122: 119: 115: 113: 108: 105: 101: 97: 93: 90: 89: 88: 86: 84: 79: 75: 71: 66: 64: 60: 59:glycosylation 56: 52: 48: 44: 40: 36: 35:Glycosylation 32: 29: 22: 3231:Biochemistry 2978: 2959:Galactolysis 2929:Glycogenesis 2734:Fermentation 2706:ATP synthase 2559: 2555: 2532: 2523: 2503: 2457: 2453: 2447: 2402:(1): 20–29. 2399: 2395: 2388: 2353: 2349: 2339: 2327:. Retrieved 2322: 2318: 2308: 2273: 2267: 2232: 2228: 2201:. Retrieved 2171: 2167: 2157: 2145:. Retrieved 2117: 2113: 2063: 2059: 2049: 2012: 2009:Biomolecules 2008: 1998: 1973: 1969: 1963: 1944: 1908: 1904: 1898: 1863: 1859: 1849: 1814: 1810: 1804: 1796: 1771: 1767: 1761: 1734: 1730: 1720: 1683: 1679: 1669: 1632: 1628: 1618: 1591: 1588:Glycobiology 1587: 1563: 1557: 1514: 1510: 1504: 1496: 1476: 1469: 1450: 1444: 1393: 1389: 1379: 1344: 1340: 1330: 1295: 1291: 1281: 1248: 1244: 1216: 1210: 1201: 1195: 1188: 1163: 1159: 1153: 1125: 1084: 1078: 1051:Fucosylation 1026:cell lines. 1020:HEK 293 1009: 996: 982: 956: 950: 944: 935: 929: 917: 894: 876: 847: 841: 837: 831: 827: 818: 793:sialic acids 763: 747: 732: 728: 725:Role of AGEs 712: 689: 666: 656: 652: 648: 644: 638: 619: 569: 561: 556: 523: 509: 503:Mus musculus 502: 496: 490: 486: 463: 437: 436: 424: 417: 401: 393: 392: 380: 331: 293: 285: 280:Helicobacter 278: 271: 229: 226:glycoprotein 201:, typically 191:carbohydrate 188: 170:side-chain. 163: 123: 111: 91: 82: 67: 58: 39:carbohydrate 34: 33: 31: 3085:lipogenesis 2947:Fructolysis 2761:Lactic acid 2517:. NBK20709. 2174:: 131–164. 2015:(12): 888. 1680:J Biol Chem 846:): removes 698:reactions, 696:Schiff base 629:prenylation 360:translation 358:or protein 220:of certain 107:side-chains 45:'), i.e. a 3205:Categories 2908:Glycolysis 2841:metabolism 2839:Nucleotide 2829:Urea cycle 2810:Amino acid 2799:Catabolism 2742:Glycolysis 2685:Glycolysis 2668:metabolism 2628:catabolism 2624:Metabolism 2329:2 November 2203:2 November 2147:1 November 1070:References 866:asparagine 864:: cleaves 685:side chain 625:GPI anchor 621:Glypiation 543:amino acid 530:tryptophan 442:eukaryotes 406:eukaryotes 328:Mechanisms 222:asparagine 195:covalently 178:Glypiation 168:tryptophan 100:asparagine 26:See also: 3081:lipolysis 2888:anabolism 2632:anabolism 2448:In silico 2082:2310-6905 1418:1755-4349 1273:206548002 1057:Glycation 973:mutations 856:threonine 807:galactose 772:from the 739:cataracts 669:glycation 338:glycation 139:threonine 78:cytoplasm 63:glycation 21:Glycation 3004:Nonhuman 2989:O-linked 2984:N-linked 2776:Specific 2586:25578468 2562:: 1–13. 2494:23840574 2454:PLOS ONE 2424:12800448 2416:28803068 2380:26805780 2300:23622397 2259:24909690 2198:20816394 2142:22917106 2134:14570055 2090:21341505 2041:31861217 1990:20549652 1925:27018258 1890:26878147 1841:26078847 1788:20496888 1712:21454577 1661:31868591 1610:17494086 1549:20044576 1436:33723379 1371:25747313 1347:: 63–9. 1322:24467287 1265:24385630 1180:21420850 1145:20301239 1030:See also 991:diabetes 938:Over 40 926:Clinical 903:and the 862:PNGase F 774:proteins 750:hormones 715:collagen 710:(AGEs). 677:covalent 586:proteins 578:nitrogen 534:C-C bond 454:bacteria 414:bacteria 296:proteome 262:zoonotic 258:antigens 218:nitrogen 203:proteins 155:ceramide 143:tyrosine 128:hydroxyl 104:arginine 96:nitrogen 3144:Ketosis 2756:Ethanol 2639:General 2577:4340844 2485:3695939 2462:Bibcode 2441:GlycoEP 2371:4746335 2325:: 39–47 2250:4254162 2032:6995512 1881:5078750 1832:4465199 1753:1317872 1703:3093833 1652:6954052 1540:2978000 1519:Bibcode 1511:Science 1427:8102341 1398:Bibcode 1362:4827424 1313:4428802 1245:Science 1204:. 2013. 780:chain. 770:glycans 766:enzymes 756:level. 526:mannose 483:glycans 473:mannose 450:archaea 444:in the 410:archaea 242:lectins 240:called 185:Purpose 85:-GlcNAc 2666:Energy 2584:  2574:  2511:  2492:  2482:  2422:  2414:  2378:  2368:  2298:  2288:  2257:  2247:  2196:  2186:  2140:  2132:  2088:  2080:  2039:  2029:  1988:  1951:  1923:  1888:  1878:  1839:  1829:  1786:  1751:  1710:  1700:  1659:  1649:  1608:  1547:  1537:  1484:  1457:  1434:  1424:  1416:  1369:  1359:  1320:  1310:  1271:  1263:  1223:  1178:  1143:  1133:  1099:  965:cancer 852:serine 801:(from 787:(from 719:lysine 582:oxygen 574:carbon 477:GlcNAc 475:, and 469:fucose 465:Xylose 236:) via 207:lipids 135:serine 131:oxygen 43:glycan 3162:Other 3122:Other 2897:Human 2778:paths 2420:S2CID 2138:S2CID 1629:eLife 1269:S2CID 854:- or 778:sugar 653:trans 375:Types 215:amide 172:Aloin 149:, or 41:(or ' 2886:and 2582:PMID 2509:ISBN 2490:PMID 2412:PMID 2376:PMID 2331:2020 2296:PMID 2286:ISBN 2255:PMID 2205:2020 2194:PMID 2184:ISBN 2149:2020 2130:PMID 2086:PMID 2078:ISSN 2037:PMID 1986:PMID 1949:ISBN 1921:PMID 1886:PMID 1837:PMID 1784:PMID 1749:PMID 1708:PMID 1657:PMID 1606:PMID 1545:PMID 1482:ISBN 1455:ISBN 1432:PMID 1414:ISSN 1367:PMID 1318:PMID 1261:PMID 1221:ISBN 1176:PMID 1141:PMID 1131:ISBN 1097:ISBN 989:and 911:and 828:endo 452:and 205:and 2910:⇄ 2751:ABE 2572:PMC 2564:doi 2480:PMC 2470:doi 2404:doi 2400:359 2366:PMC 2358:doi 2278:doi 2245:PMC 2237:doi 2233:453 2176:doi 2122:doi 2068:doi 2027:PMC 2017:doi 1978:doi 1913:doi 1876:PMC 1868:doi 1864:138 1827:PMC 1819:doi 1805:cis 1776:doi 1739:doi 1735:267 1698:PMC 1688:doi 1684:286 1647:PMC 1637:doi 1596:doi 1535:PMC 1527:doi 1515:327 1422:PMC 1406:doi 1357:PMC 1349:doi 1308:PMC 1300:doi 1253:doi 1249:343 1168:doi 1089:doi 963:or 830:-α- 754:DNA 657:cis 649:cis 631:.) 580:or 551:Gly 547:Ala 193:is 133:of 102:or 98:of 3207:: 3083:, 2927:⇄ 2744:→ 2704:+ 2695:→ 2691:→ 2687:→ 2630:, 2626:, 2580:. 2570:. 2560:57 2558:. 2554:. 2488:. 2478:. 2468:. 2456:. 2452:. 2418:. 2410:. 2398:. 2374:. 2364:. 2354:98 2352:. 2348:. 2323:15 2321:. 2317:. 2294:. 2284:. 2253:. 2243:. 2231:. 2227:. 2213:^ 2192:. 2182:. 2172:92 2170:. 2166:. 2136:. 2128:. 2116:. 2112:. 2098:^ 2084:. 2076:. 2064:56 2035:. 2025:. 2011:. 2007:. 1984:. 1974:90 1972:. 1933:^ 1919:. 1909:64 1907:. 1884:. 1874:. 1862:. 1858:. 1835:. 1825:. 1813:. 1809:. 1782:. 1772:43 1770:. 1747:. 1733:. 1729:. 1706:. 1696:. 1682:. 1678:. 1655:. 1645:. 1635:. 1631:. 1627:. 1604:. 1592:17 1590:. 1586:. 1572:^ 1543:. 1533:. 1525:. 1513:. 1509:. 1430:. 1420:. 1412:. 1404:. 1394:13 1392:. 1388:. 1365:. 1355:. 1345:11 1339:. 1316:. 1306:. 1296:13 1294:. 1290:. 1267:. 1259:. 1247:. 1235:^ 1200:. 1174:. 1164:22 1162:. 1139:. 1111:^ 1095:. 817:β- 741:, 702:, 694:, 604:, 568:. 549:, 524:A 471:, 467:, 456:. 269:. 145:, 141:, 137:, 109:. 3109:) 3105:( 3087:) 3079:( 2890:) 2881:( 2709:) 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Index

Glycation
Chemical glycosylation
carbohydrate
glycan
glycosyl donor
glycosyl acceptor
glycoconjugate
glycation
post-translational modification
rough endoplasmic reticulum
cytoplasm
O-GlcNAc
nitrogen
asparagine
arginine
side-chains
N-linked glycosylation
dolichol phosphate
hydroxyl
oxygen
serine
threonine
tyrosine
hydroxylysine
hydroxyproline
ceramide
tryptophan
Aloin
Glypiation
carbohydrate

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